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Conserved domains on  [gi|1973708721|ref|XP_039159797|]
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uncharacterized protein LOC104421554 [Eucalyptus grandis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 500-1072 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


:

Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 592.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  500 HWAAKeiTQNKTLYTWINEEGAVVCQRTYAELDSNASCIAHKLLTSRKPtikpGDRVLLVHVPGLDFVDSFFGCLRAKVV 579
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  580 PVPVLPPdplqRGGQALTKIENIAKLCNAVAILSTVGYHSAVRAgsvknlisftrkSAESTAQWPNLPWLHTDswikssk 659
Cdd:cd05931     75 AVPLPPP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRA------------FAASRPAAGTPRLLVVD------- 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  660 vLPASNIGSQSES---QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 736
Cdd:cd05931    132 -LLPDTSAADWPPpspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMVCGGTAILFSPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKT 815
Cdd:cd05931    211 TPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVrDEDLE---GLDLSSWRVALNGAEPVRPAT 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  816 LKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKPILV-------------------DWQGRICCGYVDPndaDV 876
Cdd:cd05931    288 LRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 DIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKfPGRKYTRTGDLGRVIQGNLFITGRIKDLI 956
Cdd:cd05931    365 EVRIVDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLI 442

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  957 IVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDG--KPVDKDIIKQIESRV 1034
Cdd:cd05931    443 IVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVERGadPADLAAIAAAIRAAV 509

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1973708721 1035 AEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1072
Cdd:cd05931    510 AREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
catalase_like super family cl09506
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 1722-2052 6.34e-126

Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.


The actual alignment was detected with superfamily member cd08151:

Pssm-ID: 471888  Cd Length: 328  Bit Score: 399.88  E-value: 6.34e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1722 EEMDSRYKRIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHNIFGPGKKYTVIVRHSNSLSADDDARL 1801
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1802 DARGAALRILSDEKGDDSPLlDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSYAEMH 1879
Cdd:cd08151     80 DGRGAALRFLNAGDDDAGPL-DLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1880 YYSNICRLFRFKDGQEMYVKFKLRPSDKNIGEDTGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFQNRVKSPnGVRYI 1959
Cdd:cd08151    159 YYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1960 FQLQVMPVPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSERLEFNPfLRCHEVDVIRATSSSQ-SASIDH 2038
Cdd:cd08151    238 LQIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGH 314

                          330
                   ....*....|....
gi 1973708721 2039 GRSLVYEICQHLRN 2052
Cdd:cd08151    315 LRSLVYEISQRLRK 328
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1246-1704 1.86e-26

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


The actual alignment was detected with superfamily member TIGR02353:

Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 117.93  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1246 LVFPAYLSVSAFQILVVASqklidGLPWLHHTsvvlLAPLFWILCIALTSISIAFFGNSFLRINYA------LTPEV-SV 1318
Cdd:TIGR02353    5 LQLIPIVTLSGLQWLAPLL-----GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1319 WSVDFVKWWALYKAQEVSSKVLavhLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHE 1396
Cdd:TIGR02353   76 WGSTYLRFWTVKRLVDAAPTVL---LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1397 VRNSVLRFQPIRIGRNCSVGPYAVIQKGSVLGEGAEVLALQKSEGGKSVlkmtKAENILKVSPGslKETIQQFMGIYMVG 1476
Cdd:TIGR02353  151 AERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSI----PDGERWHGSPA--QKTGADYRKVQPAR 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1477 LVSSLSATAVFLLymrLSQKVPSLEQLAFLCISGAlhwvpFTIVAYATMFTNTLPNPFEFAISLATAYFAHGLVLSLLTS 1556
Cdd:TIGR02353  225 PYTVRRRLYVAGA---LFVVFVLLPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1557 IFTNLLAS---KEKKTQTHikTWLGHRL----AVACHLRFAKLLSG-TEAFCMYLHLLGAKVGKYCSIRSINpVADPRMV 1628
Cdd:TIGR02353  297 AAVRLLLNlvlKPGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLT 373

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1629 SIGAGVHLGDfsRIMTGFYSQSGYI--QSNVHVKDNSVIGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1704
Cdd:TIGR02353  374 DIGEETFIAD--GLLMGNARLSGGWfrLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 5.33e-17

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 77.19  E-value: 5.33e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN super family cl34196
Monoamine oxidase [Amino acid transport and metabolism];
19-270 9.45e-15

Monoamine oxidase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG1231:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 79.19  E-value: 9.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTQ 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 LEEM-DLHKLALIDsLTGEYHDIN-VAEDYMSLVSLTLDIQDKAKDTNRIGIHAVSEIasDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSARR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMNLWKKISESLLIKVCCNTEVQAVRRNGSGVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234

                          250       260
                   ....*....|....*....|....*
gi 1973708721  246 DITNssGETEHkeFDKIIIsgAFPF 270
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV--TVPP 253
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1125-1186 7.26e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


:

Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.80  E-value: 7.26e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1125 EFLKQLVSEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1186
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 500-1072 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 592.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  500 HWAAKeiTQNKTLYTWINEEGAVVCQRTYAELDSNASCIAHKLLTSRKPtikpGDRVLLVHVPGLDFVDSFFGCLRAKVV 579
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  580 PVPVLPPdplqRGGQALTKIENIAKLCNAVAILSTVGYHSAVRAgsvknlisftrkSAESTAQWPNLPWLHTDswikssk 659
Cdd:cd05931     75 AVPLPPP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRA------------FAASRPAAGTPRLLVVD------- 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  660 vLPASNIGSQSES---QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 736
Cdd:cd05931    132 -LLPDTSAADWPPpspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMVCGGTAILFSPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKT 815
Cdd:cd05931    211 TPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVrDEDLE---GLDLSSWRVALNGAEPVRPAT 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  816 LKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKPILV-------------------DWQGRICCGYVDPndaDV 876
Cdd:cd05931    288 LRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 DIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKfPGRKYTRTGDLGRVIQGNLFITGRIKDLI 956
Cdd:cd05931    365 EVRIVDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLI 442

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  957 IVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDG--KPVDKDIIKQIESRV 1034
Cdd:cd05931    443 IVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVERGadPADLAAIAAAIRAAV 509

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1973708721 1035 AEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1072
Cdd:cd05931    510 AREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1722-2052 6.34e-126

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


Pssm-ID: 163707  Cd Length: 328  Bit Score: 399.88  E-value: 6.34e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1722 EEMDSRYKRIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHNIFGPGKKYTVIVRHSNSLSADDDARL 1801
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1802 DARGAALRILSDEKGDDSPLlDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSYAEMH 1879
Cdd:cd08151     80 DGRGAALRFLNAGDDDAGPL-DLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1880 YYSNICRLFRFKDGQEMYVKFKLRPSDKNIGEDTGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFQNRVKSPnGVRYI 1959
Cdd:cd08151    159 YYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1960 FQLQVMPVPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSERLEFNPfLRCHEVDVIRATSSSQ-SASIDH 2038
Cdd:cd08151    238 LQIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGH 314

                          330
                   ....*....|....
gi 1973708721 2039 GRSLVYEICQHLRN 2052
Cdd:cd08151    315 LRSLVYEISQRLRK 328
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 486-1080 3.13e-94

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 320.14  E-value: 3.13e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  486 IVFPDLPNLDSYLKHWAakEITQNKTLYTWIN---EEGAVVCQRTYAELDSNASCIAHKLltsrKPTIKPGDRVLLVHVP 562
Cdd:PRK07769    15 IRFPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  563 GLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHSAVRAgsvknlisFTRKsaESTAQ 642
Cdd:PRK07769    89 NLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDD----CTPSAILTTTDSAEGVRK--------FFRA--RPAKE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  643 WPNLpwLHTDSwiksskvLPASnIGS---QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVL 719
Cdd:PRK07769   155 RPRV--IAVDA-------VPDE-VGAtwvPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRG 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  720 VSWLPQYHDMGLIGGLFTAMvCGGTAILFSPLTFIRNPLLWLQTIS----DYKATHSAGPNFAFELVIRRlEADKAKAHD 795
Cdd:PRK07769   225 VSWLPFFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFEHAAAR-GLPKDGEPP 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  796 YDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKP--ILVDWQ----GRIC---- 865
Cdd:PRK07769   303 LDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRFVevpa 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  866 ----------CGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKF-------- 927
Cdd:PRK07769   383 dapnavaqvsAGKVGVSEWAV---IVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaeg 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  928 --PGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDVLSAK-------G 998
Cdd:PRK07769   459 apDDALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVvfddshaG 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  999 ISL-PDASDEvGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGTL 1075
Cdd:PRK07769   539 LKFdPEDTSE-QLVIVAERAPGahKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617

                          650
                   ....*....|.
gi 1973708721 1076 ------NTVPD 1080
Cdd:PRK07769   618 rsgygqPAFPD 628
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 480-1075 3.40e-90

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 308.19  E-value: 3.40e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  480 LSETHGIVFPDLPNLDSYLKHWAakEITQNKTLYTWIN---EEGAVVCQRTYAELDSNASCIAHKLltsrKPTIKPGDRV 556
Cdd:NF038339     6 LDENGNIRFPDGATLVDHVERNA--RERADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  557 LLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHSAVRagsvknliSFTRks 636
Cdd:NF038339    80 AILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEPGHTDRLHAVLGD----CKPSAILTATSSAEGVR--------KFFR-- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  637 AESTAQWPN------LPWLHTDSWIKsskvlPASNIgsqsesqpDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRR 710
Cdd:NF038339   146 SLPAKERPRviavdaVPDSVGSTWVR-----PDADL--------DDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDA 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  711 YRSTSNTVLVSWLPQYHDMGLIGGLFTAMvcGGTAILF-SPLTFIRNPLLW---LQTISDYKATHSAGPNFAFELVIRR- 785
Cdd:NF038339   213 IELDENSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARg 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  786 LEADkakAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKP--ILVDW--- 860
Cdd:NF038339   291 LPKE---GEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReel 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  861 -QGRI--------------CCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQ 925
Cdd:NF038339   368 nAGRIvevdpdapnavaqvSCGYVARSQWAV---IVDPETGTEL-PDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLK 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  926 KF-----------PGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDVL 994
Cdd:NF038339   444 SRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVPANQL 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  995 -------SAKGISL-PDASDEvGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRF 1064
Cdd:NF038339   524 paevfenSHSGLKYdADDSSE-QLVIVAERAPGagKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARR 602

                          650
                   ....*....|.
gi 1973708721 1065 ECLKQFVDGTL 1075
Cdd:NF038339   603 ACKAAYIDGTL 613
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 652-1072 1.75e-84

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 291.17  E-value: 1.75e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  652 DSWIKSSKVLPASNIGSQSESQP-DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMG 730
Cdd:NF040633   177 ESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMG 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 LIGGLFtAMVCGGTAILFSPLTFIRNPLLWLQTIS---DYKATHSAGPNFAFELVIRRleADKAKAHDYDLSSMIFFMIA 807
Cdd:NF040633   257 IILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNFALELAARY--ANPEEGEDLDLSAVDGIIIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  808 AEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKPiLVDWQGR--ICCGYVDPNDADVD-------- 877
Cdd:NF040633   334 SEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERP-LFTYFDReaLAEGRAVEVAEDSEnavpfasn 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  878 --------IRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQK----------FPGRKYTRTGDLG 939
Cdd:NF040633   413 gqvvrpqvLAIVDPETGQEL-PDGTVGEIWVHGDNMAAGYLDREEETAETFRNTLGErlaensraegAPEDNWMATGDLG 491

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  940 RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDG 1019
Cdd:NF040633   492 VIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPGD-------------DVEKLVILAERDDE 558

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721 1020 KPVDKD--IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1072
Cdd:NF040633   559 ADESGDaeAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 521-1077 3.13e-83

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 281.70  E-value: 3.13e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQALT 597
Cdd:COG0318     17 ALVFggrRLTYAELDARARRLAAAL---RALGVGPGDRVALLLPNSPEFVVAFLAALRA---------------GAVVVP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 --------KIENIAKLCNAVAILStvgyhsavragsvknlisftrksaestaqwpnlpwlhtdswiksskvlpasnigsq 669
Cdd:COG0318     79 lnprltaeELAYILEDSGARALVT-------------------------------------------------------- 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 sesqpddlCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFS 749
Cdd:COG0318    103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PltfiRNPLLWLQTISDYKATHSAG-PNFAFELvirrleADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpygl 828
Cdd:COG0318    175 R----FDPERVLELIERERVTVLFGvPTMLARL------LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF----- 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sQEVMAPGYGLAENCVFVGCAygkkkPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIG 908
Cdd:COG0318    240 -GVRIVEGYGLTETSPVVTVN-----PEDPGERRPGSVGRPLPG---VEVRIVDED-GREL-PPGEVGEIVVRGPNVMKG 308

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWGKEELSQKTFRNklqkfpGrkYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVI 987
Cdd:COG0318    309 YWNDPEATAEAFRD------G--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVV 377

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  988 SVPEDVLsakgislpdasDEVGLVVIAeLKDGKPVD-KDIIKQIESRVAeEHGVtvasvklirPRTIS------KTTSGK 1060
Cdd:COG0318    378 GVPDEKW-----------GERVVAFVV-LRPGAELDaEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGK 435

                          570
                   ....*....|....*..
gi 1973708721 1061 IKRFECLKQFVDGTLNT 1077
Cdd:COG0318    436 IDRRALRERYAAGALEA 452
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
527-1070 1.20e-74

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 261.35  E-value: 1.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltSRKPTIkpGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrggqaltkieniaklc 606
Cdd:NF038337    40 TWAQLYRRTLNVAHEV--RRHGTT--GDRAVILAPQGLPYIVAFLGAMQA------------------------------ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTV---GYH----SAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKS--SKVLPASNIGSQSESQPDDL 677
Cdd:NF038337    86 GLIAVPLSVpqpGSHdervSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPAVIEidSLDLDGPNSPSIRISDAPSI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSN------TVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPL 751
Cdd:NF038337   166 AYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPV 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQ 830
Cdd:NF038337   246 AFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTtDADLA---GLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFRE 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMAPGYGLAENCVFVGCAYGKKKPILVDWQ-GRICCGYVDPNDADVD-------------IRIVDADTGLEVdEDGKEG 896
Cdd:NF038337   323 DMMQPSYGLAEATVYVASRAEGGAPEVVHFEpEKLSEGSAQRCEARTGspllsygtptsptVRIVDPDTCIEC-PAGTVG 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  897 EIWISSPSAGIGYWGKEELSQKTFRNKLQK----FPGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTV 972
Cdd:NF038337   402 EIWVHGDNVAEGYWQKPEETRRTFGGVLANpspgTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTV 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  973 ESsselLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELK-----DGKPVDK-DIIK-QIESRVAEEHGVTVASV 1045
Cdd:NF038337   482 QE----ITGGRVAAISVPVD-------------ETEKLVTIIELKkrgdsDEEAMRKlDAVKnNVTAAISRSHGLNVADL 544

                          570       580
                   ....*....|....*....|....*
gi 1973708721 1046 KLIRPRTISKTTSGKIKRFECLKQF 1070
Cdd:NF038337   545 VLVPPGSIPTTTSGKIRRAACVEQY 569
AMP-binding pfam00501
AMP-binding enzyme;
527-959 3.74e-66

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 231.05  E-value: 3.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHkLLTSRKptIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQALT--------K 598
Cdd:pfam00501   23 TYRELDERANRLAA-GLRALG--VGKGDRVAILLPNSPEWVVAFLACLKA---------------GAVYVPlnprlpaeE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  599 IENIAKLCNAVAILSTVGYHSAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKSSKVLPASNIgsqsesQPDDLC 678
Cdd:pfam00501   85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP------DPDDLA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  679 FLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRS----TSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTFi 754
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  755 RNPLLWLQTISDYKATHSAGPNFAFELVirrleADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPyglsqeVMA 834
Cdd:pfam00501  238 LDPAALLELIERYKVTVLYGVPTLLNML-----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALV 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  835 PGYGLAENCVFVGCAYgkkkPILVDWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 914
Cdd:pfam00501  307 NGYGLTETTGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPE 378

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1973708721  915 LSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVA 959
Cdd:pfam00501  379 LTAEAFDED-------GWYRTGDLGRRDEdGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 527-952 2.51e-31

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 128.92  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSRKptIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrGG--------QALT 597
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKA---------------GAayvpldpaYPAE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGYhsavragsvknlisftrksAESTAQWPNLPWLHTDSWIKSSKVLPASNiGSQSESQPDDL 677
Cdd:TIGR01733   63 RLAFILEDAGARLLLTDSAL-------------------ASRLAGLVLPVILLDPLELAALDDAPAPP-PPDAPSGPDDL 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMVCGGTAILFSPLTFIRNP 757
Cdd:TIGR01733  123 AYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  758 LLWLQTISDYKATHSAGPNFAFELVirrleadkAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELtrpygLSQEVMAPGY 837
Cdd:TIGR01733  202 ALLAALIAEHPVTVLNLTPSLLALL--------AAALPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLY 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  838 GLAENCVFVGCAYgkKKPILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQ 917
Cdd:TIGR01733  269 GPTETTVWSTATL--VDPDDAPRESPVPIGRPLAN---TRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTA 341

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1973708721  918 KTFRN--KLQKFPGRKYtRTGDLGRVI-QGNLFITGRI 952
Cdd:TIGR01733  342 ERFVPdpFAGGDGARLY-RTGDLVRYLpDGNLEFLGRI 378
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1246-1704 1.86e-26

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 117.93  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1246 LVFPAYLSVSAFQILVVASqklidGLPWLHHTsvvlLAPLFWILCIALTSISIAFFGNSFLRINYA------LTPEV-SV 1318
Cdd:TIGR02353    5 LQLIPIVTLSGLQWLAPLL-----GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1319 WSVDFVKWWALYKAQEVSSKVLavhLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHE 1396
Cdd:TIGR02353   76 WGSTYLRFWTVKRLVDAAPTVL---LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1397 VRNSVLRFQPIRIGRNCSVGPYAVIQKGSVLGEGAEVLALQKSEGGKSVlkmtKAENILKVSPGslKETIQQFMGIYMVG 1476
Cdd:TIGR02353  151 AERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSI----PDGERWHGSPA--QKTGADYRKVQPAR 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1477 LVSSLSATAVFLLymrLSQKVPSLEQLAFLCISGAlhwvpFTIVAYATMFTNTLPNPFEFAISLATAYFAHGLVLSLLTS 1556
Cdd:TIGR02353  225 PYTVRRRLYVAGA---LFVVFVLLPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1557 IFTNLLAS---KEKKTQTHikTWLGHRL----AVACHLRFAKLLSG-TEAFCMYLHLLGAKVGKYCSIRSINpVADPRMV 1628
Cdd:TIGR02353  297 AAVRLLLNlvlKPGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLT 373

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1629 SIGAGVHLGDfsRIMTGFYSQSGYI--QSNVHVKDNSVIGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1704
Cdd:TIGR02353  374 DIGEETFIAD--GLLMGNARLSGGWfrLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 5.33e-17

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 77.19  E-value: 5.33e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 22-94 2.23e-15

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 81.03  E-value: 2.23e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
19-270 9.45e-15

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 79.19  E-value: 9.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTQ 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 LEEM-DLHKLALIDsLTGEYHDIN-VAEDYMSLVSLTLDIQDKAKDTNRIGIHAVSEIasDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSARR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMNLWKKISESLLIKVCCNTEVQAVRRNGSGVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234

                          250       260
                   ....*....|....*....|....*
gi 1973708721  246 DITNssGETEHkeFDKIIIsgAFPF 270
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV--TVPP 253
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 32-264 4.30e-11

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 67.52  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   32 SGLSAAYALAKLGyRDITVIEKHNTVGGMCESVEIEGKVYDLGGQVLaANSAPVIFHLAKESG--TQLEEMDLHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGleDRLVLPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  110 SLTGEYHDINVAEDYMSLVSL-----TLDIQDKAK---DTNRIGIHAVSEIASDLTPAYLEAHGIKSVPKSVQYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRlglAALASDALDEFDLDDFSLAESLLFLGRRGPGDVEVWDRLIDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRMKGGYMNLWKKISESLL---IKVccNTEVQAVRRNGSG 242
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRL--NTRVRSIDREGDG 236

                          250       260
                   ....*....|....*....|..
gi 1973708721  243 VNVDITNSsgetEHKEFDKIII 264
Cdd:pfam01593  237 VTVTLTDG----EVIEADAVIV 254
PLN02609 PLN02609
catalase
 1745-2015 4.97e-10

catalase


Pssm-ID: 215328 [Multi-domain]  Cd Length: 492  Bit Score: 64.38  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1745 KVKSRYFHRIGVSGKGYLKLYDDIQGLPEHNIF-GPGKKYTVIVRHSNSL--SADDDARLDARGAALRILSDEkGDdspl 1821
Cdd:PLN02609    58 RIPERVVHARGASAKGFFEVTHDISNLTCADFLrAPGVQTPVIVRFSTVIheRGSPETLRDPRGFAVKFYTRE-GN---- 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1822 LDLTLKTGKAFYARTISDFATwLVCGLaareehvKRVP--HVRD--AVW-------TSLRQ----------ADSYAEMH- 1879
Cdd:PLN02609   133 FDMVGNNFPVFFIRDGMKFPD-MVHAL-------KPNPktHIQEpwRILdflshhpESLHMftflfddrgiPQDYRHMEg 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1880 YYSNICRLFRfKDGQEMYVKFKLRPSD--KNIGEDTGkVEPSGILPPETgaiprdandtrpllflAEDFQNRVKSPNGVR 1957
Cdd:PLN02609   205 FGVHTYKLIN-KAGKAHYVKFHWKPTCgvKNLLDEEA-VRVGGSNHSHA----------------TQDLYDSIAAGNYPE 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721 1958 YIFQLQVMPvPQDEAARDI-ALDCTKPWDESQFPYIDVGEVIINENLTK--EGSERLEFNP 2015
Cdd:PLN02609   267 WKLFIQTMD-PEDEDKFDFdPLDVTKTWPEDILPLQPVGRLVLNRNIDNffAENEQLAFCP 326
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1125-1186 7.26e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.80  E-value: 7.26e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1125 EFLKQLVSEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1186
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK07233 PRK07233
hypothetical protein; Provisional
 23-68 8.90e-10

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 63.37  E-value: 8.90e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEG 68
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGG 45
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1342-1433 2.68e-09

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 57.57  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1342 VHLRGTVFLKHWfemlGARIGSSVLLDT-VDITDPSLVSIGDGAVIAEGALL--QSHEVRN---SVLRFQPIRIGRNCSV 1415
Cdd:COG0110     15 VVIGPGVRIYGG----NITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWI 90

                           90
                   ....*....|....*...
gi 1973708721 1416 GPYAVIQKGSVLGEGAEV 1433
Cdd:COG0110     91 GAGATILPGVTIGDGAVV 108
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1607-1704 1.71e-08

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 55.50  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1607 GAKVGKYCSIRS-INPVadprmvSIGAGVHLGDFSRIMTGfYSQSGYIQSNV-----------HVKDNSVIGSQSLILPG 1674
Cdd:cd04645     23 GSSVWFGAVLRGdVNPI------RIGERTNIQDGSVLHVD-PGYPTIIGDNVtvghgavlhgcTIGDNCLIGMGAIILDG 95

                           90       100       110
                   ....*....|....*....|....*....|
gi 1973708721 1675 SVVEKDVILGAISVAPVNSVLQSGGVYMGS 1704
Cdd:cd04645     96 AVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
Catalase smart01060
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ...
 1760-2002 2.30e-08

Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.


Pssm-ID: 215003  Cd Length: 373  Bit Score: 58.63  E-value: 2.30e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1760 GYLKLYDDIQGLPEHNIF-GPGKKYTVIVRHS----NSLSADDdARlDARGAALRILSDEK-----GDDSPLldltlktg 1829
Cdd:smart01060   53 GYFEVTEDISDYTKAAFFqKVGKKTPVFVRFStvagERGSADT-VR-DPRGFAVKFYTEEGnwdlvGNNTPV-------- 122

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1830 kaFYAR-TI--SDFAtwlvcglaareeH-VKRVP--HVRDA--VW-------TSLRQ----------ADSYAEMHYYSni 1884
Cdd:smart01060  123 --FFIRdPIkfPDFI------------HaQKRDPrtNLPDHdmFWdfwslnpESLHQvtwlmsdrgiPASYRHMNGFG-- 186

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1885 CRLFRF--KDGQEMYVKFKLRP-----------SDKNIGEDtgkvepsgilppetgaipRDandtrpllFLAEDFQNRVK 1951
Cdd:smart01060  187 VHTFKLvnAEGERFYVKFHFKPdqgiknltweeAAKLAGKD------------------PD--------YHRRDLYEAIE 240

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  1952 SPNGVRYIFQLQVMPvPQDEAARDI-ALDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:smart01060  241 RGDYPEWTLYVQVMP-EEDAEKFRFdPFDLTKVWPHKDYPLIEVGKMTLNRN 291
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1119-1195 1.76e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 50.62  E-value: 1.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1119 SNRNIVEFLKQLVSEQTGISIQNISATESLVS-YGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLL 1195
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 22-94 3.56e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 52.15  E-value: 3.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYR---DITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLG 77
Catalase pfam00199
Catalase;
1873-2002 1.91e-05

Catalase;


Pssm-ID: 459708  Cd Length: 383  Bit Score: 49.30  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1873 DSYAEMHYYSniCRLFRF--KDGQEMYVKFKLRP-----------SDKNIGEDtgkvepsgilppetgaipRDandtrpl 1939
Cdd:pfam00199  180 RSYRHMNGFG--VHTFKLvnADGERVYVKFHFKTdqgiknltweeAQKLAGKD------------------PD------- 232

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721 1940 lFLAEDFQNRVKSPNGVRYIFQLQVMPVPQDEAAR-DIaLDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:pfam00199  233 -YHTRDLYEAIERGDYPSWTLYVQVMTEEDAEKFRfNP-FDLTKVWPHKDYPLIEVGKMVLNRN 294
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1355-1433 1.06e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.41  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1355 EMLGARIGSSVLLDTVDITDPSLVSIGDGAV------------------IAEGALLQSH-EVRNSVL----------RFQ 1405
Cdd:PRK14356   241 ELLRARIVEKHLESGVLIHAPESVRIGPRATiepgaeiygpceiygasrIARGAVIHSHcWLRDAVVssgatihsfsHLE 320

                           90       100
                   ....*....|....*....|....*...
gi 1973708721 1406 PIRIGRNCSVGPYAVIQKGSVLGEGAEV 1433
Cdd:PRK14356   321 GAEVGDGCSVGPYARLRPGAVLEEGARV 348
PRK06753 PRK06753
hypothetical protein; Provisional
 23-178 4.47e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 45.06  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEIEGKV------YDLGGQVLAANSAPVIFHLAKESGTQ 96
Cdd:PRK06753     2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNESVKEVGAGIGIGDNVikklgnHDLAKGIKNAGQILSTMNLLDDKGTL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 LEEM---------DLHKLALIDSLTGEYHDinvaedymSLVSLTLDIQDKAKDTNRIGIHaVSEIASDLTPAYLEAHGIK 167
Cdd:PRK06753    81 LNKVklksntlnvTLHRQTLIDIIKSYVKE--------DAIFTGKEVTKIENETDKVTIH-FADGESEAFDLCIGADGIH 151

                          170
                   ....*....|....*....
gi 1973708721  168 SV------PKS-VQY-GYT 178
Cdd:PRK06753   152 SKvrqsvnADSkVRYqGYT 170
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1123-1190 4.87e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 38.00  E-value: 4.87e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  1123 IVEFLKQLVSEQTGISI-QNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANF 1190
Cdd:smart00823   13 LLDLVREQVAAVLGHAAaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 500-1072 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 592.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  500 HWAAKeiTQNKTLYTWINEEGAVVCQRTYAELDSNASCIAHKLLTSRKPtikpGDRVLLVHVPGLDFVDSFFGCLRAKVV 579
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  580 PVPVLPPdplqRGGQALTKIENIAKLCNAVAILSTVGYHSAVRAgsvknlisftrkSAESTAQWPNLPWLHTDswikssk 659
Cdd:cd05931     75 AVPLPPP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRA------------FAASRPAAGTPRLLVVD------- 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  660 vLPASNIGSQSES---QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 736
Cdd:cd05931    132 -LLPDTSAADWPPpspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMVCGGTAILFSPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKT 815
Cdd:cd05931    211 TPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVrDEDLE---GLDLSSWRVALNGAEPVRPAT 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  816 LKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKPILV-------------------DWQGRICCGYVDPndaDV 876
Cdd:cd05931    288 LRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 DIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKfPGRKYTRTGDLGRVIQGNLFITGRIKDLI 956
Cdd:cd05931    365 EVRIVDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLI 442

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  957 IVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDG--KPVDKDIIKQIESRV 1034
Cdd:cd05931    443 IVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVERGadPADLAAIAAAIRAAV 509

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1973708721 1035 AEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1072
Cdd:cd05931    510 AREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1722-2052 6.34e-126

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


Pssm-ID: 163707  Cd Length: 328  Bit Score: 399.88  E-value: 6.34e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1722 EEMDSRYKRIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHNIFGPGKKYTVIVRHSNSLSADDDARL 1801
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1802 DARGAALRILSDEKGDDSPLlDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSYAEMH 1879
Cdd:cd08151     80 DGRGAALRFLNAGDDDAGPL-DLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1880 YYSNICRLFRFKDGQEMYVKFKLRPSDKNIGEDTGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFQNRVKSPnGVRYI 1959
Cdd:cd08151    159 YYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1960 FQLQVMPVPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSERLEFNPfLRCHEVDVIRATSSSQ-SASIDH 2038
Cdd:cd08151    238 LQIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGH 314

                          330
                   ....*....|....
gi 1973708721 2039 GRSLVYEICQHLRN 2052
Cdd:cd08151    315 LRSLVYEISQRLRK 328
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 486-1080 3.13e-94

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 320.14  E-value: 3.13e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  486 IVFPDLPNLDSYLKHWAakEITQNKTLYTWIN---EEGAVVCQRTYAELDSNASCIAHKLltsrKPTIKPGDRVLLVHVP 562
Cdd:PRK07769    15 IRFPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  563 GLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHSAVRAgsvknlisFTRKsaESTAQ 642
Cdd:PRK07769    89 NLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDD----CTPSAILTTTDSAEGVRK--------FFRA--RPAKE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  643 WPNLpwLHTDSwiksskvLPASnIGS---QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVL 719
Cdd:PRK07769   155 RPRV--IAVDA-------VPDE-VGAtwvPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRG 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  720 VSWLPQYHDMGLIGGLFTAMvCGGTAILFSPLTFIRNPLLWLQTIS----DYKATHSAGPNFAFELVIRRlEADKAKAHD 795
Cdd:PRK07769   225 VSWLPFFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFEHAAAR-GLPKDGEPP 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  796 YDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKP--ILVDWQ----GRIC---- 865
Cdd:PRK07769   303 LDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRFVevpa 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  866 ----------CGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKF-------- 927
Cdd:PRK07769   383 dapnavaqvsAGKVGVSEWAV---IVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaeg 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  928 --PGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDVLSAK-------G 998
Cdd:PRK07769   459 apDDALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVvfddshaG 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  999 ISL-PDASDEvGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGTL 1075
Cdd:PRK07769   539 LKFdPEDTSE-QLVIVAERAPGahKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617

                          650
                   ....*....|.
gi 1973708721 1076 ------NTVPD 1080
Cdd:PRK07769   618 rsgygqPAFPD 628
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 527-1070 2.85e-91

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 309.57  E-value: 2.85e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSRKPtikpGDRVLLVHVPGLDFVDSFFGCLRAkvvpVPVLPPDPLQRGGQALTKIENIAKLC 606
Cdd:PRK05850    37 TWSQLYRRTLNVAEELRRHGST----GDRAVILAPQGLEYIVAFLGALQA----GLIAVPLSVPQGGAHDERVSAVLRDT 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTvgyhSAVrAGSVknlisftRKSAESTAQWPNLPWLHTDSwiksskVLPASNIGSQSESQP-DDLCFLQFTSG 685
Cdd:PRK05850   109 SPSVVLTT----SAV-VDDV-------TEYVAPQPGQSAPPVIEVDL------LDLDSPRGSDARPRDlPSTAYLQYTSG 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  686 STGDAKGVMITHGGLIHNV-KLMRRRYRST-----SNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTFIRNPLL 759
Cdd:PRK05850   171 STRTPAGVMVSHRNVIANFeQLMSDYFGDTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPAR 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  760 WLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYG 838
Cdd:PRK05850   251 WMQLLASNPHAFSAAPNFAFELAVRKTsDDDMA---GLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYG 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  839 LAENCVFVGCAYGKKKPILVDW--------QGRIC--------CGYVDPNDADVdiRIVDADTGLEVdEDGKEGEIWISS 902
Cdd:PRK05850   328 LAEATVYVATREPGQPPESVRFdyeklsagHAKRCetgggtplVSYGSPRSPTV--RIVDPDTCIEC-PAGTVGEIWVHG 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  903 PSAGIGYWGKEELSQKTFRNKLQK----FPGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssEL 978
Cdd:PRK05850   405 DNVAAGYWQKPEETERTFGATLVDpspgTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQ---EI 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  979 LRpGCCAVISVPEDvLSAKgislpdasdevgLVVIAELK-----DGKPVDK--DIIKQIESRVAEEHGVTVASVKLIRPR 1051
Cdd:PRK05850   482 TG-GRVAAISVPDD-GTEK------------LVAIIELKkrgdsDEEAMDRlrTVKREVTSAISKSHGLSVADLVLVAPG 547

                          570
                   ....*....|....*....
gi 1973708721 1052 TISKTTSGKIKRFECLKQF 1070
Cdd:PRK05850   548 SIPITTSGKIRRAACVEQY 566
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 480-1075 3.40e-90

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 308.19  E-value: 3.40e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  480 LSETHGIVFPDLPNLDSYLKHWAakEITQNKTLYTWIN---EEGAVVCQRTYAELDSNASCIAHKLltsrKPTIKPGDRV 556
Cdd:NF038339     6 LDENGNIRFPDGATLVDHVERNA--RERADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  557 LLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHSAVRagsvknliSFTRks 636
Cdd:NF038339    80 AILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEPGHTDRLHAVLGD----CKPSAILTATSSAEGVR--------KFFR-- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  637 AESTAQWPN------LPWLHTDSWIKsskvlPASNIgsqsesqpDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRR 710
Cdd:NF038339   146 SLPAKERPRviavdaVPDSVGSTWVR-----PDADL--------DDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDA 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  711 YRSTSNTVLVSWLPQYHDMGLIGGLFTAMvcGGTAILF-SPLTFIRNPLLW---LQTISDYKATHSAGPNFAFELVIRR- 785
Cdd:NF038339   213 IELDENSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARg 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  786 LEADkakAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKP--ILVDW--- 860
Cdd:NF038339   291 LPKE---GEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReel 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  861 -QGRI--------------CCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQ 925
Cdd:NF038339   368 nAGRIvevdpdapnavaqvSCGYVARSQWAV---IVDPETGTEL-PDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLK 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  926 KF-----------PGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDVL 994
Cdd:NF038339   444 SRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVPANQL 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  995 -------SAKGISL-PDASDEvGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRF 1064
Cdd:NF038339   524 paevfenSHSGLKYdADDSSE-QLVIVAERAPGagKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARR 602

                          650
                   ....*....|.
gi 1973708721 1065 ECLKQFVDGTL 1075
Cdd:NF038339   603 ACKAAYIDGTL 613
PRK05691 PRK05691
peptide synthase; Validated
 517-1232 2.90e-86

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 316.72  E-value: 2.90e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  517 NEEGAVVcqrTYAELDSNASCIAHKLLTSrkptIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQA- 595
Cdd:PRK05691    35 PGEGVVL---SYRDLDLRARTIAAALQAR----ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQEr 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  596 -LTKIEN--------IAKLCNAVAILStvgyhsAVRAGSVKNLISFTRKSAESTAQW--PNLpwlhtdswiksskvlpas 664
Cdd:PRK05691   108 lLSIIADaeprllltVADLRDSLLQME------ELAAANAPELLCVDTLDPALAEAWqePAL------------------ 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  665 nigsqsesQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYHDMGLIGGLFTAMVCG 742
Cdd:PRK05691   164 --------QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddVIVSWLPLYHDMGLIGGLLQPIFSG 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  743 GTAILFSPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLeADKAKAHdYDLSSMIFFMIAAEPVRQKTLKRFVEL 822
Cdd:PRK05691   236 VPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERV-SESALER-LDLSRWRVAYSGSEPIRQDSLERFAEK 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSQEVMAPGYGLAENCVFV-GCAYGKKKPIL-VDWQG-------------RICCGYVDPNDAdvdIRIVDADTgL 887
Cdd:PRK05691   314 FAACGFDPDSFFASYGLAEATLFVsGGRRGQGIPALeLDAEAlarnraepgtgsvLMSCGRSQPGHA---VLIVDPQS-L 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  888 EVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfPGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSAD 967
Cdd:PRK05691   390 EVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQD 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  968 VEKTVESSSELLRPGCCAVISVPEDVLSAKGISLpDASDEVGLVVIAElkdgkpvdkDIIKQIESRVAEEHGVTVASVKL 1047
Cdd:PRK05691   466 IEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAA-EISRSVQKILPPQ---------ALIKSIRQAVAEACQEAPSVVLL 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1048 IRPRTISKTTSGKIKRFECLKQFVDGTLntvpDPIVtkrlltrSFTTGTcregntprSHLAKSSLPPSPKLSNRNIVEFL 1127
Cdd:PRK05691   536 LNPGALPKTSSGKLQRSACRLRLADGSL----DSYA-------LFPALQ--------AVEAAQTAASGDELQARIAAIWC 596

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1128 KQLVSEQtgisiqnISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLLMKSQPH---LVT 1204
Cdd:PRK05691   597 EQLKVEQ-------VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIAR 669

                          730       740
                   ....*....|....*....|....*...
gi 1973708721 1205 TQSNHSEPEiltadfSMEISRLhpWLIW 1232
Cdd:PRK05691   670 LPRGQALPQ------SLAQNRL--WLLW 689
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 652-1072 1.75e-84

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 291.17  E-value: 1.75e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  652 DSWIKSSKVLPASNIGSQSESQP-DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMG 730
Cdd:NF040633   177 ESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMG 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 LIGGLFtAMVCGGTAILFSPLTFIRNPLLWLQTIS---DYKATHSAGPNFAFELVIRRleADKAKAHDYDLSSMIFFMIA 807
Cdd:NF040633   257 IILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNFALELAARY--ANPEEGEDLDLSAVDGIIIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  808 AEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKPiLVDWQGR--ICCGYVDPNDADVD-------- 877
Cdd:NF040633   334 SEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERP-LFTYFDReaLAEGRAVEVAEDSEnavpfasn 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  878 --------IRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQK----------FPGRKYTRTGDLG 939
Cdd:NF040633   413 gqvvrpqvLAIVDPETGQEL-PDGTVGEIWVHGDNMAAGYLDREEETAETFRNTLGErlaensraegAPEDNWMATGDLG 491

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  940 RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDG 1019
Cdd:NF040633   492 VIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPGD-------------DVEKLVILAERDDE 558

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721 1020 KPVDKD--IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1072
Cdd:NF040633   559 ADESGDaeAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 521-1077 3.13e-83

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 281.70  E-value: 3.13e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQALT 597
Cdd:COG0318     17 ALVFggrRLTYAELDARARRLAAAL---RALGVGPGDRVALLLPNSPEFVVAFLAALRA---------------GAVVVP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 --------KIENIAKLCNAVAILStvgyhsavragsvknlisftrksaestaqwpnlpwlhtdswiksskvlpasnigsq 669
Cdd:COG0318     79 lnprltaeELAYILEDSGARALVT-------------------------------------------------------- 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 sesqpddlCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFS 749
Cdd:COG0318    103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PltfiRNPLLWLQTISDYKATHSAG-PNFAFELvirrleADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpygl 828
Cdd:COG0318    175 R----FDPERVLELIERERVTVLFGvPTMLARL------LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF----- 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sQEVMAPGYGLAENCVFVGCAygkkkPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIG 908
Cdd:COG0318    240 -GVRIVEGYGLTETSPVVTVN-----PEDPGERRPGSVGRPLPG---VEVRIVDED-GREL-PPGEVGEIVVRGPNVMKG 308

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWGKEELSQKTFRNklqkfpGrkYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVI 987
Cdd:COG0318    309 YWNDPEATAEAFRD------G--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVV 377

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  988 SVPEDVLsakgislpdasDEVGLVVIAeLKDGKPVD-KDIIKQIESRVAeEHGVtvasvklirPRTIS------KTTSGK 1060
Cdd:COG0318    378 GVPDEKW-----------GERVVAFVV-LRPGAELDaEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGK 435

                          570
                   ....*....|....*..
gi 1973708721 1061 IKRFECLKQFVDGTLNT 1077
Cdd:COG0318    436 IDRRALRERYAAGALEA 452
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 480-1075 4.18e-80

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 278.16  E-value: 4.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  480 LSETHGIVFPDLPNLDSYLKHWAAkeITQNKTLYTWIN---EEGAVVCQRTYAELDSNASCIAHKLltsrKPTIKPGDRV 556
Cdd:PRK12476    22 LDADGNIALPPGTTLISLIERNIA--NVGDTVAYRYLDhshSAAGCAVELTWTQLGVRLRAVGARL----QQVAGPGDRV 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  557 LLVHVPGLDFVDSFFGCLRAkvvPVPVLPPDPLQRGGQAlTKIENIAKLCNAVAILSTVGYHSAVRagsvknliSFTRKs 636
Cdd:PRK12476    96 AILAPQGIDYVAGFFAAIKA---GTIAVPLFAPELPGHA-ERLDTALRDAEPTVVLTTTAAAEAVE--------GFLRN- 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  637 aestaqwpnLPWLHTDSWIKSSKVlPASNIGS--QSESQPDDLCFLQFTSGSTGDAKGVMITHGG-------LIHNVKLM 707
Cdd:PRK12476   163 ---------LPRLRRPRVIAIDAI-PDSAGESfvPVELDTDDVSHLQYTSGSTRPPVGVEITHRAvgtnlvqMILSIDLL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  708 RRryrstsNTVLVSWLPQYHDMGLIGGLFTAmVCGGTAILFSPLTFIRNPLLWLQTISD---YKATHSAGPNFAFELVIR 784
Cdd:PRK12476   233 DR------NTHGVSWLPLYHDMGLSMIGFPA-VYGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVTAAPNFAYEWAAQ 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  785 R-LEADKAkahDYDLSSMIFfMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGKKKP--ILVDWQ 861
Cdd:PRK12476   306 RgLPAEGD---DIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPsvVYLDRE 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  862 ----GR--------------ICCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNK 923
Cdd:PRK12476   382 qlgaGRavrvaadapnavahVSCGQVARSQWAV---IVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAK 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  924 LQKF-----------PGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVISVPed 992
Cdd:PRK12476   458 LQSRlaegshadgaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVP-- 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  993 vlsakgislpdASDEVGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQF 1070
Cdd:PRK12476   536 -----------AEDNERLVIVAERAAGtsRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQY 604


                   ....*
gi 1973708721 1071 VDGTL 1075
Cdd:PRK12476   605 LDGRL 609
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 671-1063 1.15e-75

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 263.01  E-value: 1.15e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGGLFTAMVCGGTAILFS 749
Cdd:PRK07768   148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVT 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEAdKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLS 829
Cdd:PRK07768   228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRR-QAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLR 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 QEVMAPGYGLAENCV---FVGCAYGkkkpILVDwqgriccgYVDPNDADVDIRIVDAD--------------TGLE---V 889
Cdd:PRK07768   307 PEAILPAYGMAEATLavsFSPCGAG----LVVD--------EVDADLLAALRRAVPATkgntrrlatlgpplPGLEvrvV 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  890 DEDGKE------GEIWISSPSAGIGYW---GKEELSQKtfrnklqkfpgRKYTRTGDLGRVIQ-GNLFITGRIKDLIIVA 959
Cdd:PRK07768   375 DEDGQVlpprgvGVIELRGESVTPGYLtmdGFIPAQDA-----------DGWLDTGDLGYLTEeGEVVVCGRVKDVIIMA 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  960 GRNIYSADVEKTVeSSSELLRPGCcaVISVPedvlsakgisLPDASDEVGLVVIAELKDGKPVD--KDIIKQIESRVAEE 1037
Cdd:PRK07768   444 GRNIYPTDIERAA-ARVEGVRPGN--AVAVR----------LDAGHSREGFAVAVESNAFEDPAevRRIRHQVAHEVVAE 510

                          410       420
                   ....*....|....*....|....*.
gi 1973708721 1038 HGVTVASVKLIRPRTISKTTSGKIKR 1063
Cdd:PRK07768   511 VGVRPRNVVVLGPGSIPKTPSGKLRR 536
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
527-1070 1.20e-74

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 261.35  E-value: 1.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltSRKPTIkpGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrggqaltkieniaklc 606
Cdd:NF038337    40 TWAQLYRRTLNVAHEV--RRHGTT--GDRAVILAPQGLPYIVAFLGAMQA------------------------------ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTV---GYH----SAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKS--SKVLPASNIGSQSESQPDDL 677
Cdd:NF038337    86 GLIAVPLSVpqpGSHdervSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPAVIEidSLDLDGPNSPSIRISDAPSI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSN------TVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPL 751
Cdd:NF038337   166 AYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPV 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQ 830
Cdd:NF038337   246 AFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTtDADLA---GLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFRE 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMAPGYGLAENCVFVGCAYGKKKPILVDWQ-GRICCGYVDPNDADVD-------------IRIVDADTGLEVdEDGKEG 896
Cdd:NF038337   323 DMMQPSYGLAEATVYVASRAEGGAPEVVHFEpEKLSEGSAQRCEARTGspllsygtptsptVRIVDPDTCIEC-PAGTVG 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  897 EIWISSPSAGIGYWGKEELSQKTFRNKLQK----FPGRKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTV 972
Cdd:NF038337   402 EIWVHGDNVAEGYWQKPEETRRTFGGVLANpspgTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTV 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  973 ESsselLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELK-----DGKPVDK-DIIK-QIESRVAEEHGVTVASV 1045
Cdd:NF038337   482 QE----ITGGRVAAISVPVD-------------ETEKLVTIIELKkrgdsDEEAMRKlDAVKnNVTAAISRSHGLNVADL 544

                          570       580
                   ....*....|....*....|....*
gi 1973708721 1046 KLIRPRTISKTTSGKIKRFECLKQF 1070
Cdd:NF038337   545 VLVPPGSIPTTTSGKIRRAACVEQY 569
PRK09192 PRK09192
fatty acyl-AMP ligase;
528-1079 3.93e-73

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 256.86  E-value: 3.93e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  528 YAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLqrGGQA--LTKIENIAKL 605
Cdd:PRK09192    52 YQTLRARAEAGARRLLAL---GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGF--GGREsyIAQLRGMLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  606 CNAVAILSTVGyhsavragsvknLISFTRKSAESTaqwpNLPWLHTDSWIKSskvLPASNIgSQSESQPDDLCFLQFTSG 685
Cdd:PRK09192   127 AQPAAIITPDE------------LLPWVNEATHGN----PLLHVLSHAWFKA---LPEADV-ALPRPTPDDIAYLQYSSG 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  686 STGDAKGVMITHGGLIHNVK-------LMRRRYRStsntvlVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTFIRNPL 758
Cdd:PRK09192   187 STRFPRGVIITHRALMANLRaishdglKVRPGDRC------VSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  759 LWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQEVMAPGY 837
Cdd:PRK09192   261 QWLDLISRNRGTISYSPPFGYELCARRVnSKDLA---ELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSY 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  838 GLAENCVFVGCA----------------YGKKKPILVDWQGR-----ICCGYVDPnDADVDIRivdadtglevDEDGKE- 895
Cdd:PRK09192   338 GLAEATLAVSFSplgsgivveevdrdrlEYQGKAVAPGAETRrvrtfVNCGKALP-GHEIEIR----------NEAGMPl 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 -----GEIWISSPSAGIGYWGKEElSQKTFR--NKLQkfpgrkytrTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADV 968
Cdd:PRK09192   407 pervvGHICVRGPSLMSGYFRDEE-SQDVLAadGWLD---------TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDI 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  969 EKTVESSSElLRPGCCAVISVPEDvlsakgislpdasDEVGLVVIAELKDGKPVDK-DIIKQIESRVAEEHGVTVaSVKL 1047
Cdd:PRK09192   477 EWIAEQEPE-LRSGDAAAFSIAQE-------------NGEKIVLLVQCRISDEERRgQLIHALAALVRSEFGVEA-AVEL 541

                          570       580       590
                   ....*....|....*....|....*....|..
gi 1973708721 1048 IRPRTISKTTSGKIKRFECLKQFVDGTLNTVP 1079
Cdd:PRK09192   542 VPPHSLPRTSSGKLSRAKAKKRYLSGAFASLD 573
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 513-1073 5.54e-72

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 252.20  E-value: 5.54e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  513 YTWINEEGAVVCQrTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRG 592
Cdd:cd05906     28 ITYIDADGSEEFQ-SYQDLLEDARRLAAGL---RQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  593 GQALTKIENIAKLCNAVAILSTVGYHSAVRagsvknlisftrksaESTAQWPNLPW-LHTDSWIKSSKVLPASNIgsqse 671
Cdd:cd05906    104 NARLRKLRHIWQLLGSPVVLTDAELVAEFA---------------GLETLSGLPGIrVLSIEELLDTAADHDLPQ----- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPL 751
Cdd:cd05906    164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAKahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQE 831
Cdd:cd05906    244 EILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDG--TWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPD 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  832 VMAPGYGLAENCVfvGCAYGkkkpiLVDWQGRI-------CCGYVDPNdadVDIRIVDADTGLEvdEDGKEGEIWISSPS 904
Cdd:cd05906    322 AIRPAFGMTETCS--GVIYS-----RSFPTYDHsqalefvSLGRPIPG---VSMRIVDDEGQLL--PEGEVGRLQVRGPV 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCC 984
Cdd:cd05906    390 VTKGYYNNPEANAEAFTED-------GWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTA 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  985 AVisvpedvlsakgiSLPDASDEVGLVVIAELKDGKPVDK--DIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIK 1062
Cdd:cd05906    463 AF-------------AVRDPGAETEELAIFFVPEYDLQDAlsETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQ 529

                          570
                   ....*....|.
gi 1973708721 1063 RFECLKQFVDG 1073
Cdd:cd05906    530 RSKLKAAFEAG 540
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 676-1062 1.28e-68

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 235.26  E-value: 1.28e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdMGLIGGLFTAMVCGGTAILFSPltfiR 755
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPK----F 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 NPLLWLQTISDYKATHSAGPNFAFELVIRRLEADkakahDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPyglsqeVMAP 835
Cdd:cd04433     76 DPEAALELIEREKVTILLGVPTLLARLLKAPESA-----GYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVN 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  836 GYGLAENCVFVGCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLevDEDGKEGEIWISSPSAGIGYWGKEEL 915
Cdd:cd04433    145 GYGLTETGGTVATGPPDDDARKPGSVGRPV--------PGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGYWNNPEA 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  916 SQKTFRNklqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEdvl 994
Cdd:cd04433    215 TAAVDED--------GWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPD--- 280

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721  995 sakgislPDASDEVGLVViaELKDGKPVDKDIIKQIesrVAEEHGVTVASVKLIRPRTISKTTSGKIK 1062
Cdd:cd04433    281 -------PEWGERVVAVV--VLRPGADLDAEELRAH---VRERLAPYKVPRRVVFVDALPRTASGKID 336
AMP-binding pfam00501
AMP-binding enzyme;
527-959 3.74e-66

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 231.05  E-value: 3.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHkLLTSRKptIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQALT--------K 598
Cdd:pfam00501   23 TYRELDERANRLAA-GLRALG--VGKGDRVAILLPNSPEWVVAFLACLKA---------------GAVYVPlnprlpaeE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  599 IENIAKLCNAVAILSTVGYHSAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKSSKVLPASNIgsqsesQPDDLC 678
Cdd:pfam00501   85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP------DPDDLA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  679 FLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRS----TSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTFi 754
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  755 RNPLLWLQTISDYKATHSAGPNFAFELVirrleADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPyglsqeVMA 834
Cdd:pfam00501  238 LDPAALLELIERYKVTVLYGVPTLLNML-----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALV 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  835 PGYGLAENCVFVGCAYgkkkPILVDWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 914
Cdd:pfam00501  307 NGYGLTETTGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPE 378

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1973708721  915 LSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVA 959
Cdd:pfam00501  379 LTAEAFDED-------GWYRTGDLGRRDEdGYLEIVGRKKDQIKLG 417
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 671-1073 1.11e-61

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 220.82  E-value: 1.11e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSP 750
Cdd:cd05908    102 CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPT 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  751 LTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADkaKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQ 830
Cdd:cd05908    182 RLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPE--KANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKR 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMAPGYGLAENCVFV-----------------GCAYGKKKPiLVDWQGRICCGYVDPNDA--DVDIRIVDADTglEVDE 891
Cdd:cd05908    260 NAILPVYGLAEASVGAslpkaqspfktitlgrrHVTHGEPEP-EVDKKDSECLTFVEVGKPidETDIRICDEDN--KILP 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  892 DGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKT 971
Cdd:cd05908    337 DGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD-------GWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERI 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  972 VEsssELlrpgccavisvpEDVLSAKgislpdasdevglVVIAELKDGKPVDKDIIKQIESRVAEEHGVTVA-------- 1043
Cdd:cd05908    410 AE---EL------------EGVELGR-------------VVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGkkikkhln 461

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1973708721 1044 -----SVKLIRP-RTISKTTSGKIKRFECLKQFVDG 1073
Cdd:cd05908    462 krggwQINEVLPiRRIPKTTSGKVKRYELAQRYQSG 497
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 512-1079 6.39e-52

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 194.10  E-value: 6.39e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  512 LYTWINEEGAVVCQRTYAELDSNASCIAHKLLTsrKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQR 591
Cdd:cd05905      1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQK--KVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  592 GGqaltkieniaklcnavAILSTVGYHSAVRAGSV-KNLISFTRKSAESTAQ-----WPNLPWLHTdswIKSSKVLPASN 665
Cdd:cd05905     79 LG----------------FLLGTCKVRVALTVEAClKGLPKKLLKSKTAAEIakkkgWPKILDFVK---IPKSKRSKLKK 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  666 IGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTA 745
Cdd:cd05905    140 WGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHT 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  746 ILFSPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKA--KAHDYDLSSMIFFMIAAE-PVRQKTLKRFVEL 822
Cdd:cd05905    220 ILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLAslKNRDVNLSSLRMCMVPCEnRPRISSCDSFLKL 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSQEVMAPGYGlaenCVFVGcaygkkkpiLVDWQG----RICCGYVDPN------------DA-------DVDIR 879
Cdd:cd05905    300 FQTLGLSPRAVSTEFG----TRVNP---------FICWQGtsgpEPSRVYLDMRalrhgvvrlderDKpnslplqDSGKV 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  880 IVDADTGLeVDEDGKE-------GEIWISSPSAGIGYWG----KEELSQKTFRNKLQKFPGRK-YTRTGDLG-------- 939
Cdd:cd05905    367 LPGAQVAI-VNPETKGlckdgeiGEIWVNSPANASGYFLldgeTNDTFKVFPSTRLSTGITNNsYARTGLLGflrptkct 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  940 ---RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVEsSSELLRPGCCavisvpedVLSAKGIslpdasdevgLVVIAEL 1016
Cdd:cd05905    446 dlnVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVM-RVHPYRGRCA--------VFSITGL----------VVVVAEQ 506

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721 1017 KDGKPVDK-DIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGTLNTVP 1079
Cdd:cd05905    507 PPGSEEEAlDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIY 570
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 521-1063 7.21e-50

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 185.46  E-value: 7.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVCQ---RTYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQA-- 595
Cdd:cd05936     17 ALIFMgrkLTYRELDALAEAFAAGLQNL---GVQPGDRVALMLPNCPQFPIAYFGALKA---------------GAVVvp 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  596 ----LT--KIENIAKLCNAVAILSTVGYHSAVRAGsvknlisftrksaESTAQWPNLPwlhtdswiksskvlpasnigsq 669
Cdd:cd05936     79 lnplYTprELEHILNDSGAKALIVAVSFTDLLAAG-------------APLGERVALT---------------------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 sesqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRY--RSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL 747
Cdd:cd05936    124 ----PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 ---FSPLTFirnpllwLQTISDYKATHSAGPNFAFELVIRRLEADKakahdYDLSSMIFFMIAAEPVRQKTLKRFVELTR 824
Cdd:cd05936    200 iprFRPIGV-------LKEIRKHRVTIFPGVPTMYIALLNAPEFKK-----RDFSSLRLCISGGAPLPVEVAERFEELTG 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  825 pyglsqevmAP---GYGLAEnCVFVGCA---YGKKKPilvdwqgriccGYVDPNDADVDIRIVDADtGLEVdEDGKEGEI 898
Cdd:cd05936    268 ---------VPiveGYGLTE-TSPVVAVnplDGPRKP-----------GSIGIPLPGTEVKIVDDD-GEEL-PPGEVGEL 324

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  899 WISSPSAGIGYWGKEELSQKTFRNklqkfpGrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessse 977
Cdd:cd05936    325 WVRGPQVMKGYWNRPEETAEAFVD------G--WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVL----- 391

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  978 LLRPGC--CAVISVPEdvlsakgislPDASDEVGLVVIaeLKDGKPVDK-DIIKQiesrvAEEHgvtVASVKliRPRTIS 1054
Cdd:cd05936    392 YEHPAVaeAAVVGVPD----------PYSGEAVKAFVV--LKEGASLTEeEIIAF-----CREQ---LAGYK--VPRQVE 449

                          570
                   ....*....|....*
gi 1973708721 1055 ------KTTSGKIKR 1063
Cdd:cd05936    450 frdelpKSAVGKILR 464
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
668-1074 9.96e-50

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 186.51  E-value: 9.96e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  668 SQSESQPDDLCF--LQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGgLFTAMVcGGT 744
Cdd:PRK05851   143 SASLTPPDSGGPavLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAF-LLTAAL-AGA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  745 AILFSPLT-FIRNPLLWLQTISDYKATHSAGPNFAFELV---IRRLEadkakahDYDLSSMIFFMIAAEPVRQKTLKRFV 820
Cdd:PRK05851   221 PLWLAPTTaFSASPFRWLSWLSDSRATLTAAPNFAYNLIgkyARRVS-------DVDLGALRVALNGGEPVDCDGFERFA 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 ELTRPYGLSQEVMAPGYGLAENCvfvgCAYGKKKP---------ILVDWQGRICCGYVDPNDADVDIRIVDADTGLEVDE 891
Cdd:PRK05851   294 TAMAPFGFDAGAAAPSYGLAEST----CAVTVPVPgiglrvdevTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAG 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  892 DGKeGEIWISSPSAGIGYWGKEELSQKTFrnklqkFPgrkytrTGDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKt 971
Cdd:PRK05851   370 REI-GEIEIRGASMMSGYLGQAPIDPDDW------FP------TGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER- 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  972 VESSSELLRPGccAVISVPEDvlsakgislpDASDEVGLVVIAELKDGkpvDKDIIK-QIESRVAEEHGVTVASVKLIRP 1050
Cdd:PRK05851   436 VAAQVRGVREG--AVVAVGTG----------EGSARPGLVIAAEFRGP---DEAGARsEVVQRVASECGVVPSDVVFVAP 500

                          410       420
                   ....*....|....*....|....
gi 1973708721 1051 RTISKTTSGKIKRFECLKQFVDGT 1074
Cdd:PRK05851   501 GSLPRTSSGKLRRLAVKRSLEAAD 524
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 521-1061 2.87e-43

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 165.09  E-value: 2.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGClrakvvpvpvlppdplqrggqalt 597
Cdd:cd17631     13 ALVFggrSLTYAELDERVNRLAHAL---RALGVAKGDRVAVLSKNSPEFLELLFAA------------------------ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 kieniaklcnavailstvgyhsaVRAGSVKNLISFtRKSAESTAqwpnlpWLHTDSwikSSKVLPasnigsqsesqpDDL 677
Cdd:cd17631     66 -----------------------ARLGAVFVPLNF-RLTPPEVA------YILADS---GAKVLF------------DDL 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVswLPQYHDMGLIGGLFTAMVCGGTAIL---FSPLT 752
Cdd:cd17631    101 ALLMYTSGTTGRPKGAMLTHRNLLWNAvnALAALDLGPDDVLLVV--APLFHIGGLGVFTLPTLLRGGTVVIlrkFDPET 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FirnpllwLQTISDYKATHSAGPNFAFELVIRRLEADkakahDYDLSSMIFFMIAAEPVRQKTLKRFVEltrpYGLsqeV 832
Cdd:cd17631    179 V-------LDLIERHRVTSFFLVPTMIQALLQHPRFA-----TTDLSSLRAVIYGGAPMPERLLRALQA----RGV---K 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAEnCVFVGCAYGKKkpilvDWQGRI-CCGYVDPNdadVDIRIVDADtGLEVDeDGKEGEIWISSPSAGIGYWG 911
Cdd:cd17631    240 FVQGYGMTE-TSPGVTFLSPE-----DHRRKLgSAGRPVFF---VEVRIVDPD-GREVP-PGEVGEIVVRGPHVMAGYWN 308

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  912 KEELSQKTFRNklqkfpGrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesssellrpgccAVISVP 990
Cdd:cd17631    309 RPEATAAAFRD------G--WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVE---------------DVLYEH 365

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  991 EDVLSAKGISLPDAS-DEVGLVVIAeLKDGKPVD-KDIIKQIESRvaeehgvtVASVKliRPRTI------SKTTSGKI 1061
Cdd:cd17631    366 PAVAEVAVIGVPDEKwGEAVVAVVV-PRPGAELDeDELIAHCRER--------LARYK--IPKSVefvdalPRNATGKI 433
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 527-1061 6.12e-41

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 159.30  E-value: 6.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGqaltkienIAKLC 606
Cdd:cd05911     12 TYAQLRTLSRRLAAGL---RKLGLKKGDVVGIISPNSTYYPPVFLGCLFA---------------GG--------IFSAA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTVGYH---------------------SAVRAGSVKNLISFT--RKSAESTAQWPNLPWLHTDSWIKSSKVLPa 663
Cdd:cd05911     66 NPIYTADELAHQlkiskpkviftdpdglekvkeAAKELGPKDKIIVLDdkPDGVLSIEDLLSPTLGEEDEDLPPPLKDG- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  664 snigsqsesqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRST--SNTVLVSWLPQYHDMGLIgGLFTAMVC 741
Cdd:cd05911    145 ----------KDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLF-TTLASLLN 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  742 GGTAIL---FSPLTFirnpllwLQTISDYKATHSAGPNFAFELVIRRLEADKakahdYDLSSMIFFMIAAEPVrqktLKR 818
Cdd:cd05911    214 GATVIImpkFDSELF-------LDLIEKYKITFLYLVPPIAAALAKSPLLDK-----YDLSSLRVILSGGAPL----SKE 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FVELTRPYGLSQEVMaPGYGLAENCVFVGCAygkkkPILVDWQGriCCGYVDPNdadVDIRIVDADTGlEVDEDGKEGEI 898
Cdd:cd05911    278 LQELLAKRFPNATIK-QGYGMTETGGILTVN-----PDGDDKPG--SVGRLLPN---VEAKIVDDDGK-DSLGPNEPGEI 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  899 WISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesssE 977
Cdd:cd05911    346 CVRGPQVMKGYYNNPEATKETFDED-------GWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELE-------A 411

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  978 LLR--PGC--CAVIsvpedvlsakGISLPDASD-EVGLVVIAelKDGKPVDKDIIKQIESRVAEEH----GVTVASvkli 1048
Cdd:cd05911    412 VLLehPGVadAAVI----------GIPDEVSGElPRAYVVRK--PGEKLTEKEVKDYVAKKVASYKqlrgGVVFVD---- 475

                          570
                   ....*....|...
gi 1973708721 1049 rprTISKTTSGKI 1061
Cdd:cd05911    476 ---EIPKSASGKI 485
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
509-1073 8.74e-39

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 154.50  E-value: 8.74e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  509 NKTLYTWINEEGAVVcQRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLvHVP-GLDFVDSFFGCLRAkvvpvpvlppd 587
Cdd:COG0365     24 DKVALIWEGEDGEER-TLTYAELRREVNRFANAL---RALGVKKGDRVAI-YLPnIPEAVIAMLACARI----------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  588 plqrGG-----------QALtkiENIAKLCNAVAILSTVGYHSAVR--------------AGSVKNLISFTRKSAEstAQ 642
Cdd:COG0365     88 ----GAvhspvfpgfgaEAL---ADRIEDAEAKVLITADGGLRGGKvidlkekvdealeeLPSLEHVIVVGRTGAD--VP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  643 WPNLPWLHTdsWIKS-SKVLPASNIGSqsesqpDDLCFLQFTSGSTGDAKGVMITHGG-LIHNVKLMRR--------RYR 712
Cdd:COG0365    159 MEGDLDWDE--LLAAaSAEFEPEPTDA------DDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYvldlkpgdVFW 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  713 STSNtvlVSWLpqyhdMGLIGGLFTAMVCGGTAILF--SPLTfiRNPLLWLQTISDYKATH-SAGPNFafelvIRRLE-A 788
Cdd:COG0365    231 CTAD---IGWA-----TGHSYIVYGPLLNGATVVLYegRPDF--PDPGRLWELIEKYGVTVfFTAPTA-----IRALMkA 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  789 DKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpyGLsqeVMAPGYGLAE-NCVFVGCAYGKK-KPilvdwqGRICC 866
Cdd:COG0365    296 GDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAV---GV---PIVDGWGQTEtGGIFISNLPGLPvKP------GSMGK 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  867 ---GYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAG--IGYWGKEELSQKTFRNKlqkFPGrkYTRTGDLGRV 941
Cdd:COG0365    364 pvpGY--------DVAVVD-EDGNPV-PPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGR---FPG--WYRTGDGARR 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  942 IQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEDVlsaKGISLpdasdeVGLVViaeLKDGK 1020
Cdd:COG0365    429 DEdGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE---AAVVGVPDEI---RGQVV------KAFVV---LKPGV 493

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721 1021 PVDKDIIKQIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRFEcLKQFVDG 1073
Cdd:COG0365    494 EPSDELAKELQAHVREE----LGPYA--YPREIEfvdelpKTRSGKIMRRL-LRKIAEG 545
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 615-1063 2.05e-38

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 150.71  E-value: 2.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  615 VGYHSAVRAGSVKNLISFTRKSAEstaqwpnLPWLHTDSWIKSSKVLpasnigsqseSQPDDLCFLQFTSGSTGDAKGVM 694
Cdd:cd05935     41 IAYFAIWRANAVVVPINPMLKERE-------LEYILNDSGAKVAVVG----------SELDDLALIPYTSGTTGLPKGCM 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  695 ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSplTFIRNPLlwLQTISDYKATHS-A 773
Cdd:cd05935    104 HTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA--RWDRETA--LELIEKYKVTFWtN 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  774 GPNFAFELVirrleaDKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpyGLSqevMAPGYGLAENcvfvgCAYGKK 853
Cdd:cd05935    180 IPTMLVDLL------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT---GLR---FVEGYGLTET-----MSQTHT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  854 KPILVdwQGRICCGYVdpnDADVDIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQKFPGRKYT 933
Cdd:cd05935    243 NPPLR--PKLQCLGIP---*FGVDARVIDIETGRELP-PNEVGEIVVRGPQIFKGYWNRPEETEESF----IEIKGRRFF 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  934 RTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEdvlsakgislPDASDEV-GLV 1011
Cdd:cd05935    313 RTGDLGyMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E---VCVISVPD----------ERVGEEVkAFI 379

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1012 VIAELKDGKPVDKDIIKQIESRvaeehgvtVASVKliRPRTIS------KTTSGKIKR 1063
Cdd:cd05935    380 VLRPEYRGKVTEEDIIEWAREQ--------MAAYK--YPREVEfvdelpRSASGKILW 427
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 527-1063 2.98e-37

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 148.61  E-value: 2.98e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPpdplqrggqALTKIE---NIA 603
Cdd:cd05926     16 TYADLAELVDDLARQL---AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP---------AYKKAEfefYLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  604 KLCNAVAILSTVGYHSAVRAGSVKNL-------ISFTRKSAESTAQWPNLPWLHTdswiksskvlpasNIGSQSESQPDD 676
Cdd:cd05926     84 DLGSKLVLTPKGELGPASRAASKLGLailelalDVGVLIRAPSAESLSNLLADKK-------------NAKSEGVPLPDD 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  677 LCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTS--NTVLVswLPQYHDMGLIGGLFTAMVCGGTAIL---FSPL 751
Cdd:cd05926    151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPddRTLVV--MPLFHVHGLVASLLSTLAAGGSVVLpprFSAS 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFirnpllWlQTISDYKAT-HSAGPNFaFELVIRRLEADKAKAHdydlSSMIFFMIAAEPVRQKTLKRfveltrpygLSQ 830
Cdd:cd05926    229 TF------W-PDVRDYNATwYTAVPTI-HQILLNRPEPNPESPP----PKLRFIRSCSASLPPAVLEA---------LEA 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMAP---GYGLAENCVFVGC---AYGKKKPILVdwqGRiccgyvdPNdaDVDIRIVDADTglEVDEDGKEGEIWISSPS 904
Cdd:cd05926    288 TFGAPvleAYGMTEAAHQMTSnplPPGPRKPGSV---GK-------PV--GVEVRILDEDG--EILPPGVVGEICLRGPN 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFrnklqkFPGRkYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PG 982
Cdd:cd05926    354 VTRGYLNNPEANAEAA------FKDG-WFRTGDLGYLDAdGYLFLTGRIKELINRGGEKISPLEVDGV------LLShPA 420

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  983 C--CAVISVPEDVLsakgislpdaSDEVGLVVIaeLKDGKPVDK-DIIKQIESRVAEehgVTVASvKLIRPRTISKTTSG 1059
Cdd:cd05926    421 VleAVAFGVPDEKY----------GEEVAAAVV--LREGASVTEeELRAFCRKHLAA---FKVPK-KVYFVDELPKTATG 484


                   ....
gi 1973708721 1060 KIKR 1063
Cdd:cd05926    485 KIQR 488
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 674-1073 1.22e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 147.26  E-value: 1.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLigGL-FTAMVCGGTAILfsPLT 752
Cdd:PRK06187   166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLpYLALMAGAKQVI--PRR 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FIRNPLLwlQTISDYKATHSAGPNFAFELVIRRLEAdkakaHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRpYGLSQev 832
Cdd:PRK06187   242 FDPENLL--DLIETERVTFFFAVPTIWQMLLKAPRA-----YFVDFSSLRLVIYGGAALPPALLREFKEKFG-IDLVQ-- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 mapGYGLAENCVFVGCAY-------GKKKPILvdwQGRICCGyvdpndadVDIRIVDADtGLEVDEDGKE-GEIWISSPS 904
Cdd:PRK06187   312 ---GYGMTETSPVVSVLPpedqlpgQWTKRRS---AGRPLPG--------VEARIVDDD-GDELPPDGGEvGEIIVRGPW 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRNklqkfpGrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKtvesssellrpgc 983
Cdd:PRK06187   377 LMQGYWNRPEATAETIDG------G--WLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYPRELED------------- 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  984 caVISVPEDVLSAKGISLPD-ASDEVGLVVIaELKDGKPVD-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------K 1055
Cdd:PRK06187   436 --ALYGHPAVAEVAVIGVPDeKWGERPVAVV-VLKPGATLDaKELRAFLRGRLA----------KFKLPKRIAfvdelpR 502

                          410
                   ....*....|....*...
gi 1973708721 1056 TTSGKIKRFECLKQFVDG 1073
Cdd:PRK06187   503 TSVGKILKRVLREQYAEG 520
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 527-1061 1.55e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 144.33  E-value: 1.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltSRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQ------RGGQALTKI- 599
Cdd:PRK08314    37 SYRELLEEAERLAGYL--QQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEelahyvTDSGARVAIv 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  600 -----ENIAKLCNAVAILSTV--GYHSAVRAGSVKNLISFTRKSAESTAQWPN--LPWLHTdswIKSSKVLPASNIGsqs 670
Cdd:PRK08314   115 gselaPKVAPAVGNLRLRHVIvaQYSDYLPAEPEIAVPAWLRAEPPLQALAPGgvVAWKEA---LAAGLAPPPHTAG--- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 esqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSp 750
Cdd:PRK08314   189 ---PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP- 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  751 ltfiRnpllW-----LQTISDYKATH-----------SAGPNFAfelvirrleadkakahDYDLSSMIFfmI----AAEP 810
Cdd:PRK08314   265 ----R----WdreaaARLIERYRVTHwtniptmvvdfLASPGLA----------------ERDLSSLRY--IggggAAMP 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  811 --VRQKTLKRFveltrpyGLS-QEvmapGYGLAENCVFVgcaygkkkpilvdwqgriccgYVDPNDA-----------DV 876
Cdd:PRK08314   319 eaVAERLKELT-------GLDyVE----GYGLTETMAQT---------------------HSNPPDRpklqclgiptfGV 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 DIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDL 955
Cdd:PRK08314   367 DARVIDPETLEELP-PGEVGEIVVHGPQVFKGYWNRPEATAEAF----IEIDGKRFFRTGDLGRMdEEGYFFITDRLKRM 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  956 IIVAGRNIYSADVEktvessSELLR-PgccavisvpeDVLSAKGISLPDA--SDEV-GLVVIAELKDGKPVDKDIIKQie 1031
Cdd:PRK08314   442 INASGFKVWPAEVE------NLLYKhP----------AIQEACVIATPDPrrGETVkAVVVLRPEARGKTTEEEIIAW-- 503

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1973708721 1032 srvAEEHgvtVASVKLirPRTIS------KTTSGKI 1061
Cdd:PRK08314   504 ---AREH---MAAYKY--PRIVEfvdslpKSGSGKI 531
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 674-1065 4.54e-34

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 135.48  E-value: 4.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMVCGGTAILFSPLTF 753
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVL-ACLTHGATMVFPSPSF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 irNPLLWLQTISDYKATHSAGPNFAFelvIRRLEADKAKahDYDLSSMIFFMIAAEPVRQKTLKRFVELtrpygLSQEVM 833
Cdd:cd05917     80 --DPLAVLEAIEKEKCTALHGVPTMF---IAELEHPDFD--KFDLSSLRTGIMAGAPCPPELMKRVIEV-----MNMKDV 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  834 APGYGLAENcvfvgcaygkkKPilVDWQGRIccgyVDPNDADV----------DIRIVDADTGlEVDEDGKEGEIWISSP 903
Cdd:cd05917    148 TIAYGMTET-----------SP--VSTQTRT----DDSIEKRVntvgrimphtEAKIVDPEGG-IVPPVGVPGELCIRGY 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  904 SAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesssELLrpg 982
Cdd:cd05917    210 SVMKGYWNDPEKTAEAIDGD-------GWLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIE-------EFL--- 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  983 ccavISVPeDVLSAKGISLPDAS--DEVGLVVIaeLKDG-KPVDKDIIKQIESRVAeEHGVtvasvklirPRTI------ 1053
Cdd:cd05917    273 ----HTHP-KVSDVQVVGVPDERygEEVCAWIR--LKEGaELTEEDIKAYCKGKIA-HYKV---------PRYVffvdef 335

                          410
                   ....*....|..
gi 1973708721 1054 SKTTSGKIKRFE 1065
Cdd:cd05917    336 PLTVSGKIQKFK 347
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 634-1065 4.23e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 134.36  E-value: 4.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  634 RKSAESTAQWPN-LPWlhtdSWIKSSKVLPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVkLMRRRY- 711
Cdd:PRK05605   181 KARAALTGPAPGtVPW----ETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWv 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  712 ---RSTSNTVLVSwLPQYHDMGLIGGLFTAMVCGGTAILF-SPltfiRNPLLwLQTISDYKATHSAG-PNfafelVIRRL 786
Cdd:PRK05605   256 pglGDGPERVLAA-LPMFHAYGLTLCLTLAVSIGGELVLLpAP----DIDLI-LDAMKKHPPTWLPGvPP-----LYEKI 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  787 eADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRpyGLSQEvmapGYGLAENC-VFVGCAYGK-KKPilvdwqgri 864
Cdd:PRK05605   325 -AEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTG--GLLVE----GYGLTETSpIIVGNPMSDdRRP--------- 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  865 ccGYVDPNDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRVIQ- 943
Cdd:PRK05605   389 --GYVGVPFPDTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD--------GWFRTGDVVVMEEd 458

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  944 GNLFITGRIKDLIIVAGRNIYSADVEktvesssELLR--PGCcavisvpEDVlSAKGISLPDASDEVGLVVIaeLKDGKP 1021
Cdd:PRK05605   459 GFIRIVDRIKELIITGGFNVYPAEVE-------EVLRehPGV-------EDA-AVVGLPREDGSEEVVAAVV--LEPGAA 521

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1022 VDKDIIKQiesrVAEEHgVTVASVklirPRTI------SKTTSGKIKRFE 1065
Cdd:PRK05605   522 LDPEGLRA----YCREH-LTRYKV----PRRFyhvdelPRDQLGKVRRRE 562
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 527-952 2.51e-31

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 128.92  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSRKptIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrGG--------QALT 597
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKA---------------GAayvpldpaYPAE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGYhsavragsvknlisftrksAESTAQWPNLPWLHTDSWIKSSKVLPASNiGSQSESQPDDL 677
Cdd:TIGR01733   63 RLAFILEDAGARLLLTDSAL-------------------ASRLAGLVLPVILLDPLELAALDDAPAPP-PPDAPSGPDDL 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMVCGGTAILFSPLTFIRNP 757
Cdd:TIGR01733  123 AYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  758 LLWLQTISDYKATHSAGPNFAFELVirrleadkAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELtrpygLSQEVMAPGY 837
Cdd:TIGR01733  202 ALLAALIAEHPVTVLNLTPSLLALL--------AAALPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLY 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  838 GLAENCVFVGCAYgkKKPILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQ 917
Cdd:TIGR01733  269 GPTETTVWSTATL--VDPDDAPRESPVPIGRPLAN---TRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTA 341

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1973708721  918 KTFRN--KLQKFPGRKYtRTGDLGRVI-QGNLFITGRI 952
Cdd:TIGR01733  342 ERFVPdpFAGGDGARLY-RTGDLVRYLpDGNLEFLGRI 378
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 526-1065 3.74e-31

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 129.04  E-value: 3.74e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  526 RTYAELDSNASCIAHKLLTSRkptIKPGDRVLlVHVPG-LDFVDSFFGCLRakvvpvpvlppdplqrggqaltkienIAK 604
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALG---VGPGDVVA-FQLPNwWEFAVLYLACLR--------------------------IGA 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  605 LCNAVailstvgyhsavragsvknLISFTRKSaestaqwpnLPWLHTDSwikSSKVL--PASNIGSQSESQPDDLCFLQF 682
Cdd:cd05903     52 VTNPI-------------------LPFFREHE---------LAFILRRA---KAKVFvvPERFRQFDPAAMPDAVALLLF 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  683 TSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSpltfIRNPLLWLQ 762
Cdd:cd05903    101 TSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALA 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  763 TISDYKATHSAG-PNFAFELVirrleaDKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYglsqevMAPGYGLAE 841
Cdd:cd05903    177 LMREHGVTFMMGaTPFLTDLL------NAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAK------VCSAYGSTE 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  842 NCvfvgCAYGKKKPILVDwqgRICC--GYVDPNdadVDIRIVDaDTGLEVDEdGKEGEIWISSPSAGIGYWGKEELsqkT 919
Cdd:cd05903    245 CP----GAVTSITPAPED---RRLYtdGRPLPG---VEIKVVD-DTGATLAP-GVEGELLSRGPSVFLGYLDRPDL---T 309

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  920 FRNklqkFPGRKYtRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGccavisvpedVLSAK 997
Cdd:cd05903    310 ADA----APEGWF-RTGDLARLDEdGYLRITGRSKDIIIRGGENIPVLEVE------DLLLGhPG----------VIEAA 368

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721  998 GISLPDA--SDEVGLVVIaeLKDGKPVDkdiikqIESRVAEEHGVTVASVKL-----IRPRtISKTTSGKIKRFE 1065
Cdd:cd05903    369 VVALPDErlGERACAVVV--TKSGALLT------FDELVAYLDRQGVAKQYWperlvHVDD-LPRTPSGKVQKFR 434
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 527-1063 4.65e-31

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 130.05  E-value: 4.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALT--------- 597
Cdd:cd05904     34 TYAELERRVRRLAAGL---AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL----------------GAVVTtanplstpa 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGYHSAVRAGSVKnLISFTRKSAESTAQWPNLPWLHTDSwiksskvLPASNIGsqsesqPDDL 677
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELAEKLASLALP-VVLLDSAEFDSLSFSDLLFEADEAE-------PPVVVIK------QDDV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTS---NTVLVSwLPQYHDMGLIGGLFTAMVCGGTAIL---FSPL 751
Cdd:cd05904    161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdseDVFLCV-LPMFHIYGLSSFALGLLRLGATVVVmprFDLE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNpllwlqtISDYKATH-SAGPNFAFELVirrleaDKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVEltrPYGLSQ 830
Cdd:cd05904    240 ELLAA-------IERYKVTHlPVVPPIVLALV------KSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRA---KFPNVD 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMapGYGLAE-NCVFVGCAYGKKKPILVDwqgriCCGYVDPNdadVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGY 909
Cdd:cd05904    304 LGQ--GYGMTEsTGVVAMCFAPEKDRAKYG-----SVGRLVPN---VEAKIVDPETG-ESLPPNQTGELWIRGPSIMKGY 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  910 WGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvesssELLrpgccavIS 988
Cdd:cd05904    373 LNNPEATAATIDKE-------GWLHTGDLCYIDEdGYLFIVDRLKELIKYKGFQVAPAELE-------ALL-------LS 431

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  989 VPEdVLSAKGISLPDasDEVGLVVIA--------ELKDgkpvdkdiiKQIESRVAEEhgvtVASVKLIRPRT----ISKT 1056
Cdd:cd05904    432 HPE-ILDAAVIPYPD--EEAGEVPMAfvvrkpgsSLTE---------DEIMDFVAKQ----VAPYKKVRKVAfvdaIPKS 495


                   ....*..
gi 1973708721 1057 TSGKIKR 1063
Cdd:cd05904    496 PSGKILR 502
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 674-1065 1.02e-30

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 128.10  E-value: 1.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGT-------AI 746
Cdd:cd05907     86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARiyfassaET 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 L------FSPLTFIRNPLLWlQTISDyKATHSAGPNFafelviRRLEADKAKahdydLSSMIFFMIAAEPVRQKTLKRFv 820
Cdd:cd05907    166 LlddlseVRPTVFLAVPRVW-EKVYA-AIKVKAVPGL------KRKLFDLAV-----GGRLRFAASGGAPLPAELLHFF- 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 eltrpYGLSQEVMApGYGLAENCVFVGCAygkkkpilVDWQGRI-CCGYVDPndaDVDIRIVDadtglevdedgkEGEIW 899
Cdd:cd05907    232 -----RALGIPVYE-GYGLTETSAVVTLN--------PPGDNRIgTVGKPLP---GVEVRIAD------------DGEIL 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  900 ISSPSAGIGYWGKEElsqKTfrnKLQKFPGRKYtRTGDLGRV-IQGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS-- 975
Cdd:cd05907    283 VRGPNVMLGYYKNPE---AT---AEALDADGWL-HTGDLGEIdEDGFLHITGRKKDLIITSgGKNISPEPIENALKASpl 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  976 -SELL-----RPGCCAVISVPEDVLS--AKGISLPDASDEVGLvviaelkdgkpVDKDIIKQIESRVAEE-HGVT-VASV 1045
Cdd:cd05907    356 iSQAVvigdgRPFLVALIVPDPEALEawAEEHGIAYTDVAELA-----------ANPAVRAEIEAAVEAAnARLSrYEQI 424

                          410       420
                   ....*....|....*....|....*..
gi 1973708721 1046 K----LIRPRTIS---KTTSGKIKRFE 1065
Cdd:cd05907    425 KkfllLPEPFTIEngeLTPTLKLKRPV 451
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 521-992 4.26e-29

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 123.02  E-value: 4.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVCQR---TYAELDSNASCIAHKLltsRKPTIKPGDRV-LLVHvPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQA- 595
Cdd:cd05930      5 AVVDGDqslTYAELDARANRLARYL---RERGVGPGDLVaVLLE-RSLEMVVAILAVLKA----------------GAAy 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  596 --------LTKIENIAKLCNAVAILStvgyhsavragsvknlisftrksaestaqwpnlpwlhtdswiksskvlpasnig 667
Cdd:cd05930     65 vpldpsypAERLAYILEDSGAKLVLT------------------------------------------------------ 90

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  668 sqsesQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMVCGGTAIL 747
Cdd:cd05930     91 -----DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVV 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 FSPLTfIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADkakahdyDLSSMIFFMIAAEPVRQKTLKRFVELTRPYG 827
Cdd:cd05930    165 LPEEV-RKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA-------ALPSLRLVLVGGEALPPDLVRRWRELLPGAR 236

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  828 LsqevmAPGYGLAENCVFVGCAYGKKKPILVDwqgRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGI 907
Cdd:cd05930    237 L-----VNLYGPTEATVDATYYRVPPDDEEDG---RVPIGRPIPN---TRVYVLDEN--LRPVPPGVPGELYIGGAGLAR 303

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  908 GYWGKEELSQKTFRNkLQKFPGRKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAV 986
Cdd:cd05930    304 GYLNRPELTAERFVP-NPFGPGERMYRTGDLVRWLPdGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE---AAV 379


                   ....*.
gi 1973708721  987 ISVPED 992
Cdd:cd05930    380 VAREDG 385
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 676-1065 8.45e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 122.01  E-value: 8.45e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL---FSPLT 752
Cdd:cd05934     82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlprFSASR 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FirnpllWLQtISDYKATHSAGPNFAFELVIRRLEADKAKAHDYDLssmIFFMIAAEPVRQKTLKRFveltrpyGLsqeV 832
Cdd:cd05934    162 F------WSD-VRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA---AYGAPNPPELHEEFEERF-------GV---R 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAENCVFVGCAYGKKKPILvdwqgriCCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWI-SSPSAGI--GY 909
Cdd:cd05934    222 LLEGYGMTETIVGVIGPRDEPRRPG-------SIGRPAP---GYEVRIVDDD-GQEL-PAGEPGELVIrGLRGWGFfkGY 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  910 WGKEELSQKTFRNklqkfpgrKYTRTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIS 988
Cdd:cd05934    290 YNMPEATAEAMRN--------GWFHTGDLGyRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE---AAVVA 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  989 VPEDVlsakgislpdASDEVGLVVIaeLKDGKPVD-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKI 1061
Cdd:cd05934    359 VPDEV----------GEDEVKAVVV--LRPGETLDpEELFAFCEGQLA----------YFKVPRYIRfvddlpKTPTEKV 416


                   ....
gi 1973708721 1062 KRFE 1065
Cdd:cd05934    417 AKAQ 420
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 527-1063 1.87e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 122.32  E-value: 1.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALTKIENIAKLC 606
Cdd:PRK07656    32 TYAELNARVRRAAAALAAL---GIGKGDRVAIWAPNSPHWVIAALGALKA----------------GAVVVPLNTRYTAD 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTVG--------------YHSAVRAGSVKNLISFtrksaESTAQWPNLPWLHT-DSWIKSSKVLPASNigsqsE 671
Cdd:PRK07656    93 EAAYILARGDakalfvlglflgvdYSATTRLPALEHVVIC-----ETEEDDPHTEKMKTfTDFLAAGDPAERAP-----E 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL---F 748
Cdd:PRK07656   163 VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPlpvF 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTFirnpllwLQTISDYKATHSAGP----NFAFelvirrleaDKAKAHDYDLSSMIFFMI--AAEPVRqkTLKRFVEL 822
Cdd:PRK07656   243 DPDEV-------FRLIETERITVLPGPptmyNSLL---------QHPDRSAEDLSSLRLAVTgaASMPVA--LLERFESE 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 trpygLSQEVMAPGYGLAEnCVFVGC---AYGKKKPIlvdwqgricCGYVDPNDADVDIRIVDADtGLEVdEDGKEGEIW 899
Cdd:PRK07656   305 -----LGVDIVLTGYGLSE-ASGVTTfnrLDDDRKTV---------AGTIGTAIAGVENKIVNEL-GEEV-PVGEVGELL 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  900 ISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseL 978
Cdd:PRK07656   368 VRGPNVMKGYYDDPEATAAAIDAD-------GWLHTGDLGRLDEeGYLYIVDRKKDMFIVGGFNVYPAEVEEV------L 434

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  979 LR-PGC--CAVISVPEDVLSakgislpdasdEVG--LVViaeLKDGKPVD-KDIIKQIESRVAeehgvtvasvKLIRPRT 1052
Cdd:PRK07656   435 YEhPAVaeAAVIGVPDERLG-----------EVGkaYVV---LKPGAELTeEELIAYCREHLA----------KYKVPRS 490

                          570
                   ....*....|....*..
gi 1973708721 1053 IS------KTTSGKIKR 1063
Cdd:PRK07656   491 IEfldelpKNATGKVLK 507
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 521-994 3.68e-28

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 121.79  E-value: 3.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLLtsrKPTIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrgG--- 593
Cdd:COG1021     43 AVVDgerRLSYAELDRRADRLAAGLL---ALGLRPGDRVV-VQLPnVAEFVIVFFALFRA----------------Gaip 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  594 -QAL-----TKIENIAKLCNAVAILST--------VGYHSAVRAG--SVKNLISftrksAESTAQWPNLpwlhtDSWIKS 657
Cdd:COG1021    103 vFALpahrrAEISHFAEQSEAVAYIIPdrhrgfdyRALARELQAEvpSLRHVLV-----VGDAGEFTSL-----DALLAA 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  658 skvlPASniGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLF 736
Cdd:COG1021    173 ----PAD--LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMVCGGTAIL---FSPLTFIrnPLlwlqtISDYKATHSA-GPnfafELVIRRLEAdkAKAHDYDLSSMIFFMI-----A 807
Cdd:COG1021    247 GVLYAGGTVVLapdPSPDTAF--PL-----IERERVTVTAlVP----PLALLWLDA--AERSRYDLSSLRVLQVggaklS 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  808 AEPVRQktlkrfVELTRPYGLsQEVmapgYGLAE---NCVFVGcaygkkKP--ILVDWQGR-ICcgyvdPNDadvDIRIV 881
Cdd:COG1021    314 PELARR------VRPALGCTL-QQV----FGMAEglvNYTRLD------DPeeVILTTQGRpIS-----PDD---EVRIV 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  882 DaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpGrkYTRTGDLGRVIQ-GNLFITGRIKDLIIVAG 960
Cdd:COG1021    369 D-EDGNPV-PPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD-----G--FYRTGDLVRRTPdGYLVVEGRAKDQINRGG 439

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1973708721  961 RNIYSADVEktvessSELLR-PGC--CAVISVPEDVL 994
Cdd:COG1021    440 EKIAAEEVE------NLLLAhPAVhdAAVVAMPDEYL 470
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 672-1064 5.73e-28

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 120.24  E-value: 5.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILF--- 748
Cdd:cd05914     86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdki 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 -------------SPLTFIRNPLLWLQTISDYKATHSAGPNFAFELVI-----RRLEADKAKAHDYDLSSMIFFMIAAEP 810
Cdd:cd05914    166 psakiialafaqvTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKkinnrKIRKLAFKKVHEAFGGNIKEFVIGGAK 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  811 VRQKTLKRFVELTRPYglsqevmAPGYGLAENCVFVgcAYGKKKPILVDwqgriCCGYVDPNdadVDIRIVDADTGLEvd 890
Cdd:cd05914    246 INPDVEEFLRTIGFPY-------TIGYGMTETAPII--SYSPPNRIRLG-----SAGKVIDG---VEVRIDSPDPATG-- 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  891 edgkEGEIWISSPSAGIGYWGKEELSQktfrnklQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIV-AGRNIYSADV 968
Cdd:cd05914    307 ----EGEIIVRGPNVMKGYYKNPEATA-------EAFDKDGWFHTGDLGKiDAEGYLYIRGRKKEMIVLsSGKNIYPEEI 375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  969 EKTVESSSELLRpgccAVISVPEDVLSAKGISLPDASDEVGLVViaelkdgkpvdKDIIKQIESRVAEEHGVTVASVK-- 1046
Cdd:cd05914    376 EAKINNMPFVLE----SLVVVQEKKLVALAYIDPDFLDVKALKQ-----------RNIIDAIKWEVRDKVNQKVPNYKki 440

                          410       420
                   ....*....|....*....|.
gi 1973708721 1047 ---LIRPRTISKTTSGKIKRF 1064
Cdd:cd05914    441 skvKIVKEEFEKTPKGKIKRF 461
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 527-994 6.31e-27

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 116.62  E-value: 6.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSRKptIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQALTkieniaklc 606
Cdd:cd05941     13 TYADLVARAARLANRLLALGK--DLRGDRVAFLAPPSAEYVVAQLAIWRA---------------GGVAVP--------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 navaiLSTvgyhsavragsvknliSFTRKSAEstaqwpnlpWLHTDSwiKSSKVLpasnigsqsesqpdDLCFLQFTSGS 686
Cdd:cd05941     67 -----LNP----------------SYPLAELE---------YVITDS--EPSLVL--------------DPALILYTSGT 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  687 TGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL---FSPLT----------- 752
Cdd:cd05941    101 TGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFlpkFDPKEvaisrlmpsit 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 -FIRNPLLWLQTISDYKAtHSAGPNFAFELVIRRLEadkakahdydlssmifFMI---AAEPVrqKTLKRFVELT----- 823
Cdd:cd05941    181 vFMGVPTIYTRLLQYYEA-HFTDPQFARAAAAERLR----------------LMVsgsAALPV--PTLEEWEAITghtll 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  824 -RpYGLSQEVMAPGYGLAencvfvgcayGKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDEdGKEGEIWISS 902
Cdd:cd05941    242 eR-YGMTEIGMALSNPLD----------GERRP-----------GTVGMPLPGVQARIVDEETGEPLPR-GEVGEIQVRG 298

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  903 PSAGIGYWGKEELSQKTFRnklqkfpGRKYTRTGDLGRV-IQGNLFITGRIKDLII-VAGRNIYSADVEKTVESssellR 980
Cdd:cd05941    299 PSVFKEYWNKPEATKEEFT-------DDGWFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLA-----H 366

                          490
                   ....*....|....*.
gi 1973708721  981 PGC--CAVISVPEDVL 994
Cdd:cd05941    367 PGVseCAVIGVPDPDW 382
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1246-1704 1.86e-26

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 117.93  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1246 LVFPAYLSVSAFQILVVASqklidGLPWLHHTsvvlLAPLFWILCIALTSISIAFFGNSFLRINYA------LTPEV-SV 1318
Cdd:TIGR02353    5 LQLIPIVTLSGLQWLAPLL-----GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1319 WSVDFVKWWALYKAQEVSSKVLavhLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHE 1396
Cdd:TIGR02353   76 WGSTYLRFWTVKRLVDAAPTVL---LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1397 VRNSVLRFQPIRIGRNCSVGPYAVIQKGSVLGEGAEVLALQKSEGGKSVlkmtKAENILKVSPGslKETIQQFMGIYMVG 1476
Cdd:TIGR02353  151 AERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSI----PDGERWHGSPA--QKTGADYRKVQPAR 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1477 LVSSLSATAVFLLymrLSQKVPSLEQLAFLCISGAlhwvpFTIVAYATMFTNTLPNPFEFAISLATAYFAHGLVLSLLTS 1556
Cdd:TIGR02353  225 PYTVRRRLYVAGA---LFVVFVLLPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1557 IFTNLLAS---KEKKTQTHikTWLGHRL----AVACHLRFAKLLSG-TEAFCMYLHLLGAKVGKYCSIRSINpVADPRMV 1628
Cdd:TIGR02353  297 AAVRLLLNlvlKPGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLT 373

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1629 SIGAGVHLGDfsRIMTGFYSQSGYI--QSNVHVKDNSVIGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1704
Cdd:TIGR02353  374 DIGEETFIAD--GLLMGNARLSGGWfrLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
674-993 1.89e-26

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 116.69  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK--------LMRRRYRstsntVLVSWLPQYHDMGLIGGLFTAMVCGGTA 745
Cdd:PRK08974   205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqakaaygpLLHPGKE-----LVVTALPLYHIFALTVNCLLFIELGGQN 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  746 ILfspltfIRNPL---LWLQTISDYKATHSAGPNFAFELVIRRLEadkakAHDYDLSSMIFFMIAAEPVRQKTLKRFVEL 822
Cdd:PRK08974   280 LL------ITNPRdipGFVKELKKYPFTAITGVNTLFNALLNNEE-----FQELDFSSLKLSVGGGMAVQQAVAERWVKL 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSqevmapGYGLAENCVFV-GCAYGkkkpiLVDWQGRIccGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWIS 901
Cdd:PRK08974   349 TGQYLLE------GYGLTECSPLVsVNPYD-----LDYYSGSI--GLPVPS---TEIKLVD-DDGNEV-PPGEPGELWVK 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  902 SPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLR 980
Cdd:PRK08974   411 GPQVMLGYWQRPEATDEVIKD--------GWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482

                          330
                   ....*....|...
gi 1973708721  981 pgcCAVISVPEDV 993
Cdd:PRK08974   483 ---VAAVGVPSEV 492
catalase_like cd08150
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 1749-2051 2.61e-26

Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.


Pssm-ID: 163706  Cd Length: 283  Bit Score: 111.11  E-value: 2.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1749 RYFHRIGVSGKGYLKLYDDIQGLPEHNIFGPGKKYTVIVRHSNSLSADDDARlDARGAALRiLSDEkgDDSPLLDLTLKT 1828
Cdd:cd08150      3 RGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKP-DIRGFAIK-FTGV--ADAGTLDFVLNN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1829 GKAFYARTISDFATWLV---------CGLAAREEHVKRVPH-VRDAVWTSLRQADSYAEMHYYSNICRLFRFKDGQEMYV 1898
Cdd:cd08150     79 TPVFFIRNTSDYEDFVAefarsargePPLDFIAWYVEKRPEdLPNLLGARSQVPDSYAAARYFSQVTFAFINGAGKYRVV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1899 KFKLRPSDKNIGEDTGKVEpsgilppetgaiprdandTRPLLFLAEDFQNRV-KSPngVRYIFQLQVMPvPQDEAARDia 1977
Cdd:cd08150    159 RSKDNPVDGIPSLEDHELE------------------ARPPDYLREELTERLqRGP--VVYDFRIQLND-DTDATTID-- 215

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721 1978 lDCTKPWDESQfPYIDVGEVIINENLTKEGSERLEFNPFLRCHEVDVIRATSssqsaSIDHGRSLVYEICQHLR 2051
Cdd:cd08150    216 -NPTILWPTEH-PVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLG-----PILEVRRRVYTSSQGLR 282
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 521-952 4.32e-26

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 118.04  E-value: 4.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVCQR---TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGG---- 593
Cdd:COG1020    494 AVVFGDqslTYAELNARANRLAHHL---RALGVGPGDLVGVCLERSLEMVVALLAVLKA---------------GAayvp 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  594 ----QALTKIENIAKLCNAVAILSTVGYHSAVRAGSVknlisftrksaestaqwpnlPWLHTDSWIKSSkvLPASNIgsQ 669
Cdd:COG1020    556 ldpaYPAERLAYMLEDAGARLVLTQSALAARLPELGV--------------------PVLALDALALAA--EPATNP--P 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMVCGGTAILFS 749
Cdd:COG1020    612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLVLAP 690

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PLTfIRNPLLWLQTISDYKATHSagpNF---AFELVirrLEADKAkahdyDLSSMIFFMIAAEPVRQKTLKRFVELtrpy 826
Cdd:COG1020    691 PEA-RRDPAALAELLARHRVTVL---NLtpsLLRAL---LDAAPE-----ALPSLRLVLVGGEALPPELVRRWRAR---- 754

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 gLSQEVMAPGYGLAENCVFVgCAYgkkkPILVD--WQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPS 904
Cdd:COG1020    755 -LPGARLVNLYGPTETTVDS-TYY----EVTPPdaDGGSVPIGRPIAN---TRVYVLDAH--LQPVPVGVPGELYIGGAG 823

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1973708721  905 AGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGRVI-QGNLFITGRI 952
Cdd:COG1020    824 LARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLpDGNLEFLGRA 872
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 673-990 1.37e-25

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 113.20  E-value: 1.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGtAILFSPlt 752
Cdd:cd05909    145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHP-- 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 firNPLLWLQ---TISDYKATHSAG-PNFaFELVIRRleadkakAHDYDLSSMIFFMIAAE----PVRQKTLKRFVelTR 824
Cdd:cd05909    222 ---NPLDYKKipeLIYDKKATILLGtPTF-LRGYARA-------AHPEDFSSLRLVVAGAEklkdTLRQEFQEKFG--IR 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  825 PYglsqevmaPGYGLAENCVFVGCaygkKKPILVDWQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKEGEIWISSPS 904
Cdd:cd05909    289 IL--------EGYGTTECSPVISV----NTPQSPNKEG--TVGRPLPG---MEVKIVSVETHEEVPI-GEGGLLLVRGPN 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFrnklqkfpGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvESSSELLRP-G 982
Cdd:cd05909    351 VMLGYLNEPELTSFAF--------GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIE---DILSEILPEdN 419


                   ....*...
gi 1973708721  983 CCAVISVP 990
Cdd:cd05909    420 EVAVVSVP 427
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 674-992 8.95e-25

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 110.03  E-value: 8.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAILFsPLTF 753
Cdd:cd05945     96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPV-PRDA 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 IRNPLLWLQTISDYKAT--HSAgPNFAfELVIRRlEADKAKAhdydLSSMIFFMIAAEPVRQKTLKRFVEL---TRPYGL 828
Cdd:cd05945    174 TADPKQLFRFLAEHGITvwVST-PSFA-AMCLLS-PTFTPES----LPSLRHFLFCGEVLPHKTARALQQRfpdARIYNT 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sqevmapgYGLAENCvfVGCAYGKKKPILVDWQGRICCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIG 908
Cdd:cd05945    247 --------YGPTEAT--VAVTYIEVTPEVLDGYDRLPIGYAKP---GAKLVILDED-GRPV-PPGEKGELVISGPSVSKG 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWGKEELSQKTFRnklqKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCAVI 987
Cdd:cd05945    312 YLNNPEKTAAAFF----PDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV---KEAVVV 384


                   ....*
gi 1973708721  988 SVPED 992
Cdd:cd05945    385 PKYKG 389
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 526-1064 2.95e-24

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 109.38  E-value: 2.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  526 RTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALTkiENIAK- 604
Cdd:cd05959     30 LTYAELEAEARRVAGAL---RALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLE--DSRARv 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  605 LCNAVAILSTVGYHSAVRAGSVKNLISFTRKSAESTAQWpnlpwlHTDSWIKSSKVLPASNigsqseSQPDDLCFLQFTS 684
Cdd:cd05959    105 VVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALL------LAELVAAEAEQLKPAA------THADDPAFWLYSS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  685 GSTGDAKGVMITHGGLIHNVKLMRRR-YRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFS--PltfirNPLLWL 761
Cdd:cd05959    173 GSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPerP-----TPAAVF 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  762 QTISDYKATHSAG-PNFAFELvirrLEADKAKahDYDLSSMIFFMIAAEPVRQKTLKRFvelTRPYGLSqevMAPGYGLA 840
Cdd:cd05959    248 KRIRRYRPTVFFGvPTLYAAM----LAAPNLP--SRDLSSLRLCVSAGEALPAEVGERW---KARFGLD---ILDGIGST 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  841 ENC-VFVGCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKT 919
Cdd:cd05959    316 EMLhIFLSNRPGRVRY---GTTGKPVPGY--------EVELRD-EDGGDV-ADGEPGELYVRGPSSATMYWNNRDKTRDT 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  920 FRNklqkfpgrKYTRTGD-LGRVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEDVlsakG 998
Cdd:cd05959    383 FQG--------EWTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGVEDED----G 447

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721  999 ISLPDAsdevgLVVIAELKDGKPVDKDIIKQ-IESRvaeehgvtVASVKliRPRTI------SKTTSGKIKRF 1064
Cdd:cd05959    448 LTKPKA-----FVVLRPGYEDSEALEEELKEfVKDR--------LAPYK--YPRWIvfvdelPKTATGKIQRF 505
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 675-1065 5.82e-24

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 107.55  E-value: 5.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLtf 753
Cdd:cd05919     91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW-- 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 iRNPLLWLQTISDYKATHSAG-PNFafelvIRRLEADKAKAHDyDLSSMIFFMIAAEPVrqktlkrfveltrPYGLSQEV 832
Cdd:cd05919    169 -PTAERVLATLARFRPTVLYGvPTF-----YANLLDSCAGSPD-ALRSLRLCVSAGEAL-------------PRGLGERW 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MA-------PGYGLAENC-VFVGCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPS 904
Cdd:cd05919    229 MEhfggpilDGIGATEVGhIFLSNRPGAWRL---GSTGRPVPGY--------EIRLVD-EEGHTI-PPGEEGDLLVRGPS 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRNKLQKfPGRKYTRTGDlgrviqGNLFITGRIKDLIIVAGRNIYSADVEKTVesssellrpgcC 984
Cdd:cd05919    296 AAVGYWNNPEKSRATFNGGWYR-TGDKFCRDAD------GWYTHAGRADDMLKVGGQWVSPVEVESLI-----------I 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  985 AVISVPEDVLsakgISLPDASDEVGLVVIAELKDGKPVDKDIIKQIESRVAEehgvTVASVKliRPRTIS------KTTS 1058
Cdd:cd05919    358 QHPAVAEAAV----VAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLE----RLSAHK--VPRRIAfvdelpRTAT 427


                   ....*..
gi 1973708721 1059 GKIKRFE 1065
Cdd:cd05919    428 GKLQRFK 434
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 527-1010 7.83e-24

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 107.01  E-value: 7.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALTKIENIAKLC 606
Cdd:cd17653     24 TYGELDAASNALANRL---LQLGVVPGDVVPLLSDRSLEMLVAILAILKA----------------GAAYVPLDAKLPSA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILSTVGyhsavragsvKNLISFTrksaestaqwpnlpwlhtdswiksskvlpasnigsqseSQPDDLCFLQFTSGS 686
Cdd:cd17653     85 RIQAILRTSG----------ATLLLTT--------------------------------------DSPDDLAYIIFTSGS 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  687 TGDAKGVMITHGGLIHNVKLMRRRYRST-SNTVLvswlpQYHDMGL---IGGLFTAMVCGGTAILfspltfiRNPLLWLQ 762
Cdd:cd17653    117 TGIPKGVMVPHRGVLNYVSQPPARLDVGpGSRVA-----QVLSIAFdacIGEIFSTLCNGGTLVL-------ADPSDPFA 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  763 TISDYKATHSAGPNFAFELvirrleadkaKAHDYDLSSMIFFmiAAEPVRQKTLKRFVELTRPYGlsqevmapGYGLAEn 842
Cdd:cd17653    185 HVARTVDALMSTPSILSTL----------SPQDFPNLKTIFL--GGEAVPPSLLDRWSPGRRLYN--------AYGPTE- 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  843 CVfVGCAYGKKKPIlvdwqGRICCGYVDPNdadVDIRIVDADTgLEVDEdGKEGEIWISSPSAGIGYWGKEELSQKTFRN 922
Cdd:cd17653    244 CT-ISSTMTELLPG-----QPVTIGKPIPN---STCYILDADL-QPVPE-GVVGEICISGVQVARGYLGNPALTASKFVP 312

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  923 kLQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPgccAVISVPEDVLSAkgISL 1001
Cdd:cd17653    313 -DPFWPGSRMYRTGDYGRwTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQ---AAAIVVNGRLVA--FVT 386


                   ....*....
gi 1973708721 1002 PDASDEVGL 1010
Cdd:cd17653    387 PETVDVDGL 395
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
527-1065 1.69e-23

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 107.53  E-value: 1.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSrkpTIKPGDRVLLvHVPGL-DFVDSFFGCLRAKVVPVPVLPPDplqrGGQALTKIENiakL 605
Cdd:PRK06087    51 TYSALDHAASRLANWLLAK---GIEPGDRVAF-QLPGWcEFTIIYLACLKVGAVSVPLLPSW----REAELVWVLN---K 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  606 CNAVAILSTVGYHSavragsvknlISFTRKSAESTAQWPNL-PWLHTDSWIKSSKVLPASNIGSQSES-------QPDDL 677
Cdd:PRK06087   120 CQAKMFFAPTLFKQ----------TRPVDLILPLQNQLPQLqQIVGVDKLAPATSSLSLSQIIADYEPlttaittHGDEL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSpltfIRNP 757
Cdd:PRK06087   190 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD----IFTP 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  758 LLWLQTISDYKATHSAGPN-FAFELvIRRLEADKakahdYDLSSMIFFMIAAEPVRqktlKRFVELTRPYGLsqeVMAPG 836
Cdd:PRK06087   266 DACLALLEQQRCTCMLGATpFIYDL-LNLLEKQP-----ADLSALRFFLCGGTTIP----KKVARECQQRGI---KLLSV 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  837 YGLAENCVFVGCAYGKKKPILVDWQGRICCGyvdpndadVDIRIVDADTGlEVDEdGKEGEIWISSPSAGIGYWGKEELS 916
Cdd:PRK06087   333 YGSTESSPHAVVNLDDPLSRFMHTDGYAAAG--------VEIKVVDEARK-TLPP-GCEGEEASRGPNVFMGYLDEPELT 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  917 QKTFRNKlqkfpGRKYtrTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVISVPEDVLS 995
Cdd:PRK06087   403 ARALDEE-----GWYY--SGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDIL---LQHPKIHDACVVAMPDERLG 472

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721  996 AKGISlpdasdevgLVVIAElKDGKPVDKDII-----KQIESRVAEEHGVTVASvklirprtISKTTSGKIKRFE 1065
Cdd:PRK06087   473 ERSCA---------YVVLKA-PHHSLTLEEVVaffsrKRVAKYKYPEHIVVIDK--------LPRTASGKIQKFL 529
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 670-1063 2.39e-23

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 105.61  E-value: 2.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAILFS 749
Cdd:TIGR01923  106 ASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVD 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PLTFIrnpllwLQTISDYKATH-SAGPNfafeLVIRRLEADkakAHDYDLSSmifFMIAAEPVRQKTLKRFVELTRPYGL 828
Cdd:TIGR01923  185 KFNQL------LEMIANERVTHiSLVPT----QLNRLLDEG---GHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYL 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sqevmapGYGLAENCVFVgCAygkkKPILVDwQGRICCGYVDPNdadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIG 908
Cdd:TIGR01923  249 -------SYGMTETCSQV-TT----ATPEML-HARPDVGRPLAG---REIKI-------KVDNKEGHGEIMVKGANLMKG 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWGKEELSQKTFRNklqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEllrpgccavi 987
Cdd:TIGR01923  306 YLYQGELTPAFEQQ--------GWFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPG---------- 367

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721  988 sVPEDVLSAKgislPDAsdEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTVASVKLirpRTISKTTSGKIKR 1063
Cdd:TIGR01923  368 -IQEAVVVPK----PDA--EWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKL---DELPYNASGKILR 433
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 648-1063 3.64e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 105.60  E-value: 3.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  648 WLHTDSWIKSSKVLPASnigsqsESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYH 727
Cdd:cd05922     96 VLDADGIRAARASAPAH------EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  728 DMGLiGGLFTAMVCGGTAILFS----PLTFIRnpllwlqTISDYKATHSAGPNFAFELvIRRLEADKAKahdydLSSMIF 803
Cdd:cd05922    170 DYGL-SVLNTHLLRGATLVLTNdgvlDDAFWE-------DLREHGATGLAGVPSTYAM-LTRLGFDPAK-----LPSLRY 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  804 FMIAAEPVRQKTLKRFVELTRpyGLSQEVMapgYGLAEncVFVGCAY-----GKKKPilvdwqGRICCGYvdPNDAdvdI 878
Cdd:cd05922    236 LTQAGGRLPQETIARLRELLP--GAQVYVM---YGQTE--ATRRMTYlpperILEKP------GSIGLAI--PGGE---F 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  879 RIVDADTGLEvdEDGKEGEIWISSPSAGIGYWGKEElsqktFRNKLQKFPGRKYtrTGDLGRVIQ-GNLFITGRIKDLII 957
Cdd:cd05922    298 EILDDDGTPT--PPGEPGEIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH--TGDLARRDEdGFLFIVGRRDRMIK 368

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  958 VAGRNIYSADVEKTVESSSELlrpGCCAVISVPedvlsakgislPDASDEVGLVVIAELKDgkpVDKDIIkqiesRVAEE 1037
Cdd:cd05922    369 LFGNRISPTEIEAAARSIGLI---IEAAAVGLP-----------DPLGEKLALFVTAPDKI---DPKDVL-----RSLAE 426

                          410       420
                   ....*....|....*....|....*..
gi 1973708721 1038 HGVTVASVKLIRP-RTISKTTSGKIKR 1063
Cdd:cd05922    427 RLPPYKVPATVRVvDELPLTASGKVDY 453
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
673-1036 4.36e-23

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 106.72  E-value: 4.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMVCGGT-AILFSPL 751
Cdd:COG1022    181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-ALAAGATvAFAESPD 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRN------------PLLW---LQTISDyKATHSAGP-----NFAFELVIRRLEA----------DKAKAHDYDLssM 801
Cdd:COG1022    260 TLAEDlrevkptfmlavPRVWekvYAGIQA-KAEEAGGLkrklfRWALAVGRRYARArlagkspsllLRLKHALADK--L 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  802 IFfmiaaEPVRQKT---LKRFV--------ELTRPY---GLsqeVMAPGYGLAENCVFVgCAYGKKKPIL--VdwqGRIC 865
Cdd:COG1022    337 VF-----SKLREALggrLRFAVsggaalgpELARFFralGI---PVLEGYGLTETSPVI-TVNRPGDNRIgtV---GPPL 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  866 CGyvdpndadVDIRIvdadtglevdedGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqkfpgrkyT-----RTGDLGR 940
Cdd:COG1022    405 PG--------VEVKI------------AEDGEILVRGPNVMKGYYKNPEATAEAF------------DadgwlHTGDIGE 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  941 VI-QGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---SELL-----RPGCCAVISVPEDVL----SAKGISLPDASD 1006
Cdd:COG1022    453 LDeDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASpliEQAVvvgdgRPFLAALIVPDFEALgewaEENGLPYTSYAE 532

                          410       420       430
                   ....*....|....*....|....*....|
gi 1973708721 1007 EVGlvviaelkdgkpvDKDIIKQIESRVAE 1036
Cdd:COG1022    533 LAQ-------------DPEVRALIQEEVDR 549
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1232-1688 1.74e-22

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 105.22  E-value: 1.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1232 WSFQLLALLYVSFILVFPAYLSVSAFQILVVASQKLIDGLPWLHHTSVVLLAPLFWILCIALTSISIAFFGNSFLRINYA 1311
Cdd:TIGR02353  231 RLYVAGALFVVFVLLPPLAFLFAIPVAITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNLVLKPG 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1312 LTPEVSvWSvdfvkWWALYKAQEV--SSKVLAVHLRGTVFLKHWFEMLGARIGSSVLLDTVDITDPSLVSIGDGAVIAEG 1389
Cdd:TIGR02353  311 RYYVHS-GF-----YYQAWTVQQLmdNSRVLLFPLYASSYIPHWYRALGAKIGKVAEISSAQHEVPDLTDIGEETFIADG 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1390 ALLQSHEVRNSVLRFQPIRIGRNCSVGPYAVIQKGSVLGEGaeVLALQKSEGGKSVlKMTKAENILKVSPGSLKETIQ-- 1467
Cdd:TIGR02353  385 LLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDN--VLLGVLSMTPKDG-KVREGVGWLGSPPFELPRRVNrd 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1468 ----------QFMGIYMVGLVSSLSATAVFLLYMRLSQKVPSLEQLAFLCISGALHWVPFTiVAYATMFTNTLPnpfeFA 1537
Cdd:TIGR02353  462 delealtfepDPRRRLARKNVENLRIILPFLLVQWAMLFALVVLDLQALDDYTEWGAVALL-AALILMAVGVGA----FL 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1538 ISLATAYFAHGLVLSLLTSIFTNLLASKEKKTQTHIKtwlghrLAVAchlRFAKLLSGTEAFCMYLHLLGAKVGKYCSIR 1617
Cdd:TIGR02353  537 ILVERKWLVFGRLKPQEHPLWSPFVWLHELHWKLYES------VAVP---NFLRPFRGTPFLPAILRLLGVKIGRGVYID 607

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721 1618 SINpVADPRMVSIGAGVHLGDFSRIMTGFYSQSGYIQSNVHVKDNSVIGSQSLILPGSVVEKDVILGAISV 1688
Cdd:TIGR02353  608 GTD-LTERDLVTIGDDSTLNEGSVIQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 521-1063 2.57e-22

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 103.47  E-value: 2.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgG---- 593
Cdd:PRK08316    29 ALVFgdrSWTYAELDAAVNRVAAALLDL---GLKKGDRVAALGHNSDAYALLWLACARA----------------Gavhv 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  594 ---QALTK--IENIAKLCNAVAILSTVGYHSAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKSskvlpasniGS 668
Cdd:PRK08316    90 pvnFMLTGeeLAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEA---------GS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSESQP----DDLCFLQFTSGSTGDAKGVMITHGGLIHNvklmrrrYRST-------SNTVLVSWLPQYHDMGLIGGLFT 737
Cdd:PRK08316   161 VAEPDVeladDDLAQILYTSGTESLPKGAMLTHRALIAE-------YVSCivagdmsADDIPLHALPLYHCAQLDVFLGP 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  738 AMVCGGTAILF-SPltfirNPLLWLQTISDYKATHSagpnFAFELV----IRRLEADKakahdYDLSSM--IFF--MIAA 808
Cdd:PRK08316   234 YLYVGATNVILdAP-----DPELILRTIEAERITSF----FAPPTVwislLRHPDFDT-----RDLSSLrkGYYgaSIMP 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  809 EPVRQKTLKRF--VELTRPYGlsQEVMAPgygLA------ENCVFVGCAygkKKPILvdwqgriccgyvdpndaDVDIRI 880
Cdd:PRK08316   300 VEVLKELRERLpgLRFYNCYG--QTEIAP---LAtvlgpeEHLRRPGSA---GRPVL-----------------NVETRV 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  881 VDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVA 959
Cdd:PRK08316   355 VDDD-GNDV-APGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG--------GWFHSGDLGVMdEEGYITVVDRKKDMIKTG 424

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  960 GRNIYSADVEKTV---ESSSELlrpgccAVISVPEDvlsaKGIslpdasDEVGLVVIaeLKDGKPVDKD-IIKQIESRva 1035
Cdd:PRK08316   425 GENVASREVEEALythPAVAEV------AVIGLPDP----KWI------EAVTAVVV--PKAGATVTEDeLIAHCRAR-- 484

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1973708721 1036 eehgvtVASVKliRPRTI------SKTTSGKI-KR 1063
Cdd:PRK08316   485 ------LAGFK--VPKRVifvdelPRNPSGKIlKR 511
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 682-1063 8.22e-22

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 99.26  E-value: 8.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  682 FTSGSTGDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLfTAMVCGGTAILFSPLTFIRNPLLW 760
Cdd:cd17635      8 FTSGTTGEPKAVLLANKTFFaVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTTYKSLFKI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  761 LQTisdYKATHSA-GPNFAFELVirrLEADKAKAHDYDLSSMIF---FMIAAEpvrqktlKRFVELTrpyGLSQEVMApg 836
Cdd:cd17635     87 LTT---NAVTTTClVPTLLSKLV---SELKSANATVPSLRLIGYggsRAIAAD-------VRFIEAT---GLTNTAQV-- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  837 YGLAENCVFVGCAYGKkkpilvdwqGRICCGYVDPNDADVDIRIVDADtGLEVDEDGkEGEIWISSPSAGIGYWGKEELS 916
Cdd:cd17635    149 YGLSETGTALCLPTDD---------DSIEINAVGRPYPGVDVYLAATD-GIAGPSAS-FGTIWIKSPANMLGYWNNPERT 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  917 QKTFRNKlqkfpgrkYTRTGDLGRVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVESSSellrpgccavisvpeDVLS 995
Cdd:cd17635    218 AEVLIDG--------WVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEGVS---------------GVQE 274

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  996 AKGISLPDAsdEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGvtvasvKLIRPRTIS------KTTSGKIKR 1063
Cdd:cd17635    275 CACYEISDE--EFGELVGLAVVASAELDENAIRALKHTIRRELE------PYARPSTIVivtdipRTQSGKVKR 340
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 673-1035 1.02e-21

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 101.49  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMVCggtaILFSplt 752
Cdd:PRK07514   154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFH----THGLFVATNV----ALLA--- 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 fiRNPLLWLqtisdykathsagPNFAFELVIR----------------RLEAD-----KAKAHdydlssMIFFMIAAEPV 811
Cdd:PRK07514   223 --GASMIFL-------------PKFDPDAVLAlmpratvmmgvptfytRLLQEprltrEAAAH------MRLFISGSAPL 281

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  812 RQKTLKRFVELT------RpYGLSQEVMapgygLAENcvfvgcAY-GKKKPilvdwqgriccGYVDPNDADVDIRIVDAD 884
Cdd:PRK07514   282 LAETHREFQERTghaileR-YGMTETNM-----NTSN------PYdGERRA-----------GTVGFPLPGVSLRVTDPE 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  885 TGLEVdEDGKEGEIWISSPSAGIGYWgkeELSQKTfrnkLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNI 963
Cdd:PRK07514   339 TGAEL-PPGEIGMIEVKGPNVFKGYW---RMPEKT----AEEFRADGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNV 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  964 YSADVEK-------TVESssellrpgccAVISVPEdvlsakgislPDASDEVGLVVIAelKDGKPVD-KDIIKQIESRVA 1035
Cdd:PRK07514   411 YPKEVEGeidelpgVVES----------AVIGVPH----------PDFGEGVTAVVVP--KPGAALDeAAILAALKGRLA 468
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 670-992 1.76e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 100.83  E-value: 1.76e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTA--MVCGGTAIL 747
Cdd:PRK06188   163 AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AGGAFFLptLLRGGTVIV 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 ---FSPLTFIRnpllwlqTISDYKAThsagpnFAFeLV---IRRLeADKAKAHDYDLSS--MIFFMIAA-EPVR-QKTLK 817
Cdd:PRK06188   239 lakFDPAEVLR-------AIEEQRIT------ATF-LVptmIYAL-LDHPDLRTRDLSSleTVYYGASPmSPVRlAEAIE 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  818 RFveltrpyglsQEVMAPGYGLAEnCVFVGCAYGKKKPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVDEdGKEGE 897
Cdd:PRK06188   304 RF----------GPIFAQYYGQTE-APMVITYLRKRDHDPDDPKRLTSCGRPTPG---LRVALLDED-GREVAQ-GEVGE 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  898 IWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 976
Cdd:PRK06188   368 ICVRGPLVMDGYWNRPEETAEAFRD--------GWLHTGDVAREDEdGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHP 439

                          330
                   ....*....|....*.
gi 1973708721  977 ELlrpGCCAVISVPED 992
Cdd:PRK06188   440 AV---AQVAVIGVPDE 452
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 471-969 1.89e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 101.27  E-value: 1.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  471 DQEETGLKTLSETHGIVFP-DLPN----------LDSYLKHWAAKEITQNKTLYTwineeGAVVcqrTYAELDSNASCIA 539
Cdd:PRK06178     1 MAEEAYLAELRALQQAAWPaGIPRepeyphgerpLTEYLRAWARERPQRPAIIFY-----GHVI---TYAELDELSDRFA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  540 hKLLTSRKptIKPGDRV--LLVHVPglDFVDSFFGCLRAKVVPVPVLPPDPLQRGGQALtkieNIAKLCNAVAILSTVGY 617
Cdd:PRK06178    73 -ALLRQRG--VGAGDRVavFLPNCP--QFHIVFFGILKLGAVHVPVSPLFREHELSYEL----NDAGAEVLLALDQLAPV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  618 HSAVRAG-SVKNLIsFTRKS----AESTAQWPNL---PWLHTDSWIKSSKVLPASNIGSQSES-QPDDLCFLQFTSGSTG 688
Cdd:PRK06178   144 VEQVRAEtSLRHVI-VTSLAdvlpAEPTLPLPDSlraPRLAAAGAIDLLPALRACTAPVPLPPpALDALAALNYTGGTTG 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  689 DAKGVMITHGGLI------HNVKLmrrryRSTSNTVLVSWLPQY----HDMGLIGGLFtamvCGGTAILFS---PLTFir 755
Cdd:PRK06178   223 MPKGCEHTQRDMVytaaaaYAVAV-----VGGEDSVFLSFLPEFwiagENFGLLFPLF----SGATLVLLArwdAVAF-- 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 npllwLQTISDYKATHSAGP-NFAFELVirrleaDKAKAHDYDLSSM-----IFFMIAAEPV-RQktlkRFVELTrpygl 828
Cdd:PRK06178   292 -----MAAVERYRVTRTVMLvDNAVELM------DHPRFAEYDLSSLrqvrvVSFVKKLNPDyRQ----RWRALT----- 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sqevmapGYGLAEncvfvgCAYGKKKPILVDwqgRICCGYVDpNDADV--------------DIRIVDADTGlEVDEDGK 894
Cdd:PRK06178   352 -------GSVLAE------AAWGMTETHTCD---TFTAGFQD-DDFDLlsqpvfvglpvpgtEFKICDFETG-ELLPLGA 413

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721  895 EGEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK06178   414 EGEIVVRTPSLLKGYWNKPEATAEALRD--------GWLHTGDIGKIDeQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 675-1065 2.29e-21

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 99.33  E-value: 2.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITH---------GGLIHNVKlMRRRYRSTSNTvlvSWLpqyhdMGLIGGLFTAMVCGGTA 745
Cdd:cd05972     81 EDPALIYFTSGTTGLPKGVLHTHsyplghiptAAYWLGLR-PDDIHWNIADP---GWA-----KGAWSSFFGPWLLGATV 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  746 ILFSPLTFirNPLLWLQTISDYKATHSAGPNFAFELVIrrleadKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRP 825
Cdd:cd05972    152 FVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLI------KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGL 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 YglsqevMAPGYGLAENCVFVG-CAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVDEdGKEGEIWISSPS 904
Cdd:cd05972    224 P------IRDGYGQTETGLTVGnFPDMPVKP---GSMGRPTPGY--------DVAIIDDD-GRELPP-GEEGDIAIKLPP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGI--GYWGKEELSQKTFRNklqkfpgrKYTRTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR- 980
Cdd:cd05972    285 PGLflGYVGDPEKTEASIRG--------DYYLTGDRAyRDEDGYFWFVGRADDIIKSSGYRIGPFEVE------SALLEh 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  981 PGC--CAVISVPEDVlsakgislpdasdeVGLVVIA--ELKDGKPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKT 1056
Cdd:cd05972    351 PAVaeAAVVGSPDPV--------------RGEVVKAfvVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKT 416


                   ....*....
gi 1973708721 1057 TSGKIKRFE 1065
Cdd:cd05972    417 ISGKIRRVE 425
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 674-1061 4.19e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 97.55  E-value: 4.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTF 753
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 iRNPLL----WlQTISDYKAThsagpnfAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpyGLS 829
Cdd:cd05944     81 -RNPGLfdnfW-KLVERYRIT-------SLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDAT---GLP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 qevMAPGYGLAENCVFVGCAY--GKKKPilvdwqGRIccGYVDPNdADVDIRIVDADTGLEVDEDGKE-GEIWISSPSAG 906
Cdd:cd05944    149 ---VVEGYGLTEATCLVAVNPpdGPKRP------GSV--GLRLPY-ARVRIKVLDGVGRLLRDCAPDEvGEICVAGPGVF 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  907 IGYWGKEelsqktfrNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKtvesssellrpgccA 985
Cdd:cd05944    217 GGYLYTE--------GNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEE--------------A 274

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721  986 VISVPEdVLSAKGISLPDASDEVGLVVIAELKDGKPVDK-DIIKQIESRVAEEHGVTVAsVKLIRPrtISKTTSGKI 1061
Cdd:cd05944    275 LLRHPA-VAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEeELLAWARDHVPERAAVPKH-IEVLEE--LPVTAVGKV 347
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 521-994 4.84e-21

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 99.32  E-value: 4.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrggqal 596
Cdd:cd05920     33 AVVDgdrRLTYRELDRRADRLAAGL---RGLGIRPGDRVV-VQLPnVAEFVVLFFALLRL-------------------- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  597 tkieniaklcNAVAILSTVGYhsavRAGSVKNLISFTRKSAestaqwpnlpWLHTDSWiksSKVLPASNIGSQSESQPDd 676
Cdd:cd05920     89 ----------GAVPVLALPSH----RRSELSAFCAHAEAVA----------YIVPDRH---AGFDHRALARELAESIPE- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  677 LCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLFTAMVCGGTAILFSPLTfir 755
Cdd:cd05920    141 VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPS--- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 nPLLWLQTISDYKATHSAgpnfafeLV--IRRLEADKAKAHDYDLSSMIFFMIAAEPVrQKTLKRFVELTRPYGLsQEVm 833
Cdd:cd05920    218 -PDAAFPLIEREGVTVTA-------LVpaLVSLWLDAAASRRADLSSLRLLQVGGARL-SPALARRVPPVLGCTL-QQV- 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  834 apgYGLAENCVfvgC--AYGKKKPILVDWQGRiccgyvdPNDADVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYWG 911
Cdd:cd05920    287 ---FGMAEGLL---NytRLDDPDEVIIHTQGR-------PMSPDDEIRVVDEE-GNPVPP-GEEGELLTRGPYTIRGYYR 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  912 KEELSQKTFRNKlqkfpgrKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVI 987
Cdd:cd05920    352 APEHNARAFTPD-------GFYRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVE------NLLLRhPAVhdAAVV 418


                   ....*..
gi 1973708721  988 SVPEDVL 994
Cdd:cd05920    419 AMPDELL 425
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 675-1082 5.48e-21

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 100.08  E-value: 5.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLqFTSGSTGDAKGVMITHGGliHNVKL---MRRRYRSTSNTVLvsWLPQyhDMGLIGG----LFTAMVCGGTAIL 747
Cdd:cd05967    231 DPLYIL-YTSGTTGKPKGVVRDNGG--HAVALnwsMRNIYGIKPGDVW--WAAS--DVGWVVGhsyiVYGPLLHGATTVL 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 FSPL-TFIRNPLLWLQTISDYKATH--SAgPNfAFElVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKrFVE--L 822
Cdd:cd05967    304 YEGKpVGTPDPGAFWRVIEKYQVNAlfTA-PT-AIR-AIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLE-WAEntL 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRP----YGLSQEvmapGYGLAENCVFVGCaygkkKPILVDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEI 898
Cdd:cd05967    380 GVPvidhWWQTET----GWPITANPVGLEP-----LPIKAGSPGKPVPGY--------QVQVLDED-GEPV-GPNELGNI 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  899 WIS---SPSAGIGYWGKEELSQKTFrnkLQKFPGrkYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVes 974
Cdd:cd05967    441 VIKlplPPGCLLTLWKNDERFKKLY---LSKFPG--YYDTGDAGYKDEdGYLFIMGRTDDVINVAGHRLSTGEMEESV-- 513

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  975 sseLLRPGC--CAVISVPEDVlsaKGislpdaSDEVGLVViaeLKDG-KPVDKDIIKQIESRVAEEHGvTVASVKL-IRP 1050
Cdd:cd05967    514 ---LSHPAVaeCAVVGVRDEL---KG------QVPLGLVV---LKEGvKITAEELEKELVALVREQIG-PVAAFRLvIFV 577

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1973708721 1051 RTISKTTSGKIKRfECLKQFVDGTLNTVPDPI 1082
Cdd:cd05967    578 KRLPKTRSGKILR-RTLRKIADGEDYTIPSTI 608
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 673-1065 1.24e-20

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 98.55  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLM-------RRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTA 745
Cdd:PRK07059   202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpaFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRN 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  746 ILfspltfIRNPL---LWLQTISDYKATHSAGPNFAFELVIRRLEADKAkahdyDLSSMIFF----MIAAEPVRqktlKR 818
Cdd:PRK07059   282 IL------IPNPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKL-----DFSKLIVAngggMAVQRPVA----ER 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FVELTR-PyglsqevMAPGYGLAENCVFVGCaygkkKPILVD-WQGRIccGYVDPNdADVDIRivdadtglevDEDGKE- 895
Cdd:PRK07059   347 WLEMTGcP-------ITEGYGLSETSPVATC-----NPVDATeFSGTI--GLPLPS-TEVSIR----------DDDGNDl 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 -----GEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK07059   402 plgepGEICIRGPQVMAGYWNRPDETAKVMTAD-------GFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  970 KTVESSSELLRpgcCAVISVPEdvlsakgislPDASDEVGLVVIAelKDGKPVDKDIIKQIESRvaeehgvtVASVKliR 1049
Cdd:PRK07059   475 EVVASHPGVLE---VAAVGVPD----------EHSGEAVKLFVVK--KDPALTEEDVKAFCKER--------LTNYK--R 529

                          410       420
                   ....*....|....*....|..
gi 1973708721 1050 PRTIS------KTTSGKIKRFE 1065
Cdd:PRK07059   530 PKFVEfrtelpKTNVGKILRRE 551
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 663-1063 2.87e-20

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 97.36  E-value: 2.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  663 ASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMV 740
Cdd:PLN02330   172 AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLR 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  741 CGGTAILFSPLTfirnpllwLQTISDYKATHSAGPNFAFELVIRRLEADKAkAHDYDLSSMIF--FMIAAEPVRQKTLKR 818
Cdd:PLN02330   252 NKGKVVVMSRFE--------LRTFLNALITQEVSFAPIVPPIILNLVKNPI-VEEFDLSKLKLqaIMTAAAPLAPELLTA 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FvELTRPYGLSQEvmapGYGLAE-NCVFV-------GCAYGKKKPIlvdwqgriccGYVDPNdadVDIRIVDADTGLEVD 890
Cdd:PLN02330   323 F-EAKFPGVQVQE----AYGLTEhSCITLthgdpekGHGIAKKNSV----------GFILPN---LEVKFIDPDTGRSLP 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  891 EDgKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PLN02330   385 KN-TPGELCVRSQCVMQGYYNNKEETDRTIDED-------GWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELE 456

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  970 ktvesssellrpgccAVISVPEDVLSAKGISLPD-ASDEVGLVVIAELKDGKPVDKDIIKQIESRVAeeHGVTVASVKLI 1048
Cdd:PLN02330   457 ---------------AILLTHPSVEDAAVVPLPDeEAGEIPAACVVINPKAKESEEDILNFVAANVA--HYKKVRVVQFV 519

                          410
                   ....*....|....*
gi 1973708721 1049 rpRTISKTTSGKIKR 1063
Cdd:PLN02330   520 --DSIPKSLSGKIMR 532
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 680-1065 7.81e-20

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 95.44  E-value: 7.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  680 LQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVcGGTAILfspLTFIRNPLL 759
Cdd:cd12118    138 LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAV-GGTNVC---LRKVDAKAI 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  760 WlQTISDYKATHSAGPNFAFELVIRRLEADKAKahdydLSSMIFFMIAAEPVRQKTLKRFVEL----TRPYGLSqEVmap 835
Cdd:cd12118    214 Y-DLIEKHKVTHFCGAPTVLNMLANAPPSDARP-----LPHRVHVMTAGAPPPAAVLAKMEELgfdvTHVYGLT-ET--- 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  836 gYGLAENCVFvgcaygkkKPilvDWQG-----------RICCGYVDPNDADVdiriVDADTGLEVDEDGKE-GEIWISSP 903
Cdd:cd12118    284 -YGPATVCAW--------KP---EWDElpteerarlkaRQGVRYVGLEEVDV----LDPETMKPVPRDGKTiGEIVFRGN 347

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  904 SAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGrVIQ--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRp 981
Cdd:cd12118    348 IVMKGYLKNPEATAEAFRG--------GWFHSGDLA-VIHpdGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLE- 417

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  982 gcCAVISVPedvlsakgislpdasDEV-GLVVIA--ELKDGKPV-DKDIIKQIESRVAeehgvtvasvKLIRPRTIS--- 1054
Cdd:cd12118    418 --AAVVARP---------------DEKwGEVPCAfvELKEGAKVtEEEIIAFCREHLA----------GFMVPKTVVfge 470

                          410
                   ....*....|...
gi 1973708721 1055 --KTTSGKIKRFE 1065
Cdd:cd12118    471 lpKTSTGKIQKFV 483
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 525-1064 1.23e-19

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 95.21  E-value: 1.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  525 QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDplqRGGQaltkIENIAK 604
Cdd:PRK06155    46 RWTYAEAARAAAAAAHAL---AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL---RGPQ----LEHILR 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  605 LCNAVAILSTVGYHSAVRA--GSVKNLISFTRKSAESTAQWPnLPWlHTDSWIKSSKVLPASNIgsqsesQPDDLCFLQF 682
Cdd:PRK06155   116 NSGARLLVVEAALLAALEAadPGDLPLPAVWLLDAPASVSVP-AGW-STAPLPPLDAPAPAAAV------QPGDTAAILY 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  683 TSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAIL---FSPLTFirnpll 759
Cdd:PRK06155   188 TSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLeprFSASGF------ 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  760 WlqtisDYKATHSAGPNFAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEP-VRQKTLKRF-VELtrpyglsqevmAPGY 837
Cdd:PRK06155   261 W-----PAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAaLHAAFRERFgVDL-----------LDGY 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  838 GLAENCVFVGCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISS--PSA-GIGYWGKEE 914
Cdd:PRK06155   325 GSTETNFVIAVTHGSQRP---GSMGRLAPGF--------EARVVDEH-DQEL-PDGEPGELLLRAdePFAfATGYFGMPE 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  915 LSQKTFRNKlqkfpgrkYTRTGDlgRVIQ---GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPE 991
Cdd:PRK06155   392 KTVEAWRNL--------WFHTGD--RVVRdadGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA---AAVFPVPS 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  992 DVlsakgislpdASDEVGLVVIaeLKDGKPVD-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKIKRF 1064
Cdd:PRK06155   459 EL----------GEDEVMAAVV--LRDGTALEpVALVRHCEPRLA----------YFAVPRYVEfvaalpKTENGKVQKF 516
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 671-992 1.26e-19

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 94.70  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMVCGGTAILFSP 750
Cdd:cd17655    133 VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDAS-VTEIFASLLSGNTLYIVRK 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  751 LTFIRNPLLwLQTISDYKATHSAGPNFAFELVirrleadkAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELtrpYGLSQ 830
Cdd:cd17655    212 ETVLDGQAL-TQYIRQNRITIIDLTPAHLKLL--------DAADDSEGLSLKHLIVGGEALSTELAKKIIEL---FGTNP 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMApGYGLAENCvfVGCAYGKKKPiLVDWQGRICCGyvdpnDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYW 910
Cdd:cd17655    280 TITN-AYGPTETT--VDASIYQYEP-ETDQQVSVPIG-----KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYL 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  911 GKEELSQKTFRNklQKF-PGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEK---TVESSSEllrpgccA 985
Cdd:cd17655    351 NRPELTAEKFVD--DPFvPGERMYRTGDLARWLpDGNIEFLGRIDHQVKIRGYRIELGEIEArllQHPDIKE-------A 421


                   ....*..
gi 1973708721  986 VISVPED 992
Cdd:cd17655    422 VVIARKD 428
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 674-1064 1.71e-19

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 95.12  E-value: 1.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSpltf 753
Cdd:PRK13295   196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---- 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 IRNPLLWLQTISDYKATHS-AGPNFAFELvirrleADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRfveLTRPYGLSqev 832
Cdd:PRK13295   272 IWDPARAAELIRTEGVTFTmASTPFLTDL------TRAVKESGRPVSSLRTFLCAGAPIPGALVER---ARAALGAK--- 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAEN-CVFVGC-AYGKKKPILVDwqgriccGYVDPNdadVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYW 910
Cdd:PRK13295   340 IVSAWGMTENgAVTLTKlDDPDERASTTD-------GCPLPG---VEVRVVDAD-GAPLPA-GQIGRLQVRGCSNFGGYL 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  911 GKEELSQKTFRNklqkfpgrkYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISV 989
Cdd:PRK13295   408 KRPQLNGTDADG---------WFDTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ---VAIVAY 475

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721  990 PEDVLSAKGislpdasdeVGLVViaeLKDGKPVDKDIIKqiesRVAEEHGVTVASV--KLIRPRTISKTTSGKIKRF 1064
Cdd:PRK13295   476 PDERLGERA---------CAFVV---PRPGQSLDFEEMV----EFLKAQKVAKQYIpeRLVVRDALPRTPSGKIQKF 536
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 676-1010 2.13e-19

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 91.79  E-value: 2.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLI-------HNVKLmrrryRSTSNTVLVSwlPQYHDMGLIGGLFTAMVCGGTAIlf 748
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaaawaDCADL-----TEDDRYLIIN--PFFHTFGYKAGIVACLLTGATVV-- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 sPLTfIRNPLLWLQTISDYKATHSAGPNFAFELVIrrleaDKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVEltrpyGL 828
Cdd:cd17638     72 -PVA-VFDVDAILEAIERERITVLPGPPTLFQSLL-----DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----EL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 SQEVMAPGYGLAENCVFVGCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDAdtglevdedgkeGEIWISSPSAGIG 908
Cdd:cd17638    140 GFETVLTAYGLTEAGVATMCRPGDDAETVATTCGRAC--------PGFEVRIADD------------GEVLVRGYNVMQG 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWGKEELSQKTFrnklqkfPGRKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVI 987
Cdd:cd17638    200 YLDDPEATAEAI-------DADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGAL---AEHPGVAQVAVI 269

                          330       340
                   ....*....|....*....|...
gi 1973708721  988 SVPEDVLSAKGISLPDASDEVGL 1010
Cdd:cd17638    270 GVPDERMGEVGKAFVVARPGVTL 292
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
527-1065 3.61e-19

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 94.17  E-value: 3.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSRKptIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQR--------GGQALTK 598
Cdd:PRK08751    52 TYREADQLVEQFAAYLLGELQ--LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRElkhqlidsGASVLVV 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  599 IENIAKLCNAV--------AILSTVGYHSAVRAGSVKNLISFTRKSAESTAQWPNLPWLHTDSWIKSSKVLPASNIgsqs 670
Cdd:PRK08751   130 IDNFGTTVQQViadtpvkqVITTGLGDMLGFPKAALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQI---- 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 esQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTS-----NTVLVSWLPQYHDMGLIGGLFTAMVCGGTA 745
Cdd:PRK08751   206 --EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleegCEVVITALPLYHIFALTANGLVFMKIGGCN 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  746 ILFS-PltfiRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAkahdyDLSSMIFFMIAAEPVRQKTLKRFVELTr 824
Cdd:PRK08751   284 HLISnP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVAERWKQVT- 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  825 pyGLSqevMAPGYGLAEN----CVfvgcaygkkKPI-LVDWQGRIccGYVDPNdADVDIRIvDADTGLEVdedGKEGEIW 899
Cdd:PRK08751   354 --GLT---LVEAYGLTETspaaCI---------NPLtLKEYNGSI--GLPIPS-TDACIKD-DAGTVLAI---GEIGELC 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  900 ISSPSAGIGYWGKEELSQKTfrnklqkFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKtvesssel 978
Cdd:PRK08751   413 IKGPQVMKGYWKRPEETAKV-------MDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIED-------- 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  979 lrpgccaVISVPEDVLSAKGISLPD-ASDEVGLVVIaelkdgkpVDKDiiKQIESRVAEEHGVT-VASVKLIR----PRT 1052
Cdd:PRK08751   478 -------VIAMMPGVLEVAAVGVPDeKSGEIVKVVI--------VKKD--PALTAEDVKAHARAnLTGYKQPRiiefRKE 540

                          570
                   ....*....|...
gi 1973708721 1053 ISKTTSGKIKRFE 1065
Cdd:PRK08751   541 LPKTNVGKILRRE 553
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 527-992 7.39e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 92.90  E-value: 7.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltSRKPTIKPGDRVLlVHVPG-LDFVDSFFGCLRAKVVPVPVLPPDPLQR--------GGQALT 597
Cdd:PRK05677    51 TYGELYKLSGAFAAWL--QQHTDLKPGDRIA-VQLPNvLQYPVAVFGAMRAGLIVVNTNPLYTAREmehqfndsGAKALV 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAV--------AILSTVG-YHSAVRAGSVKNLISFTRKSaestaqwpnLPWLHTDSWIKSSKVLPASNIGS 668
Cdd:PRK05677   128 CLANMAHLAEKVlpktgvkhVIVTEVAdMLPPLKRLLINAVVKHVKKM---------VPAYHLPQAVKFNDALAKGAGQP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSES--QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSN---TVLVSWLPQYHDMGLIGGLFTAMVCGG 743
Cdd:PRK05677   199 VTEAnpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNegcEILIAPLPLYHIYAFTFHCMAMMLIGN 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  744 TAILfspltfIRNPL---LWLQTISDYKATHSAGPNFAFELVIRRleadkAKAHDYDLSSMIFFMIAAEPVRQKTLKRFV 820
Cdd:PRK05677   279 HNIL------ISNPRdlpAMVKELGKWKFSGFVGLNTLFVALCNN-----EAFRKLDFSALKLTLSGGMALQLATAERWK 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 ELTrpyGLSqevMAPGYGLAENcvfvgcaygkkKPIL-VDWQGRICCGYVDPNDADVDIRIVDaDTGLEVDEdGKEGEIW 899
Cdd:PRK05677   348 EVT---GCA---ICEGYGMTET-----------SPVVsVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPL-GEVGELC 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  900 ISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGrVIQ--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSE 977
Cdd:PRK05677   409 VKGPQVMKGYWQRPEATDEILDSD-------GWLKTGDIA-LIQedGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPG 480

                          490
                   ....*....|....*
gi 1973708721  978 LLRpgcCAVISVPED 992
Cdd:PRK05677   481 VLQ---CAAIGVPDE 492
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 527-1017 1.51e-18

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 92.19  E-value: 1.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltSRKPTIKPGDRVLlVHVPG-LDFVDSFFGCLRAKVVPVPVLPPDPLQR--------GGQALT 597
Cdd:PRK12492    51 SYAELERHSAAFAAYL--QQHTDLVPGDRIA-VQMPNvLQYPIAVFGALRAGLIVVNTNPLYTAREmrhqfkdsGARALV 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGYHSAVRAGSVknlisftrksaESTAQwpnlPWLHTDSWIKSSKVLPASNI----------- 666
Cdd:PRK12492   128 YLNMFGKLVQEVLPDTGIEYLIEAKMGDL-----------LPAAK----GWLVNTVVDKVKKMVPAYHLpqavpfkqalr 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  667 -GSQSESQP-----DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRST----------SNTVLVSWLPQYHDMG 730
Cdd:PRK12492   193 qGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEVMIAPLPLYHIYA 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 LIGGLFTAMVCGGTAILfspLTFIRNPLLWLQTISDYKATHSAGPNFAFELVIrrleaDKAKAHDYDLSSMIFFMIAAEP 810
Cdd:PRK12492   273 FTANCMCMMVSGNHNVL---ITNPRDIPGFIKELGKWRFSALLGLNTLFVALM-----DHPGFKDLDFSALKLTNSGGTA 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  811 VRQKTLKRFVELTrpyGLSqevMAPGYGLAEnCVFVGCA--YGKkkpilvdwQGRIccGYVDPNDADVDIRIVDaDTGLE 888
Cdd:PRK12492   345 LVKATAERWEQLT---GCT---IVEGYGLTE-TSPVASTnpYGE--------LARL--GTVGIPVPGTALKVID-DDGNE 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  889 VDEdGKEGEIWISSPSAGIGYWGKEELSQktfrnklQKFPGRKYTRTGDLGrVIQGNLF--ITGRIKDLIIVAGRNIYSA 966
Cdd:PRK12492   407 LPL-GERGELCIKGPQVMKGYWQQPEATA-------EALDAEGWFKTGDIA-VIDPDGFvrIVDRKKDLIIVSGFNVYPN 477

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1973708721  967 DVEKTVESSSELlrpGCCAVISVPeDVLSAKGISLPDASDEVGLVViAELK 1017
Cdd:PRK12492   478 EIEDVVMAHPKV---ANCAAIGVP-DERSGEAVKLFVVARDPGLSV-EELK 523
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 669-969 2.30e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 91.37  E-value: 2.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgglFTAMVC--GGTAI 746
Cdd:PRK12583   195 QASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMV---LANLGCmtVGACL 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 LFSPLTFirNPLLWLQTISDYKAT--HSAGPNFAFELvirrleaDKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFV-ELT 823
Cdd:PRK12583   272 VYPNEAF--DPLATLQAVEEERCTalYGVPTMFIAEL-------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMdEMH 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  824 RPyglsqEVMApGYGLAENC-VFVGCAYGKKKPILVDWQGRiccgyvdpNDADVDIRIVDADTglEVDEDGKEGEIWISS 902
Cdd:PRK12583   343 MA-----EVQI-AYGMTETSpVSLQTTAADDLERRVETVGR--------TQPHLEVKVVDPDG--ATVPRGEIGELCTRG 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721  903 PSAGIGYWGKEELSQKTFrnklqkfPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK12583   407 YSVMKGYWNNPEATAESI-------DEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIE 467
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 683-1035 2.86e-18

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 88.48  E-value: 2.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  683 TSGSTGDAKGVMITHGGLIH-NVKLMRRrYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAILFSPLtfirNPLLWL 761
Cdd:cd17637      8 TAAVAGRPRGAVLSHGNLIAaNLQLIHA-MGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKF----DPAEAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  762 QTISDYKATHSagpnFAFELVIRRLEaDKAKAHDYDLSSM--IFFMIAAEpvrqkTLKRFVELTRPYGLSqevmapGYGL 839
Cdd:cd17637     82 ELIEEEKVTLM----GSFPPILSNLL-DAAEKSGVDLSSLrhVLGLDAPE-----TIQRFEETTGATFWS------LYGQ 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  840 AENCVFVGCAYGKKKPilvdwqGriCCGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKT 919
Cdd:cd17637    146 TETSGLVTLSPYRERP------G--SAGRPGPL---VRVRIVD-DNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYT 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  920 FRNklqkfpgrKYTRTGDLGRV-IQGNLFITGRI--KDLIIVAGRNIYSADVEKTvessseLLRPGCCAVISVpedvlsa 996
Cdd:cd17637    213 FRN--------GWHHTGDLGRFdEDGYLWYAGRKpeKELIKPGGENVYPAEVEKV------ILEHPAIAEVCV------- 271

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1973708721  997 kgISLPDASDEVGLVVIAELKDGKPV-DKDIIKQIESRVA 1035
Cdd:cd17637    272 --IGVPDPKWGEGIKAVCVLKPGATLtADELIEFVGSRIA 309
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 661-974 5.27e-18

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 89.64  E-value: 5.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  661 LPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMV 740
Cdd:cd12114    112 LAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALS 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  741 CGGTAILFSPLTfIRNPLLWLQTISDYKATHSagpNFA---FELVIRRLEAD-------------------------KAK 792
Cdd:cd12114    191 AGATLVLPDEAR-RRDPAHWAELIERHGVTLW---NSVpalLEMLLDVLEAAqallpslrlvllsgdwipldlparlRAL 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  793 AHDYDLSSM----------IFFMIAAEPVRQKTLkrfveltrPYglsqevmapGYGLAENCVFVgcaygkkkpilVDWQG 862
Cdd:cd12114    267 APDARLISLggateasiwsIYHPIDEVPPDWRSI--------PY---------GRPLANQRYRV-----------LDPRG 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  863 RICcgyvdPndadvdirivdadtglevdeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnkLQKFPGRKYTRTGDLGRVI 942
Cdd:cd12114    319 RDC-----P--------------------DWVPGELWIGGRGVALGYLGDPELTAARF---VTHPDGERLYRTGDLGRYR 370

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1973708721  943 -QGNLFITGRIKDLIIVAGRNIYSADVEKTVES 974
Cdd:cd12114    371 pDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 678-1035 6.35e-18

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 87.36  E-value: 6.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLI-HNVKLMRRRyRSTSNTVLVSWLPQYHdMGLIGGLFTAMVCGGTAIlfspltFIR- 755
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQ-AIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNV------FVRr 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 -NPLLWLQTISDYKATHS--AGPNFAfelVIRRLEADKAkahdYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGLSQ-E 831
Cdd:cd17636     75 vDAEEVLELIEAERCTHAflLPPTID---QIVELNADGL----YDLSSLRSSPAAPEWNDMATVDTSPWGRKPGGYGQtE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  832 VMAPG--YGLAENCVfvgCAYGKKKPILVdwqgriccgyvdpndadvdIRIVDADtGLEVdEDGKEGEIWISSPSAGIGY 909
Cdd:cd17636    148 VMGLAtfAALGGGAI---GGAGRPSPLVQ-------------------VRILDED-GREV-PDGEVGEIVARGPTVMAGY 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  910 WGKEELSQKTFRNklqkfpgrKYTRTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellRPGC--CAV 986
Cdd:cd17636    204 WNRPEVNARRTRG--------GWHHTNDLGrREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-----HPAVadAAV 270

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  987 ISVPEDVL--SAKGIslpdasdevglVViaeLKDGKPVDK-DIIKQIESRVA 1035
Cdd:cd17636    271 IGVPDPRWaqSVKAI-----------VV---LKPGASVTEaELIEHCRARIA 308
PRK07529 PRK07529
AMP-binding domain protein; Validated
 674-1023 9.49e-18

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 89.63  E-value: 9.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTF 753
Cdd:PRK07529   212 PDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 iRNPLL----WlQTISDYKATH-SAGPNfafelVIRRLEADKAKAHdyDLSSMIFFMIAAEPVRQKTLKRFVELTrpyGL 828
Cdd:PRK07529   292 -RGPGVianfW-KIVERYRINFlSGVPT-----VYAALLQVPVDGH--DISSLRYALCGAAPLPVEVFRRFEAAT---GV 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 SqevMAPGYGLAENCVFVGCAY--GKKKP----ILVDWQgriccgyvdpndaDVDIRIVDADTGLEVD-EDGKEGEIWIS 901
Cdd:PRK07529   360 R---IVEGYGLTEATCVSSVNPpdGERRIgsvgLRLPYQ-------------RVRVVILDDAGRYLRDcAVDEVGVLCIA 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  902 SPSAGIGYwgkeelsqKTFRNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR 980
Cdd:PRK07529   424 GPNVFSGY--------LEAAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEA------LLR 489

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1973708721  981 -PgccavisvpeDVLSAKGISLPDA-SDEVGlVVIAELKDGKPVD 1023
Cdd:PRK07529   490 hP----------AVALAAAVGRPDAhAGELP-VAYVQLKPGASAT 523
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
674-1035 1.13e-17

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 89.18  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDlCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL-----F 748
Cdd:PRK05852   176 PDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpargrF 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTFirnpllWlQTISDYKAT-HSAGPNFAFELVIRRLEADKAKAHdydlSSMIFFMIAAEPVRQKTLKrfveltrpyG 827
Cdd:PRK05852   255 SAHTF------W-DDIKAVGATwYTAVPTIHQILLERAATEPSGRKP----AALRFIRSCSAPLTAETAQ---------A 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  828 LSQEVMAPgyglaencvfVGCAYGKKKPI------LVDWQGR-----ICCGYVDPNDAdVDIRIVDADtGLEVDEDgKEG 896
Cdd:PRK05852   315 LQTEFAAP----------VVCAFGMTEAThqvtttQIEGIGQtenpvVSTGLVGRSTG-AQIRIVGSD-GLPLPAG-AVG 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  897 EIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvess 975
Cdd:PRK05852   382 EVWLRGTTVVRGYLGDPTITAANFTDG--------WLRTGDLGSLSAaGDLSIRGRIKELINRGGEKISPERVE------ 447

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  976 sellrpgccAVISVPEDVLSAKGISLPDA--SDEVGLVVIAElKDGKPVDKDIIKQIESRVA 1035
Cdd:PRK05852   448 ---------GVLASHPNVMEAAVFGVPDQlyGEAVAAVIVPR-ESAPPTAEELVQFCRERLA 499
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 672-1071 1.90e-17

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 87.98  E-value: 1.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VL--------VSwlpqyhdmglIGGLFTAMVCG 742
Cdd:cd05918    103 SSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVS----------ILEIFTTLAAG 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  743 GTaiLFSPLTFIR-NPLlwLQTISDYKATHsagpnfAFeL---VIRRLEADkakahdyDLSSMIFFMIAAEPVRQKTLKR 818
Cdd:cd05918    173 GC--LCIPSEEDRlNDL--AGFINRLRVTW------AF-LtpsVARLLDPE-------DVPSLRTLVLGGEALTQSDVDT 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FVELTRpyglsqeVMApGYGLAENCVFVGCaygkkKPILVDWQGRI------CCGY-VDPNDADvdiRIVDAdtglevde 891
Cdd:cd05918    235 WADRVR-------LIN-AYGPAECTIAATV-----SPVVPSTDPRNigrplgATCWvVDPDNHD---RLVPI-------- 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  892 dGKEGEIWISSPSAGIGYWGKEELSQKTF-------RNKLQKFPGRKYtRTGDLGRVI-QGNLFITGRIKDLIIVAGRNI 963
Cdd:cd05918    291 -GAVGELLIEGPILARGYLNDPEKTAAAFiedpawlKQEGSGRGRRLY-RTGDLVRYNpDGSLEYVGRKDTQVKIRGQRV 368

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  964 YSADVEKTVESSSELLRPgCCAVISVPED---------VLSAKGISLPDASDEVGLVVIAelkdgkPVDKDIIKQIESRV 1034
Cdd:cd05918    369 ELGEIEHHLRQSLPGAKE-VVVEVVKPKDgssspqlvaFVVLDGSSSGSGDGDSLFLEPS------DEFRALVAELRSKL 441

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1973708721 1035 AE---EHGVTVASVKLirpRTISKTTSGKIKRfECLKQFV 1071
Cdd:cd05918    442 RQrlpSYMVPSVFLPL---SHLPLTASGKIDR-RALRELA 477
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 521-1063 1.92e-17

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 88.17  E-value: 1.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALT 597
Cdd:cd17651     13 ALVAegrRLTYAELDRRANRLAHRL---RARGVGPGDLVALCARRSAELVVALLAILKA----------------GAAYV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KI------ENIAklcnavAILSTVGYHSAVRAgsvknlisftrkSAESTAQWPNLPWLHTDSWIKSSKVLPASNIgsqSE 671
Cdd:cd17651     74 PLdpaypaERLA------FMLADAGPVLVLTH------------PALAGELAVELVAVTLLDQPGAAAGADAEPD---PA 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAIL---- 747
Cdd:cd17651    133 LDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLppee 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 --FSPLTFIRnpllWLQTisdYKATHSAGPNFAFELVIrrLEADKAKAHDYDLSSMIffmIAAEPVRQKTLKRFVELTRP 825
Cdd:cd17651    212 vrTDPPALAA----WLDE---QRISRVFLPTVALRALA--EHGRPLGVRLAALRYLL---TGGEQLVLTEDLREFCAGLP 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 YGLsqevMAPGYGLAENCVfvgcAYGKKKPILVD-WQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPS 904
Cdd:cd17651    280 GLR----LHNHYGPTETHV----VTALSLPGDPAaWPAPPPIGRPIDN---TRVYVLDAA--LRPVPPGVPGELYIGGAG 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRnKLQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLRpgc 983
Cdd:cd17651    347 LARGYLNRPELTAERFV-PDPFVPGARMYRTGDLARWLpDGELEFLGRADDQVKIRGFRIELGEIE------AALAR--- 416

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  984 cavisVPeDVLSAKGISLPDASDEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTVASVKLIR-PRtiskTTSGKIK 1062
Cdd:cd17651    417 -----HP-GVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDAlPL----TPNGKLD 486


                   .
gi 1973708721 1063 R 1063
Cdd:cd17651    487 R 487
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 671-1035 2.17e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 88.07  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFlqfTSGSTGDAKGVMITHGGLI-HNVKLMRR--RYRSTSNTVLVSwLPQYHDMGLigGL-FTAMVCGGTAI 746
Cdd:cd12119    162 ENTAAAICY---TSGTTGNPKGVVYSHRSLVlHAMAALLTdgLGLSESDVVLPV-VPMFHVNAW--GLpYAAAMVGAKLV 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 LFSPLTfirNPLLWLQTISDYKATHSAG-PnfafelVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELtrp 825
Cdd:cd12119    236 LPGPYL---DPASLAELIEREGVTFAAGvP------TVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER--- 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 yGLsqEVMApGYGLAENCVFVGCAYGKKK----PILVDW-----QGRICCGyvdpndadVDIRIVDADTGlEVDEDGKE- 895
Cdd:cd12119    304 -GV--RVIH-AWGMTETSPLGTVARPPSEhsnlSEDEQLalrakQGRPVPG--------VELRIVDDDGR-ELPWDGKAv 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 GEIWISSPSAGIGYWGKEELSQKTFRNklqkfpGrkYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKtves 974
Cdd:cd12119    371 GELQVRGPWVTKSYYKNDEESEALTED------G--WLRTGDVATIDeDGYLTITDRSKDVIKSGGEWISSVELEN---- 438

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721  975 ssellrpgccaVISVPEDVLSAKGISLPDAS-DEVGLVVIAeLKDGKPVD-KDIIKQIESRVA 1035
Cdd:cd12119    439 -----------AIMAHPAVAEAAVIGVPHPKwGERPLAVVV-LKEGATVTaEELLEFLADKVA 489
PRK08315 PRK08315
AMP-binding domain protein; Validated
 669-1065 3.22e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 87.94  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILF 748
Cdd:PRK08315   193 QATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYP 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLtFirNPLLWLQTISDYKATHSAG-----------PNFAfelvirrleadkakahDYDLSSMIFFMIAAEPVRQKTLK 817
Cdd:PRK08315   273 GEG-F--DPLATLAAVEEERCTALYGvptmfiaeldhPDFA----------------RFDLSSLRTGIMAGSPCPIEVMK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  818 RFVELTrpyGLSQEVMApgYGLAEnCVFVGCAYGKKKPIL--VDWQGRiccgyVDPNdadVDIRIVDADTGLEVdEDGKE 895
Cdd:PRK08315   334 RVIDKM---HMSEVTIA--YGMTE-TSPVSTQTRTDDPLEkrVTTVGR-----ALPH---LEVKIVDPETGETV-PRGEQ 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 GEIWISSPSAGIGYWGKEElsqKTfrnklqkfpgRK------YTRTGDLGrVI--QGNLFITGRIKDLIIVAGRNIYSAD 967
Cdd:PRK08315   399 GELCTRGYSVMKGYWNDPE---KT----------AEaidadgWMHTGDLA-VMdeEGYVNIVGRIKDMIIRGGENIYPRE 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  968 VEktvesssELLR--PgccavisvpeDVLSAKGISLPDA--SDEVGLVVIaeLKDGKPVDKDIIK-----QIesrvaeeh 1038
Cdd:PRK08315   465 IE-------EFLYthP----------KIQDVQVVGVPDEkyGEEVCAWII--LRPGATLTEEDVRdfcrgKI-------- 517

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1973708721 1039 gvtvASVKLirPRTIS------KTTSGKIKRFE 1065
Cdd:PRK08315   518 ----AHYKI--PRYIRfvdefpMTVTGKIQKFK 544
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 5.33e-17

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 77.19  E-value: 5.33e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 670-1069 8.86e-17

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 85.09  E-value: 8.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMvcgGTAILFS 749
Cdd:cd05912     72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLSILM---RSVIYGM 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 PLTFIR--NPLLWLQTISDYKATH-SAGPNfafelVIRRLEADKAKAHDYDLSSMiffMIAAEPVRQKTLKRFVELTRPY 826
Cdd:cd05912    145 TVYLVDkfDAEQVLHLINSGKVTIiSVVPT-----MLQRLLEILGEGYPNNLRCI---LLGGGPAPKPLLEQCKEKGIPV 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 GLSqevmapgYGLAENC---VFVGCAYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDedgkeGEIWISSP 903
Cdd:cd05912    217 YQS-------YGMTETCsqiVTLSPEDALNKI-----------GSAGKPLFPVELKIEDDGQPPYEV-----GEILLKGP 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  904 SAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPG 982
Cdd:cd05912    274 NVTKGYLNRPDATEESFENG--------WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAG 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  983 CcavisvpedvlsakgISLPDasDEVGLVVIAELKDGKPVDKD-IIKQIESRVAeehgvtvasvKLIRPRTI------SK 1055
Cdd:cd05912    346 V---------------VGIPD--DKWGQVPVAFVVSERPISEEeLIAYCSEKLA----------KYKVPKKIyfvdelPR 398

                          410
                   ....*....|....
gi 1973708721 1056 TTSGKIKRFEcLKQ 1069
Cdd:cd05912    399 TASGKLLRHE-LKQ 411
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 527-1035 9.53e-17

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 86.25  E-value: 9.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSrkpTIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrGG--------QALT 597
Cdd:PRK07470    34 TWREIDARVDALAAALAAR---GVRKGDRIL-VHSRnCNQMFESMFAAFRL---------------GAvwvptnfrQTPD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGY--HS-AVRAGSVKNLISFTRKSAESTAqwpnlpwlhtdswikSSKVLPASNIGSQSESQP 674
Cdd:PRK07470    95 EVAYLAEASGARAMICHADFpeHAaAVRAASPDLTHVVAIGGARAGL---------------DYEALVARHLGARVANAA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 ---DDLCFLQFTSGSTGDAKGVMITHGGLI-----HNVKLMRRryrSTSNTVLVSWLPQYHDMGlIGGLftAMVCGGTAI 746
Cdd:PRK07470   160 vdhDDPCWFFFTSGTTGRPKAAVLTHGQMAfvitnHLADLMPG---TTEQDASLVVAPLSHGAG-IHQL--CQVARGAAT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 LFSPLTFIRNPLLWlQTISDYKATHSagpnFAFELVIRRLEADKAkAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPy 826
Cdd:PRK07470   234 VLLPSERFDPAEVW-ALVERHRVTNL----FTVPTILKMLVEHPA-VDRYDHSSLRYVIYAGAPMYRADQKRALAKLGK- 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 glsqeVMAPGYGLAE--NCVFVgcaygkKKPILVDW----QGRI-CCGYvdpndadvdirivdADTGLEV---DEDGKE- 895
Cdd:PRK07470   307 -----VLVQYFGLGEvtGNITV------LPPALHDAedgpDARIgTCGF--------------ERTGMEVqiqDDEGREl 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 -----GEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK07470   362 ppgetGEICVIGPAVFAGYYNNPEANAKAFRDG--------WFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPREIE 433

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  970 KTVessseLLRPGC--CAVISVPEDVLSakgislpdasdEVGLVVIAeLKDGKPVDKD-IIKQIESRVA 1035
Cdd:PRK07470   434 EKL-----LTHPAVseVAVLGVPDPVWG-----------EVGVAVCV-ARDGAPVDEAeLLAWLDGKVA 485
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 659-992 1.05e-16

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 87.29  E-value: 1.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  659 KVLPASNIGS--QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 736
Cdd:PRK08633   764 RLLPARLLKRlyGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLW 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMvCGGTAILFSPltfirNPLLWL---QTISDYKATHSAG-PNFaFELVIRrleadKAKAHDYDLSSMIFFMIAAEPVR 812
Cdd:PRK08633   844 LPL-LEGIKVVYHP-----DPTDALgiaKLVAKHRATILLGtPTF-LRLYLR-----NKKLHPLMFASLRLVVAGAEKLK 911

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  813 QKTLKRFVEL--TRPYglsqevmaPGYGLAEncvfvgCAygkkkPIlvdwqgrICCGYVDPNDAD--------------- 875
Cdd:PRK08633   912 PEVADAFEEKfgIRIL--------EGYGATE------TS-----PV-------ASVNLPDVLAADfkrqtgskegsvgmp 965

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  876 ---VDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqkFPGRKYTRTGDLGRV-IQGNLFITGR 951
Cdd:PRK08633   966 lpgVAVRIVDPETFEEL-PPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD----IDGIGWYVTGDKGHLdEDGFLTITDR 1040

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1973708721  952 IKDLIIVAGRNIYSADVEktvESSSELL--RPGCCAVISVPED 992
Cdd:PRK08633  1041 YSRFAKIGGEMVPLGAVE---EELAKALggEEVVFAVTAVPDE 1080
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 515-1061 1.84e-16

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 85.32  E-value: 1.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  515 WINEEGAVVCQRTYAELDSNASCIAHKLltsRKPTIKPGDRVLlVHVPGL-DFVDSFFGCLRAKVVPVPVLppdplqrGG 593
Cdd:cd17634     74 YEGDDTSQSRTISYRELHREVCRFAGTL---LDLGVKKGDRVA-IYMPMIpEAAVAMLACARIGAVHSVIF-------GG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  594 QALTKIENIAKLCNAVAILSTVGYhsaVRAGSVKNLISFTRKSAESTA----------------QWPNLPWLHTDSWIKS 657
Cdd:cd17634    143 FAPEAVAGRIIDSSSRLLITADGG---VRAGRSVPLKKNVDDALNPNVtsvehvivlkrtgsdiDWQEGRDLWWRDLIAK 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  658 skvlpASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGliHNVKL---MRRRYRSTSNTVlVSWlpqYHDMGLIGG 734
Cdd:cd17634    220 -----ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGG--YLVYAattMKYVFDYGPGDI-YWC---TADVGWVTG 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  735 ----LFTAMVCGGTAILFSPLTFIRNPLLWLQTISDYKATHSagpnFAFELVIRRLEADKAKA-HDYDLSSMIFFMIAAE 809
Cdd:cd17634    289 hsylLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNIL----YTAPTAIRALMAAGDDAiEGTDRSSLRILGSVGE 364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  810 PVRQKTLKRFVELTrpyGLSQEVMAPGYGLAEncvfVGCAYGKKKPILVDWQGRiccgyvDPNDADVDIRIVDADTGLEV 889
Cdd:cd17634    365 PINPEAYEWYWKKI---GKEKCPVVDTWWQTE----TGGFMITPLPGAIELKAG------SATRPVFGVQPAVVDNEGHP 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  890 DEDGKEGEIWISSPSAG--IGYWGKEELSQKTFrnkLQKFPGrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSA 966
Cdd:cd17634    432 QPGGTEGNLVITDPWPGqtRTLFGDHERFEQTY---FSTFKG--MYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTA 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  967 DVEKTVESSSELLRpgcCAVISVPEDVlsaKGISLpdasdeVGLVViaeLKDGKPVDKDIIKQIESRVAEEHGVTVASVK 1046
Cdd:cd17634    507 EIESVLVAHPKVAE---AAVVGIPHAI---KGQAP------YAYVV---LNHGVEPSPELYAELRNWVRKEIGPLATPDV 571

                          570
                   ....*....|....*
gi 1973708721 1047 LIRPRTISKTTSGKI 1061
Cdd:cd17634    572 VHWVDSLPKTRSGKI 586
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 527-1064 2.26e-16

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 84.07  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTsrKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrggqaltkieniaklc 606
Cdd:cd05958     12 TYRDLLALANRIANVLVG--ELGIVPGNRVLLRGSNSPELVACWFGIQKA------------------------------ 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAilstVGYHSAVRAGSVKNLISFTRksaestaqwpnlpwlhtdswiksskvlPASNIGSQSESQPDDLCFLQFTSGS 686
Cdd:cd05958     60 GAIA----VATMPLLRPKELAYILDKAR---------------------------ITVALCAHALTASDDICILAFTSGT 108

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  687 TGDAKGVMITHggliHNVKLMRRRY-----RSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPLTfirnPLLWL 761
Cdd:cd05958    109 TGAPKATMHFH----RDPLASADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT----PDLLL 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  762 QTISDYKATHSAGPNFAFelvirRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpyGLsqEVMaPGYGLAE 841
Cdd:cd05958    181 SAIARYKPTVLFTAPTAY-----RAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT---GI--PII-DGIGSTE 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  842 NC-VFVGCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISSPSagiGYWGKEELSQKTF 920
Cdd:cd05958    250 MFhIFISARPGDARP---GATGKPVPGY--------EAKVVDDE-GNPV-PDGTIGRLAVRGPT---GCRYLADKRQRTY 313

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  921 RNKLQKFPGRKYTRTGDlgrviqGNLFITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVISVPedvlsakg 998
Cdd:cd05958    314 VQGGWNITGDTYSRDPD------GYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVaeCAVVGHP-------- 374

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721  999 islpdasDEVGLVVIAE---LKDGKPVDKDIIKQIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRF 1064
Cdd:cd05958    375 -------DESRGVVVKAfvvLRPGVIPGPVLARELQDHAKAH----IAPYK--YPRAIEfvtelpRTATGKLQRF 436
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 657-1065 2.53e-16

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 84.89  E-value: 2.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  657 SSKVLPASNIGSqsesqpDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRR------RYRSTSNTVLVSwLPQYHDMG 730
Cdd:PLN02574   186 DFDFVPKPVIKQ------DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasqyEYPGSDNVYLAA-LPMFHIYG 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 LigGLF-TAMVCGGTAILFSPlTFIRNPLlwLQTISDYKATHsagpnfaFELVIRRLEA--DKAKAHDYD-LSSMIFFMI 806
Cdd:PLN02574   259 L--SLFvVGLLSLGSTIVVMR-RFDASDM--VKVIDRFKVTH-------FPVVPPILMAltKKAKGVCGEvLKSLKQVSC 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  807 AAEPVRQKTLKRFVELTRPYGLSQevmapGYGLAENCVFVGCAYGKKKpilvdWQGRICCGYVDPNdadVDIRIVDADTG 886
Cdd:PLN02574   327 GAAPLSGKFIQDFVQTLPHVDFIQ-----GYGMTESTAVGTRGFNTEK-----LSKYSSVGLLAPN---MQAKVVDWSTG 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  887 LEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYS 965
Cdd:PLN02574   394 CLL-PPGNCGELWIQGPGVMKGYLNNPKATQSTIDKD-------GWLRTGDIAYFDEdGYLYIVDRLKEIIKYKGFQIAP 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  966 ADVEKTVESSSELLRpgcCAVISVPEdvlsakgislpDASDEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTvasv 1045
Cdd:PLN02574   466 ADLEAVLISHPEIID---AAVTAVPD-----------KECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVR---- 527

                          410       420
                   ....*....|....*....|
gi 1973708721 1046 KLIRPRTISKTTSGKIKRFE 1065
Cdd:PLN02574   528 KVVFVQSIPKSPAGKILRRE 547
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 675-1063 3.08e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 84.70  E-value: 3.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVkLMRRRYR---STSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILFSPL 751
Cdd:PRK06710   206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLyncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKF 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFirnpLLWLQTISDYKATHSAGpnfAFELVIRRLEADKAKahDYDLSSMIFFMIAAEPVRQKTLKRFVELTrpyglsQE 831
Cdd:PRK06710   285 DM----KMVFEAIKKHKVTLFPG---APTIYIALLNSPLLK--EYDISSIRACISGSAPLPVEVQEKFETVT------GG 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  832 VMAPGYGLAENCVFVGCAYgkkkpilvDWQGRIcCGYVDPNDADVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWG 911
Cdd:PRK06710   350 KLVEGYGLTESSPVTHSNF--------LWEKRV-PGSIGVPWPDTEAMIMSLETG-EALPPGEIGEIVVKGPQIMKGYWN 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  912 KEELSQKTFRNklqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKtvesssellrpgccaVISVP 990
Cdd:PRK06710   420 KPEETAAVLQD--------GWLHTGDVGYMDEdGFFYVKDRKKDMIVASGFNVYPREVEE---------------VLYEH 476

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  991 EDVLSAKGISLPDASDEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTvasvKLIRPRT-ISKTTSGKIKR 1063
Cdd:PRK06710   477 EKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVP----KVYEFRDeLPKTTVGKILR 546
PRK09274 PRK09274
peptide synthase; Provisional
 527-1051 4.37e-16

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 84.18  E-value: 4.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFgclrakvvpvpvlppdplqrggqALTKIeniaklc 606
Cdd:PRK09274    43 SFAELDARSDAIAHGLNAA---GIGRGMRAVLMVTPSLEFFALTF-----------------------ALFKA------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  607 NAVAILstvgyhsaVRAG-SVKNLISFTRKSAEST------AQW------PNLPWLHT-----DSWIKSSKVLPASNIGS 668
Cdd:PRK09274    90 GAVPVL--------VDPGmGIKNLKQCLAEAQPDAfigipkAHLarrlfgWGKPSVRRlvtvgGRLLWGGTTLATLLRDG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSES------QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhdmgligGLFtAMVCG 742
Cdd:PRK09274   162 AAAPfpmadlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF-------ALF-GPALG 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  743 GTAILfSPLTFIR----NPLLWLQTISDYKATHSAGpNFAfelVIRRLeADKAKAHDYDLSSMIFFMIAAEPVRQKTLKR 818
Cdd:PRK09274   234 MTSVI-PDMDPTRpatvDPAKLFAAIERYGVTNLFG-SPA---LLERL-GRYGEANGIKLPSLRRVISAGAPVPIAVIER 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 F-------VELTRPYGL----------SQEVMAPGYGLAENcvfvgcaygkkkpilvdwQGRICCGYVDPndaDVDIRIV 881
Cdd:PRK09274   308 FramlppdAEILTPYGAtealpissieSREILFATRAATDN------------------GAGICVGRPVD---GVEVRII 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  882 DADTGL--EVDED-----GKEGEIWISSPSAGIGYWGKEELSQKtfrNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIK 953
Cdd:PRK09274   367 AISDAPipEWDDAlrlatGEIGEIVVAGPMVTRSYYNRPEATRL---AKIPDGQGDVWHRMGDLGYLdAQGRLWFCGRKA 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  954 DLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEdvlsaKGISLPdasdevglVVIAELKDGKPVDKDIIKQiESR 1033
Cdd:PRK09274   444 HRVETAGGTLYTIPCERIFNTHPGVKR---SALVGVGV-----PGAQRP--------VLCVELEPGVACSKSALYQ-ELR 506

                          570       580
                   ....*....|....*....|.
gi 1973708721 1034 V-AEEHGVTvASVK--LIRPR 1051
Cdd:PRK09274   507 AlAAAHPHT-AGIErfLIHPS 526
PLN02246 PLN02246
4-coumarate--CoA ligase
 527-1063 7.13e-16

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 83.49  E-value: 7.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRakvvpvpvlppdplqRGGQALT--------K 598
Cdd:PLN02246    52 TYADVELLSRRVAAGL---HKLGIRQGDVVMLLLPNCPEFVLAFLGASR---------------RGAVTTTanpfytpaE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  599 IENIAKLCNAVAILSTVGYhsavrAGSVKNLisftrksaestAQWPNLPWLHTDSWIK-----SSKVLPASNIGSQSESQ 673
Cdd:PLN02246   114 IAKQAKASGAKLIITQSCY-----VDKLKGL-----------AEDDGVTVVTIDDPPEgclhfSELTQADENELPEVEIS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLM----RRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMVCG---GTAI 746
Cdd:PLN02246   178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGlrvGAAI 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 LFSPlTFIRNPLLWLqtISDYKAThsAGPnFAFELVirrLEADKAKA-HDYDLSSMIFFMIAAEPVrQKTLKRFVELTRP 825
Cdd:PLN02246   254 LIMP-KFEIGALLEL--IQRHKVT--IAP-FVPPIV---LAIAKSPVvEKYDLSSIRMVLSGAAPL-GKELEDAFRAKLP 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 yglsQEVMAPGYGLAE-NCVFVGCAYGKKKPILVDwQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKEGEIWISSPS 904
Cdd:PLN02246   324 ----NAVLGQGYGMTEaGPVLAMCLAFAKEPFPVK-SG--SCGTVVRN---AELKIVDPETGASLPR-NQPGEICIRGPQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgc 983
Cdd:PLN02246   393 IMKGYLNDPEATANTIDKD-------GWLHTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD--- 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  984 CAVISVPEDVLSakgiSLPdasdeVGLVVIAElkdGKPVDKDIIKQIesrVAEEhgvtVASVKLIRP----RTISKTTSG 1059
Cdd:PLN02246   463 AAVVPMKDEVAG----EVP-----VAFVVRSN---GSEITEDEIKQF---VAKQ----VVFYKRIHKvffvDSIPKAPSG 523


                   ....
gi 1973708721 1060 KIKR 1063
Cdd:PLN02246   524 KILR 527
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
664-991 7.54e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 82.99  E-value: 7.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  664 SNIGSQSESQPDDLCFlqfTSGSTGDAKGVMITHGGL----IHNVKLMRRryrsTSNTVLVSWLPQYHDMGLigGLFT-- 737
Cdd:PRK06839   141 DNFVEKNESASFIICY---TSGTTGKPKGAVLTQENMfwnaLNNTFAIDL----TMHDRSIVLLPLFHIGGI--GLFAfp 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  738 AMVCGGTAILfsPLTFirNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAkahdyDLSSMIFFMIAAEPVRQKTLK 817
Cdd:PRK06839   212 TLFAGGVIIV--PRKF--EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETT-----NLQSVRWFYNGGAPCPEELMR 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  818 RFVELTRPYGlsqevmaPGYGLAENC--VFvgcaygkkkpILVDWQGRICCGYVDPNDADVDIRIVDADTGlEVdEDGKE 895
Cdd:PRK06839   283 EFIDRGFLFG-------QGFGMTETSptVF----------MLSEEDARRKVGSIGKPVLFCDYELIDENKN-KV-EVGEV 343

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 GEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVES 974
Cdd:PRK06839   344 GELLIRGPNVMKEYWNRPDATEETIQD--------GWLCTGDLARVDEdGFVYIVGRKKEMIISGGENIYPLEVEQVINK 415

                          330
                   ....*....|....*..
gi 1973708721  975 SSELLRpgcCAVISVPE 991
Cdd:PRK06839   416 LSDVYE---VAVVGRQH 429
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 22-94 2.23e-15

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 81.03  E-value: 2.23e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 495-1063 3.21e-15

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 81.77  E-value: 3.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  495 DSYLKHWAAKEITQnkTLYTWINEEGAVVcQRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCL 574
Cdd:cd05968     64 EQLLDKWLADTRTR--PALRWEGEDGTSR-TLTYGELLYEVKRLANGL---RALGVGKGDRVGIYLPMIPEIVPAFLAVA 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  575 RAKVVPVPVLPPDPLqrgGQALTKIENiaklCNAVAILSTVGYhsaVRAGSVKNLISFTRKSAESTAQ-----------W 643
Cdd:cd05968    138 RIGGIVVPIFSGFGK---EAAATRLQD----AEAKALITADGF---TRRGREVNLKEEADKACAQCPTvekvvvvrhlgN 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  644 PNLPWLHTDSWIKSSKvlpASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWL 723
Cdd:cd05968    208 DFTPAKGRDLSYDEEK---ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWF 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  724 PqyhDMGLIGG---LFTAMVCGGTAILF--SPlTFIRNPLLWlQTISDYKATH-SAGPNfafelVIRRLEA---DKAKAH 794
Cdd:cd05968    285 T---DLGWMMGpwlIFGGLILGATMVLYdgAP-DHPKADRLW-RMVEDHEITHlGLSPT-----LIRALKPrgdAPVNAH 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  795 dyDLSSMIFFMIAAEPVRQKTLKRFVELtrpyglsqevmapgyglaencvfVGcayGKKKPIL-----VDWQGRICCGYV 869
Cdd:cd05968    355 --DLSSLRVLGSTGEPWNPEPWNWLFET-----------------------VG---KGRNPIInysggTEISGGILGNVL 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  870 ----DPNDADVDIRIVDADTgleVDEDGK-----EGEIWISSPSAGI--GYWGKEELSQKTFrnkLQKFPGrKYTRtGDL 938
Cdd:cd05968    407 ikpiKPSSFNGPVPGMKADV---LDESGKparpeVGELVLLAPWPGMtrGFWRDEDRYLETY---WSRFDN-VWVH-GDF 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  939 GRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEDVlsaKGislpdaSDEVGLVViaeLK 1017
Cdd:cd05968    479 AYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE---SAAIGVPHPV---KG------EAIVCFVV---LK 543

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1018 DGKPVDKDIIKQIESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1063
Cdd:cd05968    544 PGVTPTEALAEELMERVADELG------KPLSPERIlfvkdlPKTRNAKVMR 589
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 671-975 4.38e-15

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 80.48  E-value: 4.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMVCGGTAILFSP 750
Cdd:cd17640     84 ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYTSI 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  751 LTFirnpllwLQTISDYKATHSAGpnfafelVIRRLEADKAKAHDyDLSSMiffmiaaEPVRQKTLKRFVELTR-PYGLS 829
Cdd:cd17640    163 RTL-------KDDLKRVKPHYIVS-------VPRLWESLYSGIQK-QVSKS-------SPIKQFLFLFFLSGGIfKFGIS 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 QE-VMAP---------------GYGLAENCVfVGCAYGKKKPILvdwqgriccGYVDPNDADVDIRIVDADTGlEVDEDG 893
Cdd:cd17640    221 GGgALPPhvdtffeaigievlnGYGLTETSP-VVSARRLKCNVR---------GSVGRPLPGTEIKIVDPEGN-VVLPPG 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  894 KEGEIWISSPSAGIGYWGKEE-----LSQKTFRNklqkfpgrkytrTGDLGR-VIQGNLFITGRIKDLIIVA-GRNIYSA 966
Cdd:cd17640    290 EKGIVWVRGPQVMKGYYKNPEatskvLDSDGWFN------------TGDLGWlTCGGELVLTGRAKDTIVLSnGENVEPQ 357


                   ....*....
gi 1973708721  967 DVEKTVESS 975
Cdd:cd17640    358 PIEEALMRS 366
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 674-1063 4.62e-15

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 80.62  E-value: 4.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTaILFSPLTF 753
Cdd:PRK09088   134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS-ILVSNGFE 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 IRNPLLWLQTiSDYKATHSAG-PNFAfeLVIRRLEADKAKAhdydLSSMIFFMIAAEPVRQKTLKRFVELTRPyglsqev 832
Cdd:PRK09088   213 PKRTLGRLGD-PALGITHYFCvPQMA--QAFRAQPGFDAAA----LRHLTALFTGGAPHAAEDILGWLDDGIP------- 278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAEncvfVGCAYGkkkpILVDwQGRI-----CCGYVDPNdadVDIRIVDADtglevDED---GKEGEIWISSPS 904
Cdd:PRK09088   279 MVDGFGMSE----AGTVFG----MSVD-CDVIrakagAAGIPTPT---VQTRVVDDQ-----GNDcpaGVPGELLLRGPN 341

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTfrnklqkFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgc 983
Cdd:PRK09088   342 LSPGYWRRPQATARA-------FTGDGWFRTGDIARRdADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRE--- 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  984 CAVISVpedvlsakgislPDAS-DEVGLVVIAeLKDGKPVD-KDIIKQIESRVAE----EHGVTVASVklirPRtiskTT 1057
Cdd:PRK09088   412 CAVVGM------------ADAQwGEVGYLAIV-PADGAPLDlERIRSHLSTRLAKykvpKHLRLVDAL----PR----TA 470


                   ....*.
gi 1973708721 1058 SGKIKR 1063
Cdd:PRK09088   471 SGKLQK 476
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 673-992 5.86e-15

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 79.82  E-value: 5.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILfSPLT 752
Cdd:cd17650     91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVI-CPDE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FIRNPLLWLQTISDYKAThsagpnfAFELV---IRRLEADKAKaHDYDLSSMIFFMIAAEPVrqkTLKRFVELTRPYGLS 829
Cdd:cd17650    170 VKLDPAALYDLILKSRIT-------LMESTpalIRPVMAYVYR-NGLDLSAMRLLIVGSDGC---KAQDFKTLAARFGQG 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 QEVMApGYGLAENCVFVGCAYGKKKPILVdwQGRICCGYVDPNDAdvdIRIVDADtgLEVDEDGKEGEIWISSPSAGIGY 909
Cdd:cd17650    239 MRIIN-SYGVTEATIDSTYYEEGRDPLGD--SANVPIGRPLPNTA---MYVLDER--LQPQPVGVAGELYIGGAGVARGY 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  910 WGKEELSQKTF-RNKLQkfPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLRPGCC--A 985
Cdd:cd17650    311 LNRPELTAERFvENPFA--PGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIE------SQLARHPAIdeA 382


                   ....*..
gi 1973708721  986 VISVPED 992
Cdd:cd17650    383 VVAVRED 389
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 516-974 7.93e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 80.17  E-value: 7.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  516 INEEGAVvcqrTYAELDSNASCIAHKLLtsrKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQ----- 590
Cdd:PRK06164    30 IDEDRPL----SRAELRALVDRLAAWLA---AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHevahi 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  591 --RGGQALTKIENIAKLCNAVAILSTVGyHSAVRAgsVKNLISFTRKSAESTAQWP----NLPWLHtdswiksskvLPAS 664
Cdd:PRK06164   103 lgRGRARWLVVWPGFKGIDFAAILAAVP-PDALPP--LRAIAVVDDAADATPAPAPgarvQLFALP----------DPAP 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  665 NIGSQSESQPDDLCFLQFT-SGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLftAMVCGG 743
Cdd:PRK06164   170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL--GALAGG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  744 TAILFSPlTFIRNPLLwlQTISDYKATHSAGPNfafELVIRRLEADKAKAhdyDLSSMIFFMIAA-----EPVRQKTLKR 818
Cdd:PRK06164   248 APLVCEP-VFDAARTA--RALRRHRVTHTFGND---EMLRRILDTAGERA---DFPSARLFGFASfapalGELAALARAR 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FVELTRPYGlSQEVMApgyglaencvFVGCaygkkKPILVDWQGRICCGYVdPNDADVDIRIVDADTGlEVDEDGKEGEI 898
Cdd:PRK06164   319 GVPLTGLYG-SSEVQA----------LVAL-----QPATDPVSVRIEGGGR-PASPEARVRARDPQDG-ALLPDGESGEI 380

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721  899 WISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQGNLFI-TGRIKDLIIVAGRNIYSADVEKTVES 974
Cdd:PRK06164   381 EIRAPSLMRGYLDNPDATARALTDD-------GYFRTGDLGYTRGDGQFVyQTRMGDSLRLGGFLVNPAEIEHALEA 450
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 676-1063 8.33e-15

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 78.14  E-value: 8.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMVCggtAILFSPLTFIR 755
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH----VGGLAILVRS---LLAGAELVLLE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 NPLLWLQTISDYKATHSAgpnfafeLV---IRRLEADKAKAHDYDLSSMIFfmIAAEPVRQKTLKRFVELTRPyglsqev 832
Cdd:cd17630     74 RNQALAEDLAPPGVTHVS-------LVptqLQRLLDSGQGPAALKSLRAVL--LGGAPIPPELLERAADRGIP------- 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAEncvFVGCAYGKKkpilvdwQGRICCGYVDPNDADVDIRIVDadtglevdedgkEGEIWISSPSAGIGYWGK 912
Cdd:cd17630    138 LYTTYGMTE---TASQVATKR-------PDGFGRGGVGVLLPGRELRIVE------------DGEIWVGGASLAMGYLRG 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  913 EELSQktfrnklqkFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPE 991
Cdd:cd17630    196 QLVPE---------FNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD---AFVVGVPD 263

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  992 DVLSAKgislpdasdevgLVVIAELKDGKPVDkdiikQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKR 1063
Cdd:cd17630    264 EELGQR------------PVAVIVGRGPADPA-----ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDR 318
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
19-270 9.45e-15

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 79.19  E-value: 9.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTQ 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 LEEM-DLHKLALIDsLTGEYHDIN-VAEDYMSLVSLTLDIQDKAKDTNRIGIHAVSEIasDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSARR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMNLWKKISESLLIKVCCNTEVQAVRRNGSGVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234

                          250       260
                   ....*....|....*....|....*
gi 1973708721  246 DITNssGETEHkeFDKIIIsgAFPF 270
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV--TVPP 253
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 672-969 7.80e-14

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 76.58  E-value: 7.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlvsWLpQYHDMGL---IGGLFTAMVCGGTAILF 748
Cdd:cd17643     90 TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFdfsVWEIWGALLHGGRLVVV 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTfIRNPLLWLQTISDYKAT-HSAGPNfAFELVIrrLEADKAKAHDYDLSSMIFfmiAAEPVRQKTLKRFVEltrPYG 827
Cdd:cd17643    166 PYEV-ARSPEDFARLLRDEGVTvLNQTPS-AFYQLV--EAADRDGRDPLALRYVIF---GGEALEAAMLRPWAG---RFG 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  828 LSQEVMAPGYGLAENCVFVgcaygKKKPILVDwqgriccgYVDPNDA--------DVDIRIVDADtGLEVdEDGKEGEIW 899
Cdd:cd17643    236 LDRPQLVNMYGITETTVHV-----TFRPLDAA--------DLPAAAAspigrplpGLRVYVLDAD-GRPV-PPGVVGELY 300

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721  900 ISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:cd17643    301 VSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARrLPDGELEYLGRADEQVKIRGFRIELGEIE 371
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 521-1063 8.17e-14

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 76.56  E-value: 8.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAKVVPVPVLPPDPLQRggqalt 597
Cdd:cd12116      5 AVRDddrSLSYAELDERANRLAARL---RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR------ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 kIENIAKLCNAVAILstvgyhsavragsvknlisfTRKSAESTAQWPNLPWLHtdswikSSKVLPASNIGSQSESQPDDL 677
Cdd:cd12116     76 -LRYILEDAEPALVL--------------------TDDALPDRLPAGLPVLLL------ALAAAAAAPAAPRTPVSPDDL 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMVCGGTAILFSPLTfIRNP 757
Cdd:cd12116    129 AYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAPRET-QRDP 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  758 LLWLQTISDYKATH-SAGPNFAfelvirRLEAD---KAKAHdydlssmIFFMIAAEPVrqktlkrfveltrPYGLSQEVM 833
Cdd:cd12116    207 EALARLIEAHSITVmQATPATW------RMLLDagwQGRAG-------LTALCGGEAL-------------PPDLAARLL 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  834 APG------YGLAENCVfvgcaygkkkpilvdWQgriCCGYVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWI 900
Cdd:cd12116    261 SRVgslwnlYGPTETTI---------------WS---TAARVTAAAGPIPIgrplantQVYVLDAALRPVPPGVPGELYI 322

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  901 SSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELL 979
Cdd:cd12116    323 GGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRAdGRLEYLGRADGQVKIRGHRIELGEIE------AALA 396

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  980 R-PGC--CAVISVPEDvlsakgislpdasDEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTVAsvkLIRPRTISKT 1056
Cdd:cd12116    397 AhPGVaqAAVVVREDG-------------GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSA---FVRLDALPLT 460


                   ....*..
gi 1973708721 1057 TSGKIKR 1063
Cdd:cd12116    461 ANGKLDR 467
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 675-969 9.63e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 76.35  E-value: 9.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhdmgligGLFTAmVCGGTAIL--FSPLT 752
Cdd:cd05910     85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGP-ALGLTSVIpdMDPTR 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FIR-NPLLWLQTISDYKATHSAGPNFAFELVIRRLEAdkakaHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPyglSQE 831
Cdd:cd05910    157 PARaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ-----HGITLPSLRRVLSAGAPVPIALAARLRKMLSD---EAE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  832 VMAPgYGLAEnCVFVgCAYGKKKPI-----LVDWQGRICCGY-VDPNDADV----DIRIVDADTGLEVDeDGKEGEIWIS 901
Cdd:cd05910    229 ILTP-YGATE-ALPV-SSIGSRELLatttaATSGGAGTCVGRpIPGVRVRIieidDEPIAEWDDTLELP-RGEIGEITVT 304

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  902 SPSAGIGYWGKEelsQKTFRNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:cd05910    305 GPTVTPTYVNRP---VATALAKIDDNSEGFWHRMGDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVE 370
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 671-956 9.73e-14

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 76.48  E-value: 9.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDM------------GLIG--- 733
Cdd:cd17639     84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllGPDDRYLAYLPLAHIFelaaenvclyrgGTIGygs 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  734 --GLFTAMV--CGGTAILFSPLTFIRNPLLWlQTIsdYKATHS--AGPNFAFELVIRRLEADKAKAHDYDLSSMIFFMIA 807
Cdd:cd17639    164 prTLTDKSKrgCKGDLTEFKPTLMVGVPAIW-DTI--RKGVLAklNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELV 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  808 AEPVRQKT-----------------LKRFVE-LTRPyglsqevMAPGYGLAENCvfvGCAygkkkPILVDWQGRICCgyV 869
Cdd:cd17639    241 FKKVRAALggrlrymlsggaplsadTQEFLNiVLCP-------VIQGYGLTETC---AGG-----TVQDPGDLETGR--V 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  870 DPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqkFPGRkYTRTGDLGRVI-QGNLF 947
Cdd:cd17639    304 GPPLPCCEIKLVDwEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAF------DGDG-WFHTGDIGEFHpDGTLK 376


                   ....*....
gi 1973708721  948 ITGRIKDLI 956
Cdd:cd17639    377 IIDRKKDLV 385
y4iL_like cd08152
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ...
 1759-2016 1.38e-13

Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.


Pssm-ID: 163708  Cd Length: 305  Bit Score: 73.83  E-value: 1.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1759 KGYLKLYDDiqgLPEH---NIFGPGKKYTVIVRHSNSLSADDDARL-DARGAALRIL--SDEK---GDDSPLLDLTLKTG 1829
Cdd:cd08152     16 KAEFTVLDD---LPPElaqGLFAEPGTYPAVIRFSNAPGDILDDSVpDPRGMAIKVLgvPGEKllpEEDATTQDFVLVNH 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1830 KAFYARTISDFA--TWLVCGLAAREEHVKRVPH----VRDAVWTSLRQADSYAEMH-----------YYSniCRLFRFKD 1892
Cdd:cd08152     93 PVFFARDAKDYLalLKLLARTTSLPDGAKAALSaplrGALRVLEAAGGESPTLKLGghppahplgetYWS--QAPYRFGD 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1893 GqemYVKFKLRPsdknigedtgkVEPSgiLPPETGAIPRDANDT---RPLL--FLAEdfqnrvkspNGVRYIFQLQV--- 1964
Cdd:cd08152    171 Y---VAKYSVVP-----------ASPA--LPALTGKELDLTDDPdalREALadFLAE---------NDAEFEFRIQLctd 225

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721 1965 ---MPVpqdEaardialDCTKPWDESQFPYIDVGEVIIN------ENLTKEGSERLEFNPF 2016
Cdd:cd08152    226 lekMPI---E-------DASVEWPEALSPFVPVATITIPpqdfdsPARQRAFDDNLSFNPW 276
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 674-969 1.87e-13

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 75.10  E-value: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMVCGGTAILfspltf 753
Cdd:cd17649     93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVL------ 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  754 iRNPLLWLQTISDYKATHSAG-------PNFAFELVirrLEADKAKAHDYdlSSMIFFMIAAEPVRQKTLKRF----VEL 822
Cdd:cd17649    166 -RPDELWASADELAEMVRELGvtvldlpPAYLQQLA---EEADRTGDGRP--PSLRLYIFGGEALSPELLRRWlkapVRL 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSQEVMAPgyglaenCVFVGCAY----GKKKPIlvdwqGRICCGYVdpndadvdIRIVDADTGLEvdEDGKEGEI 898
Cdd:cd17649    240 FNAYGPTEATVTP-------LVWKCEAGaaraGASMPI-----GRPLGGRS--------AYILDADLNPV--PVGVTGEL 297

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  899 WISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:cd17649    298 YIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIE 369
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 671-1063 2.97e-13

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 74.72  E-value: 2.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLcflQFTSGSTGDAKGVMITH-GGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDMGLIgGLFTAMVCGGTAIL 747
Cdd:cd05929    124 EAAGWKM---LYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVL 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 ---FSPLTFirnpllwLQTISDYKATHSagpNFAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEP----VRQKTLKrfv 820
Cdd:cd05929    200 mekFDPEEF-------LRLIERYRVTFA---QFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppwVKEQWID--- 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 eltrpygLSQEVMAPGYGLAEnCVFVGCAYGKkkpilvDWQ------GRICCGyvdpndadvDIRIVDADtGLEVdEDGK 894
Cdd:cd05929    267 -------WGGPIIWEYYGGTE-GQGLTIINGE------EWLthpgsvGRAVLG---------KVHILDED-GNEV-PPGE 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  895 EGEIWIsSPSAGIGY-----WGKEELSQKTFRNklqkfpgrkytrTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADV 968
Cdd:cd05929    322 IGEVYF-ANGPGFEYtndpeKTAAARNEGGWST------------LGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEI 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  969 EKtvesssellrpgccAVISVPeDVLSAKGISLPDasDEVGLVVIAELKDGKPVDKDiiKQIESRVAEEHGVTVASVKLi 1048
Cdd:cd05929    389 EN--------------ALIAHP-KVLDAAVVGVPD--EELGQRVHAVVQPAPGADAG--TALAEELIAFLRDRLSRYKC- 448

                          410       420
                   ....*....|....*....|.
gi 1973708721 1049 rPRTIS------KTTSGKIKR 1063
Cdd:cd05929    449 -PRSIEfvaelpRDDTGKLYR 468
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
875-1069 2.98e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 74.61  E-value: 2.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  875 DVDIRIVDadtGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKfpgrkytrTGDLGRV-IQGNLFITGRIK 953
Cdd:PRK03640   315 PCELKIEK---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK--------TGDIGYLdEEGFLYVLDRRS 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  954 DLIIVAGRNIYSADVEktvesssellrpgccAVISVPEDVLSAKGISLPDasDEVGLVVIAELKDGKPVDKDIIKQIesr 1033
Cdd:PRK03640   384 DLIISGGENIYPAEIE---------------EVLLSHPGVAEAGVVGVPD--DKWGQVPVAFVVKSGEVTEEELRHF--- 443

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1973708721 1034 vAEEHgvtVASVKliRPRTI------SKTTSGKIKRFEcLKQ 1069
Cdd:PRK03640   444 -CEEK---LAKYK--VPKRFyfveelPRNASGKLLRHE-LKQ 478
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 671-1065 3.98e-13

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 74.03  E-value: 3.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLC--------FLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRS---TSNTVLVSWLPqyhdMGL-IGGLFTA 738
Cdd:COG1541     71 DNYPFGLFavpleeivRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAagvRPGDRVQNAFG----YGLfTGGLGLH 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  739 MVC---GGTAILFSPLtfirNPLLWLQTISDYKATHSAG-PNFAFELvIRRLEADKAKAHDYDLSSMIFfmiAAEPVRQK 814
Cdd:COG1541    147 YGAerlGATVIPAGGG----NTERQLRLMQDFGPTVLVGtPSYLLYL-AEVAEEEGIDPRDLSLKKGIF---GGEPWSEE 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  815 TLKRFVELtrpYGLsqEVMApGYGLAENCVFVG--CAYgkkKPILVDWQGRIccgYVDpndadvdirIVDADTGlEVDED 892
Cdd:COG1541    219 MRKEIEER---WGI--KAYD-IYGLTEVGPGVAyeCEA---QDGLHIWEDHF---LVE---------IIDPETG-EPVPE 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  893 GKEGEIWISSpsagigywgkeelsqktfrnkLQK--FPGRKYtRTGDLGRVIQGN----------LFITGRIKDLIIVAG 960
Cdd:COG1541    277 GEEGELVVTT---------------------LTKeaMPLIRY-RTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRG 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  961 RNIYSADVEKTVESSSELlrpGCCAVISVPEDvlsakgislpDASDEvgLVVIAELKDGKPVDkDIIKQIESRVAEEHGV 1040
Cdd:COG1541    335 VNVFPSQIEEVLLRIPEV---GPEYQIVVDRE----------GGLDE--LTVRVELAPGASLE-ALAEAIAAALKAVLGL 398

                          410       420
                   ....*....|....*....|....*
gi 1973708721 1041 TVAsVKLIRPRTISKTTsGKIKRFE 1065
Cdd:COG1541    399 RAE-VELVEPGSLPRSE-GKAKRVI 421
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 670-1065 1.21e-12

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 72.91  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKgvMITH------GGLI-----HNVKLMRRRYrSTSNTvlvSWlpqyhDMGLIGGLFTA 738
Cdd:cd05970    180 SYPCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVtakywQNVREGGLHL-TVADT---GW-----GKAVWGKIYGQ 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  739 MVCGGTAILFSPLTFIrnPLLWLQTISDYKATHSAGPNFAFELVIRrleadkAKAHDYDLSSMIFFMIAAEPVRQKTLKR 818
Cdd:cd05970    249 WIAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIR------EDLSRYDLSSLRYCTTAGEALNPEVFNT 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  819 FVELTrpyGLSqevMAPGYGLAENCVFVGCAYG-KKKPILVdwqGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGE 897
Cdd:cd05970    321 FKEKT---GIK---LMEGFGQTETTLTIATFPWmEPKPGSM---GKPAPGY--------EIDLIDRE-GRSC-EAGEEGE 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  898 IWISSpSAGI------GYWGKEELSQKTFRNklqkfpgrKYTRTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEK 970
Cdd:cd05970    382 IVIRT-SKGKpvglfgGYYKDAEKTAEVWHD--------GYYHTGDAAwMDEDGYLWFVGRTDDLIKSSGYRIGPFEVES 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  971 TVESSSELLRpgcCAVISVPEDVLsakgislpdasdevGLVVIAEL---KDGKPVDkDIIKQIESRVAEehgVTvASVKL 1047
Cdd:cd05970    453 ALIQHPAVLE---CAVTGVPDPIR--------------GQVVKATIvlaKGYEPSE-ELKKELQDHVKK---VT-APYKY 510

                          410       420
                   ....*....|....*....|....
gi 1973708721 1048 irPRTIS------KTTSGKIKRFE 1065
Cdd:cd05970    511 --PRIVEfvdelpKTISGKIRRVE 532
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 662-992 2.24e-12

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 72.23  E-value: 2.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  662 PASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLI-----HNVKLmrrryRSTSNTVLVSWLPQYHdmglIGglf 736
Cdd:PRK06145   136 GGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksidHVIAL-----GLTASERLLVVGPLYH----VG--- 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 tAMVCGGTAILF--SPLTFIRN--PLLWLQTISDYKAThsaGPNFAFELVIRRL---EADKakahdYDLSSMIFFMIAAE 809
Cdd:PRK06145   204 -AFDLPGIAVLWvgGTLRIHREfdPEAVLAAIERHRLT---CAWMAPVMLSRVLtvpDRDR-----FDLDSLAWCIGGGE 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  810 PVRQKTLKRFVELTRpyglsQEVMAPGYGLAENCVFVGCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLEv 889
Cdd:PRK06145   275 KTPESRIRDFTRVFT-----RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRAL--------AHVEIRIADGAGRWL- 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  890 dEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADV 968
Cdd:PRK06145   341 -PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG--------DWFRSGDVGYLDeEGFLYLTDRKKDMIISGGENIASSEV 411

                          330       340
                   ....*....|....*....|....
gi 1973708721  969 EKTVESSSELLRpgcCAVISVPED 992
Cdd:PRK06145   412 ERVIYELPEVAE---AAVIGVHDD 432
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 674-970 2.92e-12

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 71.73  E-value: 2.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYH---DMGLIGGLFTamvcGGTAILFS- 749
Cdd:cd05932    136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHvteRVFVEGGSLY----GGVLVAFAe 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 -------------PLTFIRNPLLWLQTisdYKATHSAGPNFAFEL-----VIRRLEadKAKAHD-YDLSSMIFFMIAAEP 810
Cdd:cd05932    212 sldtfvedvqrarPTLFFSVPRLWTKF---QQGVQDKIPQQKLNLllkipVVNSLV--KRKVLKgLGLDQCRLAGCGSAP 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  811 VRQKTLkrfvELTRPYGLSqevMAPGYGLAENCvfvgcAYGkkkpiLVDWQGRICCGYVDPNDADVDIRIVDadtglevd 890
Cdd:cd05932    287 VPPALL----EWYRSLGLN---ILEAYGMTENF-----AYS-----HLNYPGRDKIGTVGNAGPGVEVRISE-------- 341

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  891 edgkEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVA-GRNIYSADV 968
Cdd:cd05932    342 ----DGEILVRSPALMMGYYKDPEATAEAFTAD-------GFLRTGDKGELdADGNLTITGRVKDIFKTSkGKYVAPAPI 410


                   ..
gi 1973708721  969 EK 970
Cdd:cd05932    411 EN 412
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 672-1003 3.07e-12

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 71.43  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMVCGGTAILFSPL 751
Cdd:cd17645    101 TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFD-ASAWEIFPHLTAGAALHVVPSE 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TfirnpLLWLQTISDYKATHSAGPNFAFELVIRRLEAdkakahdYDLSSMIFFMIAAEpvrqkTLKRFVEltRPYGLSQe 831
Cdd:cd17645    180 R-----RLDLDALNDYFNQEGITISFLPTGAAEQFMQ-------LDNQSLRVLLTGGD-----KLKKIER--KGYKLVN- 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  832 vmapGYGLAENCVFVGCAYgkkkpilvdwqgriccgyVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWISSPS 904
Cdd:cd17645    240 ----NYGPTENTVVATSFE------------------IDKPYANIPIgkpidntRVYILDEALQLQPIGVAGELCIAGEG 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 AGIGYWGKEELSQKTFRNKLQkFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELL---- 979
Cdd:cd17645    298 LARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLpDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIElaav 376

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1973708721  980 --------RPGCCAVISVPEDVLSAK-----GISLPD 1003
Cdd:cd17645    377 lakedadgRKYLVAYVTAPEEIPHEElrewlKNDLPD 413
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 516-1036 3.85e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 71.50  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  516 INEEGavvcQRTYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrG--- 592
Cdd:PRK07788    69 IDERG----TLTYAELDEQSNALARGLLAL---GVRAGDGVAVLARNHRGFVLALYAAGKV---------------Gari 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  593 -----GQALTKIENIAKLCNAVAILSTVGYHSAVRA-----GSVKNLISFTRKSAESTAQWPNLpwlhtDSWI--KSSKV 660
Cdd:PRK07788   127 illntGFSGPQLAEVAAREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETL-----DDLIagSSTAP 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  661 LPASnigsqseSQPDDLCFLqfTSGSTGDAKGVMITH-------GGLIHNVKLmrrryRSTSNTVLVSwlPQYHDMGLiG 733
Cdd:PRK07788   202 LPKP-------PKPGGIVIL--TSGTTGTPKGAPRPEpsplaplAGLLSRVPF-----RAGETTLLPA--PMFHATGW-A 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  734 GLFTAMVCGGTAIL---FSPLTFIRNpllwlqtISDYKAThsagpnfafELVI------RRLEADKAKAHDYDLSSMIFF 804
Cdd:PRK07788   265 HLTLAMALGSTVVLrrrFDPEATLED-------IAKHKAT---------ALVVvpvmlsRILDLGPEVLAKYDTSSLKII 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  805 MIAAEPVRQKTLKRFVELTRP-----YGlSQEV----MAPGYGLAENcvfvgcaygkkkPILVdwqGRICCGyvdpndad 875
Cdd:PRK07788   329 FVSGSALSPELATRALEAFGPvlynlYG-STEVafatIATPEDLAEA------------PGTV---GRPPKG-------- 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  876 VDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYWGKeelsqktfRNKlQKFPGrkYTRTGDLGRVIQ-GNLFITGRIKD 954
Cdd:PRK07788   385 VTVKILDEN-GNEVPR-GVVGRIFVGNGFPFEGYTDG--------RDK-QIIDG--LLSSGDVGYFDEdGLLFVDGRDDD 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  955 LIIVAGRNIYSADVEktvesssELLRPgccavisvPEDVLSAKGISLPDasDEVG--LVVIAELKDGKPVDKDIIKQ-IE 1031
Cdd:PRK07788   452 MIVSGGENVFPAEVE-------DLLAG--------HPDVVEAAVIGVDD--EEFGqrLRAFVVKAPGAALDEDAIKDyVR 514


                   ....*
gi 1973708721 1032 SRVAE 1036
Cdd:PRK07788   515 DNLAR 519
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 673-972 5.86e-12

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 70.85  E-value: 5.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGL----IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTaILF 748
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQ-VYF 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 S-----------------PLTFIRNPLLW-----------------------------LQTISDYKATHSagPNFAFELV 782
Cdd:cd05933    227 AqpdalkgtlvktlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGES--PSPLFYRL 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  783 IRRLEADKAKAHdYDLSSMIFFMIAAEPVRQKTLKRFVELTRPYGlsqevmaPGYGLAENCvfvGCAYgkkkpILVDWQG 862
Cdd:cd05933    305 AKKLVFKKVRKA-LGLDRCQKFFTGAAPISRETLEFFLSLNIPIM-------ELYGMSETS---GPHT-----ISNPQAY 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  863 RI-CCGYVDPNdadVDIRIVdadtglEVDEDGkEGEIWISSPSAGIGYWGKEElsqKTfRNKLQKfpgRKYTRTGDLGRV 941
Cdd:cd05933    369 RLlSCGKALPG---CKTKIH------NPDADG-IGEICFWGRHVFMGYLNMED---KT-EEAIDE---DGWLHSGDLGKL 431

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1973708721  942 -IQGNLFITGRIKDLIIVA-GRNIYSADVEKTV 972
Cdd:cd05933    432 dEDGFLYITGRIKELIITAgGENVPPVPIEDAV 464
PRK05857 PRK05857
fatty acid--CoA ligase;
662-1063 7.67e-12

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 70.42  E-value: 7.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  662 PASNIGSQSesqpDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMR----RRYRSTSNTVLVSWLPQYHdmglIGGLFT 737
Cdd:PRK05857   160 LAGNADQGS----EDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQkeglNWVTWVVGETTYSPLPATH----IGGLWW 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  738 AMVC---GGTAIlfsplTFIRNPLLWLQTISDYK-ATHSAGPNFAFELVirrleaDKAKAHDYDLSSMIFF------MIA 807
Cdd:PRK05857   232 ILTClmhGGLCV-----TGGENTTSLLEILTTNAvATTCLVPTLLSKLV------SELKSANATVPSLRLVgyggsrAIA 300

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  808 AEpvrqktlKRFVELTrpyGLSQevmAPGYGLAENCVFVGCAYGKKKPIlvdwqGRICCGYVDPNDADVDIRIVDADTGL 887
Cdd:PRK05857   301 AD-------VRFIEAT---GVRT---AQVYGLSETGCTALCLPTDDGSI-----VKIEAGAVGRPYPGVDVYLAATDGIG 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  888 EVDEDGKE----GEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDL-GRVIQGNLFITGRIKDLIIVAGRN 962
Cdd:PRK05857   363 PTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLID--------GWVNTGDLlERREDGFFYIKGRSSEMIICGGVN 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  963 IYSADVEKTVESSSELLRPGCcavISVPEDVLSAKgislpdasdeVGLVVIAELKdgkpVDKDIIKQIESRVAEEHGVTV 1042
Cdd:PRK05857   435 IAPDEVDRIAEGVSGVREAAC---YEIPDEEFGAL----------VGLAVVASAE----LDESAARALKHTIAARFRRES 497

                          410       420
                   ....*....|....*....|....*..
gi 1973708721 1043 ASVKliRPRT------ISKTTSGKIKR 1063
Cdd:PRK05857   498 EPMA--RPSTivivtdIPRTQSGKVMR 522
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
498-952 1.35e-11

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 69.54  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  498 LKHWAAKEitQNKTLYTWINEEgavvcqRTYAELDSNASCIAHKLLTSRKPTIKPgdrvLLVHvPGLDF--VDSFFGCLR 575
Cdd:PRK04813     8 IEEFAQTQ--PDFPAYDYLGEK------LTYGQLKEDSDALAAFIDSLKLPDKSP----IIVF-GHMSPemLATFLGAVK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  576 AKVVPVPVLPPDPLQRggqaLTKIENIAKlcnAVAILSTVGyhSAVRAGSVKNLisftrKSAESTAQWPNLPWLHTDSWI 655
Cdd:PRK04813    75 AGHAYIPVDVSSPAER----IEMIIEVAK---PSLIIATEE--LPLEILGIPVI-----TLDELKDIFATGNPYDFDHAV 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  656 KsskvlpasnigsqsesqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGgL 735
Cdd:PRK04813   141 K-----------------GDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMD-L 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  736 FTAMVCGGTaiLFS-PLTFIRNPLLWLQTISDYK-ATHSAGPNFAfELVIrrLEADKAKAHdydLSSMIFFMIAAE--PV 811
Cdd:PRK04813   203 YPTLASGGT--LVAlPKDMTANFKQLFETLPQLPiNVWVSTPSFA-DMCL--LDPSFNEEH---LPNLTHFLFCGEelPH 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  812 R--QKTLKRFveltrPyglsQEVMAPGYGLAENCVFVG--------CAYGKKKPIlvdwqgriccGYVDPndaDVDIRIV 881
Cdd:PRK04813   275 KtaKKLLERF-----P----SATIYNTYGPTEATVAVTsieitdemLDQYKRLPI----------GYAKP---DSPLLII 332

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721  882 DADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnklqKFPGRKYTRTGDLGRVIQGNLFITGRI 952
Cdd:PRK04813   333 DEE--GTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF----TFDGQPAYHTGDAGYLEDGLLFYQGRI 397
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 674-1065 1.55e-11

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 69.00  E-value: 1.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLI-H--NVKLMRRRYRSTSNtvlVSWLPQyhDMGLIGGLFTAMV----CGGTAI 746
Cdd:cd05971     87 SDDPALIIYTSGTTGPPKGALHAHRVLLgHlpGVQFPFNLFPRDGD---LYWTPA--DWAWIGGLLDVLLpslyFGVPVL 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  747 LFSPLTFirNPLLWLQTISDYKATHSAGPNFAfeLVIRRLEADKAKAHDYDLSSMIffmIAAEPVRQKTLkrfVELTRPY 826
Cdd:cd05971    162 AHRMTKF--DPKAALDLMSRYGVTTAFLPPTA--LKMMRQQGEQLKHAQVKLRAIA---TGGESLGEELL---GWAREQF 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 GLSqevMAPGYGLAE-NCVFVGCA-YGKKKPILVdwqGRICCGYvdpndadvDIRIVDaDTGLEVDEdGKEGEIWISSPS 904
Cdd:cd05971    232 GVE---VNEFYGQTEcNLVIGNCSaLFPIKPGSM---GKPIPGH--------RVAIVD-DNGTPLPP-GEVGEIAVELPD 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  905 --AGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR- 980
Cdd:cd05971    296 pvAFLGYWNNPSATEKKMAGD--------WLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEEC------LLKh 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  981 PGccavisvpedVLSAKGISLPDAsdEVGLVVIA--ELKDGKPVDKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTS 1058
Cdd:cd05971    362 PA----------VLMAAVVGIPDP--IRGEIVKAfvVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429


                   ....*..
gi 1973708721 1059 GKIKRFE 1065
Cdd:cd05971    430 GKIRRRE 436
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 670-1012 1.57e-11

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 69.46  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  670 SESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGL-IGGLFTAMVcgGTAILF 748
Cdd:PRK06334   178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLS--GVPVVF 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 S--PLtfirNPLLWLQTISDYKATHSAGPNFAFELVIRrleadKAKAHDYDLSSMIFFMIAAE----PVRQKTLKRFVEL 822
Cdd:PRK06334   256 AynPL----YPKKIVEMIDEAKVTFLGSTPVFFDYILK-----TAKKQESCLPSLRFVVIGGDafkdSLYQEALKTFPHI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TrpygLSQevmapGYGLAEnCVFVGCAYGKKKPilvdwQGRICCGYvdPNDAdVDIRIVDADTGLEVdEDGKEGEIWISS 902
Cdd:PRK06334   327 Q----LRQ-----GYGTTE-CSPVITINTVNSP-----KHESCVGM--PIRG-MDVLIVSEETKVPV-SSGETGLVLTRG 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  903 PSAGIGYWGKEelsqktFRNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIysadvekTVESSSELLRP 981
Cdd:PRK06334   388 TSLFSGYLGED------FGQGFVELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMV-------SLEALESILME 454

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1973708721  982 GCcavisvpedvlsakgiSLPDASDEVGLVV 1012
Cdd:PRK06334   455 GF----------------GQNAADHAGPLVV 469
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 676-1063 2.24e-11

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 67.43  E-value: 2.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLIH----NVKLMrrrYRSTSNTVLVSWlPQYHDMGLIGGLFtAMVCGGTAILFSPL 751
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIEsfvcNEDLF---NISGEDAILAPG-PLSHSLFLYGAIS-ALYLGGTFIGQRKF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 tfirNPLLWLQTISDYKAThsagpnfAFELVIRRLEAdKAKAHDYDLSSMIFFMIAA--EPVRQKTLKRfveltrpyGLS 829
Cdd:cd17633     76 ----NPKSWIRKINQYNAT-------VIYLVPTMLQA-LARTLEPESKIKSIFSSGQklFESTKKKLKN--------IFP 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 QEVMAPGYGLAE-NCVFVGCAYGKKKPILVdwqGRICcgyvdPNdadVDIRIVDADtglevdeDGKEGEIWISSPSAGIG 908
Cdd:cd17633    136 KANLIEFYGTSElSFITYNFNQESRPPNSV---GRPF-----PN---VEIEIRNAD-------GGEIGKIFVKSEMVFSG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  909 YWgKEELSQKTfrnklqkfpgrKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEllrpgccavi 987
Cdd:cd17633    198 YV-RGGFSNPD-----------GWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPG---------- 255

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721  988 svpedVLSAKGISLPDAsdEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHgvtVASvKLIRPRTISKTTSGKIKR 1063
Cdd:cd17633    256 -----IEEAIVVGIPDA--RFGEIAVALYSGDKLTYKQLKRFLKQKLSRYE---IPK-KIIFVDSLPYTSSGKIAR 320
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 682-1063 2.51e-11

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 68.57  E-value: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  682 FTSGSTGDAKGVM---ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVcGGTAIL---FSPLTFir 755
Cdd:PRK12406   159 YTSGTTGHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL-GGVLVLqprFDPEEL-- 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 npllwLQTISDYKATHSAGPNFAFelvIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPyglsqeVMAP 835
Cdd:PRK12406   236 -----LQLIERHRITHMHMVPTMF---IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYE 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  836 GYGLAENCVFVGCAYGK--KKPILVdwqGRICCGyvdpndadVDIRIVDADtGLEVdEDGKEGEIWISSPS-AGIGYWGK 912
Cdd:PRK12406   302 YYGSTESGAVTFATSEDalSHPGTV---GKAAPG--------AELRFVDED-GRPL-PQGEIGEIYSRIAGnPDFTYHNK 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  913 EELSQKTFRNKLqkfpgrkyTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIs 988
Cdd:PRK12406   369 PEKRAEIDRGGF--------ITSGDVGYLDAdGYLFLCDRKRDMVISGGVNIYPAEIE------AVLHAvPGVhdCAVF- 433

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  989 vpedvlsakGIslPDAsdEVGLVVIA--ELKDGKPVDKDIIK-QIESRVAeehGVTVASVKLIRPRtISKTTSGKI-KR 1063
Cdd:PRK12406   434 ---------GI--PDA--EFGEALMAvvEPQPGATLDEADIRaQLKARLA---GYKVPKHIEIMAE-LPREDSGKIfKR 495
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 876-1063 2.62e-11

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 68.74  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  876 VDIRIVDADTGlEVDEDGkEGEIWISSPSAGI--GYWGKEELSQKTFrnkLQKFPGrkYTRTGDLGRVIQ-GNLFITGRI 952
Cdd:cd05966    419 IEPAILDEEGN-EVEGEV-EGYLVIKRPWPGMarTIYGDHERYEDTY---FSKFPG--YYFTGDGARRDEdGYYWITGRV 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  953 KDLIIVAGRNIYSADVEktvesSSELLRPGC--CAVISVPEDVlsaKGISLpdasdeVGLVViaeLKDGKPVDKDIIKQI 1030
Cdd:cd05966    492 DDVINVSGHRLGTAEVE-----SALVAHPAVaeAAVVGRPHDI---KGEAI------YAFVT---LKDGEEPSDELRKEL 554

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1973708721 1031 ESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1063
Cdd:cd05966    555 RKHVRKEIG------PIATPDKIqfvpglPKTRSGKIMR 587
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 674-964 3.36e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 68.40  E-value: 3.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNV----KLMRRRYRSTSNTVLVSWLPQYHdmgliggLF-----TAMVCGGT 744
Cdd:cd05927    113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAH-------IFervveALFLYHGA 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  745 AILF---------------SPLTFIRNPLLwLQTISD-YKATHSAGP-------NFAFELVIRRLEADKAKAHDY-D--- 797
Cdd:cd05927    186 KIGFysgdirlllddikalKPTVFPGVPRV-LNRIYDkIFNKVQAKGplkrklfNFALNYKLAELRSGVVRASPFwDklv 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  798 -------LSSMIFFMI-AAEPVRQKTLKRFveltRPYgLSQEVMApGYGLAENCvfVGCAygkkkpilVDWQGRICCGYV 869
Cdd:cd05927    265 fnkikqaLGGNVRLMLtGSAPLSPEVLEFL----RVA-LGCPVLE-GYGQTECT--AGAT--------LTLPGDTSVGHV 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  870 DPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpGrkYTRTGDLGRvIQGNlfi 948
Cdd:cd05927    329 GGPLPCAEVKLVDvPEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED-----G--WLHTGDIGE-WLPN--- 397

                          330
                   ....*....|....*.
gi 1973708721  949 tGRIKdlIIVAGRNIY 964
Cdd:cd05927    398 -GTLK--IIDRKKNIF 410
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 498-1069 3.75e-11

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 68.26  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  498 LKHWAAKEIT----QNKTLYtWINEEGAVVcQRTYAELDSNASCIAHKLltSRKPTIKPGDRVLLV--HVPGLDFVDsfF 571
Cdd:cd05928     12 LDQWADKEKAgkrpPNPALW-WVNGKGDEV-KWSFRELGSLSRKAANVL--SGACGLQRGDRVAVIlpRVPEWWLVN--V 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  572 GCLRAKVVPVPVLPPDPLQ--------RGGQALTKIENIAKLCNAVAilstvgyhSAVRAGSVKNLISFTRKSAestaqw 643
Cdd:cd05928     86 ACIRTGLVFIPGTIQLTAKdilyrlqaSKAKCIVTSDELAPEVDSVA--------SECPSLKTKLLVSEKSRDG------ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  644 pnlpWLHTDSWIKSskvlpASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlVSWl 723
Cdd:cd05928    152 ----WLNFKELLNE-----ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASD-IMW- 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  724 pQYHDMG----LIGGLFTAMVCGGTAILFSPLTFirNPLLWLQTISDYKATHSAGPNFAFELVIRRleadkakahdyDLS 799
Cdd:cd05928    221 -NTSDTGwiksAWSSLFEPWIQGACVFVHHLPRF--DPLVILKTLSSYPITTFCGAPTVYRMLVQQ-----------DLS 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  800 SMIF-----FMIAAEPVRQKTLKRFVELTrpyGLSqevMAPGYGLAENCVFVGCAYGKK-KPilvdwqgriccGYVDPND 873
Cdd:cd05928    287 SYKFpslqhCVTGGEPLNPEVLEKWKAQT---GLD---IYEGYGQTETGLICANFKGMKiKP-----------GSMGKAS 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  874 ADVDIRIVDaDTGlEVDEDGKEGEIWIS-SPSAGIG----YWGKEELSQKTFRnklqkfpgRKYTRTGDLGRVIQ-GNLF 947
Cdd:cd05928    350 PPYDVQIID-DNG-NVLPPGTEGDIGIRvKPIRPFGlfsgYVDNPEKTAATIR--------GDFYLTGDRGIMDEdGYFW 419

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  948 ITGRIKDLIIVAGRNIYSADVEKtvesssellrpgccAVISVPEDVLSAKgISLPDA-SDEV--GLVVIAelKDGKPVDK 1024
Cdd:cd05928    420 FMGRADDVINSSGYRIGPFEVES--------------ALIEHPAVVESAV-VSSPDPiRGEVvkAFVVLA--PQFLSHDP 482

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1025 D-IIKQIESRVAEehgvTVASVKLirPRTIS------KTTSGKIKRFECLKQ 1069
Cdd:cd05928    483 EqLTKELQQHVKS----VTAPYKY--PRKVEfvqelpKTVTGKIQRNELRDK 528
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 32-264 4.30e-11

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 67.52  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   32 SGLSAAYALAKLGyRDITVIEKHNTVGGMCESVEIEGKVYDLGGQVLaANSAPVIFHLAKESG--TQLEEMDLHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGleDRLVLPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  110 SLTGEYHDINVAEDYMSLVSL-----TLDIQDKAK---DTNRIGIHAVSEIASDLTPAYLEAHGIKSVPKSVQYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRlglAALASDALDEFDLDDFSLAESLLFLGRRGPGDVEVWDRLIDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRMKGGYMNLWKKISESLL---IKVccNTEVQAVRRNGSG 242
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRL--NTRVRSIDREGDG 236

                          250       260
                   ....*....|....*....|..
gi 1973708721  243 VNVDITNSsgetEHKEFDKIII 264
Cdd:pfam01593  237 VTVTLTDG----EVIEADAVIV 254
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
616-751 1.06e-10

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 67.04  E-value: 1.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  616 GYHSAVRAGSVKNLISfTRKSAESTAQWPnLP-------WLHTDS-----------WIKSSKVLPAsniGSQSESQPDDL 677
Cdd:PRK08043   293 GLTSAITAAEIKTIFT-SRQFLDKGKLWH-LPeqltqvrWVYLEDlkddvttadklWIFAHLLMPR---LAQVKQQPEDA 367

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILF-SPL 751
Cdd:PRK08043   368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPL 442
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 520-1014 1.19e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 66.64  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  520 GAVVcqrTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGclrakvvpvpvlppdpLQRGGQALTKI 599
Cdd:PRK13391    22 GEVV---TYRELDERSNRLAHLF---RSLGLKRGDHVAIFMENNLRYLEVCWA----------------AERSGLYYTCV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  600 ENIAKLCNAVAILSTVGyhsavragsVKNLISFTRKS---AESTAQWPNL-PWLHTD---------SWIKSSKVLPASNI 666
Cdd:PRK13391    80 NSHLTPAEAAYIVDDSG---------ARALITSAAKLdvaRALLKQCPGVrHRLVLDgdgelegfvGYAEAVAGLPATPI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  667 GSQSESQPddlcfLQFTSGSTGDAKGVM--ITHGGLIHNVKL---MRRRYRSTSNTVLVSWLPQYHDmgliGGLFTAMVC 741
Cdd:PRK13391   151 ADESLGTD-----MLYSSGTTGRPKGIKrpLPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHS----APQRAVMLV 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  742 ---GGTAIL---FSPLTFirnpllwLQTISDYKATHSagpNFAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKT 815
Cdd:PRK13391   222 irlGGTVIVmehFDAEQY-------LALIEEYGVTHT---QLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQV 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  816 LKRFVELTRPyglsqeVMAPGYGLAENCVFVGCAYGK--KKPILVdwqGRICCGyvdpndadvDIRIVDaDTGLEVDEdG 893
Cdd:PRK13391   292 KEQMIDWWGP------IIHEYYAATEGLGFTACDSEEwlAHPGTV---GRAMFG---------DLHILD-DDGAELPP-G 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  894 KEGEIWIsspsagigywgKEELSQKTF----RNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADV 968
Cdd:PRK13391   352 EPGTIWF-----------EGGRPFEYLndpaKTAEARHPDGTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEA 420

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  969 EKTVESSSELLRpgcCAVISVPEDVL--SAKGISLP----DASDEVGLVVIA 1014
Cdd:PRK13391   421 ENLLITHPKVAD---AAVFGVPNEDLgeEVKAVVQPvdgvDPGPALAAELIA 469
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 644-1025 1.23e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 66.63  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  644 PNLPWLHTDSWIKSSKVLP-ASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGL-IHNVKLMRRRYRSTSNTVLVS 721
Cdd:PRK07867   120 PGVRVINVDSPAWADELAAhRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRFGLGPDDVCYVS 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  722 wLPQYHDMGLIGGLFTAMVCGGTAIL---FSPLTFirnpllwLQTISDYKATHS--AGPNFAFELvirrleADKAKAHDY 796
Cdd:PRK07867   200 -MPLFHSNAVMAGWAVALAAGASIALrrkFSASGF-------LPDVRRYGATYAnyVGKPLSYVL------ATPERPDDA 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  797 DLSSMIFFMIAAEPVrqkTLKRFVeltRPYGLsqeVMAPGYGLAENCVFVGCAYGKKKPILvdwqGRiccgyvdpndADV 876
Cdd:PRK07867   266 DNPLRIVYGNEGAPG---DIARFA---RRFGC---VVVDGFGSTEGGVAITRTPDTPPGAL----GP----------LPP 322

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 DIRIVDADTGLEV-----DEDGKE------GEIW-ISSPSAGIGYWGKEELSQKTFRNklqkfpGRKYtrTGDLG-RVIQ 943
Cdd:PRK07867   323 GVAIVDPDTGTECppaedADGRLLnadeaiGELVnTAGPGGFEGYYNDPEADAERMRG------GVYW--SGDLAyRDAD 394

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  944 GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PGC--CAVISVPEdvlsakgislPDASDEVGLVVIaeLKDGK 1020
Cdd:PRK07867   395 GYAYFAGRLGDWMRVDGENLGTAPIERI------LLRyPDAteVAVYAVPD----------PVVGDQVMAALV--LAPGA 456


                   ....*
gi 1973708721 1021 PVDKD 1025
Cdd:PRK07867   457 KFDPD 461
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 661-1063 2.36e-10

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 65.63  E-value: 2.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  661 LPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIhnVKLMRRRYRSTSN-----TVLVSWLPQYHDMGLIGGL 735
Cdd:cd17642    170 FNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNqiipdTAILTVIPFHHGFGMFTTL 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  736 fTAMVCGGTAILFSplTFIRNplLWLQTISDYKATHS--AGPNFAF----ELVirrleaDKakahdYDLSSMIFFMIAAE 809
Cdd:cd17642    248 -GYLICGFRVVLMY--KFEEE--LFLRSLQDYKVQSAllVPTLFAFfaksTLV------DK-----YDLSNLHEIASGGA 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  810 PVRQKTLKRFVELTRPYGLSQevmapGYGLAENcvfvgcaygkKKPILVDWQGRI---CCGYVDPNdadVDIRIVDADTG 886
Cdd:cd17642    312 PLSKEVGEAVAKRFKLPGIRQ-----GYGLTET----------TSAILITPEGDDkpgAVGKVVPF---FYAKVVDLDTG 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  887 --LEVDEdgkEGEIWISSPSAGIGYWGKEElSQKTFRNKlqkfpgRKYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNI 963
Cdd:cd17642    374 ktLGPNE---RGELCVKGPMIMKGYVNNPE-ATKALIDK------DGWLHSGDIAYYDEdGHFFIVDRLKSLIKYKGYQV 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  964 YSADVEKTVESSSELLRPGccaVISVPEdvlsakgislPDASDEVGLVVIaeLKDGKPV-DKDIIKQIESRVAEEHGVTv 1042
Cdd:cd17642    444 PPAELESILLQHPKIFDAG---VAGIPD----------EDAGELPAAVVV--LEAGKTMtEKEVMDYVASQVSTAKRLR- 507

                          410       420
                   ....*....|....*....|.
gi 1973708721 1043 ASVKLIrpRTISKTTSGKIKR 1063
Cdd:cd17642    508 GGVKFV--DEVPKGLTGKIDR 526
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 672-969 2.56e-10

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 65.35  E-value: 2.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLvswlpQYHDMGLIGG---LFTAMVCGGTAIL 747
Cdd:cd17652     90 TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVL-----QFASPSFDASvweLLMALLAGATLVL 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 FSPLTFIRNPLLwLQTISDYKATHSAGPNFAfelvIRRLEADkakahdyDLSSMIFFMIAAEPVRQktlkrfvELTRPYG 827
Cdd:cd17652    165 APAEELLPGEPL-ADLLREHRITHVTLPPAA----LAALPPD-------DLPDLRTLVVAGEACPA-------ELVDRWA 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  828 LSQeVMAPGYGLAENCV---FVGCAYGKKK-PILVDWQGriccgyvdpndadVDIRIVDAdtGLEVDEDGKEGEIWISSP 903
Cdd:cd17652    226 PGR-RMINAYGPTETTVcatMAGPLPGGGVpPIGRPVPG-------------TRVYVLDA--RLRPVPPGVPGELYIAGA 289

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721  904 SAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:cd17652    290 GLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARwRADGQLEFLGRADDQVKIRGFRIELGEVE 356
srpA_like cd08153
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ...
 1780-2015 4.09e-10

Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.


Pssm-ID: 163709  Cd Length: 295  Bit Score: 63.40  E-value: 4.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1780 GKKYTVIVRHSNS--LSADDDARLDARGAALRIlsdeKGDDSPLLDLTLKTGKAFYARTISDFATWLVCGL--------- 1848
Cdd:cd08153     45 GGSVPVTGRFSLGggNPKAPDDAANPRGMALKF----RLPDGEQWRMVMNSFPVFPVRTPEEFLALLKAIApdatgkpdp 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1849 AAREEHVKRVPHVRDAVwTSLRQA---DSYAEMHYYS-NIcrlFRF--KDGQEMYVKFKLRPSDKNIGEDtgkvepsgil 1922
Cdd:cd08153    121 AKLKAFLAAHPEAAAFL-AWIKTApppASFANTTYYGvNA---FYFtnANGKRQPVRWRFVPEDGVKYLS---------- 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1923 PPETGAIPRDandtrpllFLAEDFQNRVKSPNgVRYIFQLQVmPVPQDEAArdialDCTKPWDESQfPYIDVGEVIINEN 2002
Cdd:cd08153    187 DEEAAKLGPD--------FLFDELAQRLAQGP-VRWDLVLQL-AEPGDPTD-----DPTKPWPADR-KEVDAGTLTITKV 250

                          250
                   ....*....|....*
gi 1973708721 2003 LTKEG--SERLEFNP 2015
Cdd:cd08153    251 APDQGgaCRDINFDP 265
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 674-1065 4.83e-10

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 64.82  E-value: 4.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHN--VKLMRRRYrsTSNTVLVSWLPQYHdmglIGGLFTAMvcggtAILFSpl 751
Cdd:PLN02860   171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslAKIAIVGY--GEDDVYLHTAPLCH----IGGLSSAL-----AMLMV-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 tfirnpllwlqtisdyKATHSAGPNFAFELVIRRLEadkakahDYDLSSMIFF--MIA--AEPVRQK-------TLKRFv 820
Cdd:PLN02860   238 ----------------GACHVLLPKFDAKAALQAIK-------QHNVTSMITVpaMMAdlISLTRKSmtwkvfpSVRKI- 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 eLTRPYGLSQEVMA------------PGYGLAENC----------------VFVGCAYGKKKPILVDWQGRICCGYVDPN 872
Cdd:PLN02860   294 -LNGGGSLSSRLLPdakklfpnaklfSAYGMTEACssltfmtlhdptlespKQTLQTVNQTKSSSVHQPQGVCVGKPAPH 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  873 dadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIGYWG--KEELSQKTFRNKLQkfpgrkytrTGDLGRVIQ-GNLFIT 949
Cdd:PLN02860   373 ---VELKI-------GLDESSRVGRILTRGPHVMLGYWGqnSETASVLSNDGWLD---------TGDIGWIDKaGNLWLI 433

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  950 GRIKDLIIVAGRNIYSADVEktvesssellrpgccAVISVPEDVLSAKGISLPDAsdEVGLVVIA--ELKDGkpvdkdII 1027
Cdd:PLN02860   434 GRSNDRIKTGGENVYPEEVE---------------AVLSQHPGVASVVVVGVPDS--RLTEMVVAcvRLRDG------WI 490

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721 1028 KQIESRVAEEHGVTVASV---------KLIR---PRTISK-------TTSGKIKRFE 1065
Cdd:PLN02860   491 WSDNEKENAKKNLTLSSEtlrhhcrekNLSRfkiPKLFVQwrkpfplTTTGKIRRDE 547
PLN02609 PLN02609
catalase
 1745-2015 4.97e-10

catalase


Pssm-ID: 215328 [Multi-domain]  Cd Length: 492  Bit Score: 64.38  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1745 KVKSRYFHRIGVSGKGYLKLYDDIQGLPEHNIF-GPGKKYTVIVRHSNSL--SADDDARLDARGAALRILSDEkGDdspl 1821
Cdd:PLN02609    58 RIPERVVHARGASAKGFFEVTHDISNLTCADFLrAPGVQTPVIVRFSTVIheRGSPETLRDPRGFAVKFYTRE-GN---- 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1822 LDLTLKTGKAFYARTISDFATwLVCGLaareehvKRVP--HVRD--AVW-------TSLRQ----------ADSYAEMH- 1879
Cdd:PLN02609   133 FDMVGNNFPVFFIRDGMKFPD-MVHAL-------KPNPktHIQEpwRILdflshhpESLHMftflfddrgiPQDYRHMEg 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1880 YYSNICRLFRfKDGQEMYVKFKLRPSD--KNIGEDTGkVEPSGILPPETgaiprdandtrpllflAEDFQNRVKSPNGVR 1957
Cdd:PLN02609   205 FGVHTYKLIN-KAGKAHYVKFHWKPTCgvKNLLDEEA-VRVGGSNHSHA----------------TQDLYDSIAAGNYPE 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721 1958 YIFQLQVMPvPQDEAARDI-ALDCTKPWDESQFPYIDVGEVIINENLTK--EGSERLEFNP 2015
Cdd:PLN02609   267 WKLFIQTMD-PEDEDKFDFdPLDVTKTWPEDILPLQPVGRLVLNRNIDNffAENEQLAFCP 326
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 527-969 5.12e-10

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 64.60  E-value: 5.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  527 TYAELDSNASCIAHkLLTSRkpTIKPGDRVLlVHVP-GLDFVDSFFGCLRAkvvpvpvlppdplqrGGQAL--------T 597
Cdd:cd17646     25 TYRELDERANRLAH-LLRAR--GVGPEDRVA-VLLPrSADLVVALLAVLKA---------------GAAYLpldpgypaD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KIENIAKLCNAVAILSTVGYHSAVRAGSVKNLISFTRKSAESTAqwpnlpwlhtdswiksskvlpasniGSQSESQPDDL 677
Cdd:cd17646     86 RLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPAT-------------------------PPLVPPRPDNL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  678 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMVCGGTAILFSPLTFiRNP 757
Cdd:cd17646    141 AYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPGGH-RDP 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  758 LLWLQTISDYKAThsagpnfAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRpyglsqevmAP-- 835
Cdd:cd17646    219 AYLAALIREHGVT-------TCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG---------AElh 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  836 -GYGLAENCVFV------GCAYGKKKPIlvdwqGRiccgyvdPNdADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIG 908
Cdd:cd17646    283 nLYGPTEAAIDVthwpvrGPAETPSVPI-----GR-------PV-PNTRLYVLDDA--LRPVPVGVPGELYLGGVQLARG 347

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721  909 YWGKEELSQKTFrnklqkFP------GRKYtRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:cd17646    348 YLGRPALTAERF------VPdpfgpgSRMY-RTGDLARWRpDGALEFLGRSDDQVKIRGFRVEPGEIE 408
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1125-1186 7.26e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.80  E-value: 7.26e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1125 EFLKQLVSEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1186
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 680-1065 7.98e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 63.81  E-value: 7.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  680 LQFTSGSTGDAKGVMITHGGLIHNvklmrrryrSTSNTVlvSW-----------LPQYH--------DMGLIGGlftAMV 740
Cdd:PRK08162   187 LNYTSGTTGNPKGVVYHHRGAYLN---------ALSNIL--AWgmpkhpvylwtLPMFHcngwcfpwTVAARAG---TNV 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  741 CggtailfspLTFIRnPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAKahdydLSSMIFFMIAAEP----VRQKTL 816
Cdd:PRK08162   253 C---------LRKVD-PKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG-----IDHPVHAMVAGAAppaaVIAKME 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  817 KRFVELTRPYGLSqEVmapgYGLAENCVfvgcaygkKKPilvDW-----------QGRICCGYVdpndADVDIRIVDADT 885
Cdd:PRK08162   318 EIGFDLTHVYGLT-ET----YGPATVCA--------WQP---EWdalplderaqlKARQGVRYP----LQEGVTVLDPDT 377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  886 GLEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGrVIQ--GNLFITGRIKDLIIVAGRN 962
Cdd:PRK08162   378 MQPVPADGETiGEIMFRGNIVMKGYLKNPKATEEAFAGG--------WFHTGDLA-VLHpdGYIKIKDRSKDIIISGGEN 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  963 IYSADVEKTvessseLLR-PgccavisvpeDVLSAKGISLPDAS-DEVGLVVIaELKDGKPVDK-DIIKQIESRVAeehG 1039
Cdd:PRK08162   449 ISSIEVEDV------LYRhP----------AVLVAAVVAKPDPKwGEVPCAFV-ELKDGASATEeEIIAHCREHLA---G 508

                          410       420
                   ....*....|....*....|....*.
gi 1973708721 1040 VTVAsvKLIRPRTISKTTSGKIKRFE 1065
Cdd:PRK08162   509 FKVP--KAVVFGELPKTSTGKIQKFV 532
PRK12467 PRK12467
peptide synthase; Provisional
 652-1075 8.65e-10

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 64.80  E-value: 8.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  652 DSWIKSSKVLPASNIGsqsesqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGl 731
Cdd:PRK12467   639 DLLCGYSGHNPEVALD------PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG- 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  732 IGGLFTAMVCGGTAILFSPLTfIRNPLLWLQTISDYKATHSAGPNFAFELVIRrleaDKAKAHDYDLSSMIFFMIAAEPV 811
Cdd:PRK12467   712 VTELFGALASGATLHLLPPDC-ARDAEAFAALMADQGVTVLKIVPSHLQALLQ----ASRVALPRPQRALVCGGEALQVD 786

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  812 RQKTLKRFVELTRPYGLsqevmapgYGLAENCVFVgcAYGKKKPILVDWQGRICCGYVdpndADVDIRIVDADtgLEVDE 891
Cdd:PRK12467   787 LLARVRALGPGARLINH--------YGPTETTVGV--STYELSDEERDFGNVPIGQPL----ANLGLYILDHY--LNPVP 850

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  892 DGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDLIIVAGRNIYSADVEK 970
Cdd:PRK12467   851 VGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIELGEIEA 930

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  971 TVEsssellrpgccAVISVPEDVLSAkgisLPDASDE--VGLVVIAELKDG--KPVDKDIIKQIESRVAEEHGVTVASVK 1046
Cdd:PRK12467   931 RLL-----------AQPGVREAVVLA----QPGDAGLqlVAYLVPAAVADGaeHQATRDELKAQLRQVLPDYMVPAHLLL 995

                          410       420
                   ....*....|....*....|....*....
gi 1973708721 1047 LIRprtISKTTSGKIKRfECLKQFVDGTL 1075
Cdd:PRK12467   996 LDS---LPLTPNGKLDR-KALPKPDASAV 1020
PRK07233 PRK07233
hypothetical protein; Provisional
 23-68 8.90e-10

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 63.37  E-value: 8.90e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEG 68
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGG 45
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 679-1063 1.07e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 63.61  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  679 FLQFTSGSTGDAKGVMITHGGlihNVKLMRRRYRSTSNTVLVSWLPQYHDMGLI---GGLFTAMVCGGTAILFSPlTFIR 755
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSLSLGNTFVMFEG-GIIK 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  756 NPL----LWlQTISDYKATHSagpnFAFELVIRRL-----EADKAKAhDYDLSSMIFFMIAAEPVRQ-------KTLKrf 819
Cdd:PTZ00237   334 NKHieddLW-NTIEKHKVTHT----LTLPKTIRYLiktdpEATIIRS-KYDLSNLKEIWCGGEVIEEsipeyieNKLK-- 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  820 VELTRPYGLSQevmapgyglaencvfVGCAYgkkkpilvdwqgRICCGYVD-PNDAdvdirivdadTGLE--------VD 890
Cdd:PTZ00237   406 IKSSRGYGQTE---------------IGITY------------LYCYGHINiPYNA----------TGVPsifikpsiLS 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  891 EDGKE------GEIWIS---SPSAGIGYWGKEELSQKTFrnklQKFPGrkYTRTGDLGRVIQGNLF-ITGRIKDLIIVAG 960
Cdd:PTZ00237   449 EDGKElnvneiGEVAFKlpmPPSFATTFYKNDEKFKQLF----SKFPG--YYNSGDLGFKDENGYYtIVSRSDDQIKISG 522

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  961 RNIYSADVEKTVESSSELLRpgCCAVisvpedvlsakGISLPD-ASDEVGLVVIAELKDGKPVDKDIIK-QIESRVAEEH 1038
Cdd:PTZ00237   523 NKVQLNTIETSILKHPLVLE--CCSI-----------GIYDPDcYNVPIGLLVLKQDQSNQSIDLNKLKnEINNIITQDI 589

                          410       420
                   ....*....|....*....|....*
gi 1973708721 1039 GVTVASVKLIRPRTISKTTSGKIKR 1063
Cdd:PTZ00237   590 ESLAVLRKIIIVNQLPKTKTGKIPR 614
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 23-60 1.07e-09

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 63.23  E-value: 1.07e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGM 60
Cdd:COG0493    123 KVAVVGSGPAGLAAAYQLARAGH-EVTVFEALDKPGGL 159
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 518-992 1.08e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 63.38  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  518 EEGAVVcqrTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALT 597
Cdd:PRK08276     7 PSGEVV---TYGELEARSNRLAHGL---RALGLREGDVVAILLENNPEFFEVYWAARRS----------------GLYYT 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 ---------KIENIAKLCNAVAILSTVGYHSAVR--AGSVKNLISFTRKSAESTAQWpnLPWlhtDSWIKSSkvlPASNI 666
Cdd:PRK08276    65 pinwhltaaEIAYIVDDSGAKVLIVSAALADTAAelAAELPAGVPLLLVVAGPVPGF--RSY---EEALAAQ---PDTPI 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  667 GSQSESQPddlcfLQFTSGSTGDAKGVM-------ITHGGLIHNVKLMRRRYRSTSNTVLVSwLPQYHDMGLIGGLfTAM 739
Cdd:PRK08276   137 ADETAGAD-----MLYSSGTTGRPKGIKrplpgldPDEAPGMMLALLGFGMYGGPDSVYLSP-APLYHTAPLRFGM-SAL 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  740 VCGGTAIL---FSPLTFirnpllwLQTISDYKATHSagpnfafELV----IRRL---EADKAKahdYDLSSMIFFMIAAE 809
Cdd:PRK08276   210 ALGGTVVVmekFDAEEA-------LALIERYRVTHS-------QLVptmfVRMLklpEEVRAR---YDVSSLRVAIHAAA 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  810 PVRQKTLKRFVELTRP----YGLSQEvmapGYGLAencvFVGCAYGKKKPILVD--WQGRIccgyvdpndadvdiRIVDA 883
Cdd:PRK08276   273 PCPVEVKRAMIDWWGPiiheYYASSE----GGGVT----VITSEDWLAHPGSVGkaVLGEV--------------RILDE 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  884 DtGLEVDEdGKEGEIWISSPSAGIGYWGKEElsqKTFRNKLqkfpGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRN 962
Cdd:PRK08276   331 D-GNELPP-GEIGTVYFEMDGYPFEYHNDPE---KTAAARN----PHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVN 401

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1973708721  963 IYSADVEktvessSELLR-PGC--CAVISVPED 992
Cdd:PRK08276   402 IYPQEIE------NLLVThPKVadVAVFGVPDE 428
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 675-1064 1.15e-09

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 63.31  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLvsWlpQYHDMGLIGGLFTAMV----CGGTAIL--- 747
Cdd:cd05973     88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--W--NAADPGWAYGLYYAITgplaLGHPTILleg 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 -FSPltfirnPLLWlQTISDYKATHSAGPNFAFelviRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRF-VELTRP 825
Cdd:cd05973    164 gFSV------ESTW-RVIERLGVTNLAGSPTAY----RLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFdAALGVP 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 yglsqevMAPGYGLAENCVFVGCAYGKKKPILVDWQGRICCGYvdpndadvdiRI-VDADTGLEVDEdGKEGEIWI---S 901
Cdd:cd05973    233 -------IHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGW----------RVaVLDDDGDELGP-GEPGRLAIdiaN 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  902 SPSAGI-GYWGKEelsqktfrnklQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesSSELL 979
Cdd:cd05973    295 SPLMWFrGYQLPD-----------TPAIDGGYYLTGDTVEFdPDGSFSFIGRADDVITMSGYRIGPFDVE-----SALIE 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  980 RPGC--CAVISVPEDVLSakgislpdasdEV--GLVVIAELKDGKPVDKDIIKQIESRVAEEHGvtvasvkliRPRTIS- 1054
Cdd:cd05973    359 HPAVaeAAVIGVPDPERT-----------EVvkAFVVLRGGHEGTPALADELQLHVKKRLSAHA---------YPRTIHf 418

                          410
                   ....*....|....*
gi 1973708721 1055 -----KTTSGKIKRF 1064
Cdd:cd05973    419 vdelpKTPSGKIQRF 433
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 674-1063 1.20e-09

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 62.90  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIhnvklmrrRYRSTSNTVL------VSWLPQyhDMGLIGGLFTAMVC---GGT 744
Cdd:cd05969     88 PEDPTLLHYTSGTTGTPKGVLHVHDAMI--------FYYFTGKYVLdlhpddIYWCTA--DPGWVTGTVYGIWApwlNGV 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  745 AILFSPLTFirNPLLWLQTISDYKAT--HSAGPNfafelvIRRL-EADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVE 821
Cdd:cd05969    158 TNVVYEGRF--DAESWYGIIERVKVTvwYTAPTA------IRMLmKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGME 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  822 LtrpYGLSqevMAPGYGLAENCVFVGCAYgKKKPILVDWQGRICCGyvdpndadVDIRIVDADtGLEVdEDGKEGEIWIS 901
Cdd:cd05969    230 V---FGVP---IHDTWWQTETGSIMIANY-PCMPIKPGSMGKPLPG--------VKAAVVDEN-GNEL-PPGTKGILALK 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  902 S--PSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvesssel 978
Cdd:cd05969    293 PgwPSMFRGIWNDEERYKNSFIDG--------WYLTGDLAYRDEdGYFWFVGRADDIIKTSGHRVGPFEVE--------- 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  979 lrpgcCAVISVPEdVLSAKGISLPDAsdEVGLVVIA--ELKDG-KPVDKdIIKQIESRVAEEHGVTVAsvklirPRTIS- 1054
Cdd:cd05969    356 -----SALMEHPA-VAEAGVIGKPDP--LRGEIIKAfiSLKEGfEPSDE-LKEEIINFVRQKLGAHVA------PREIEf 420

                          410
                   ....*....|....
gi 1973708721 1055 -----KTTSGKIKR 1063
Cdd:cd05969    421 vdnlpKTRSGKIMR 434
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 673-992 1.39e-09

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 62.91  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRR--YRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILfsP 750
Cdd:cd05923    148 EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV--V 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  751 LTFirNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAKahdydLSSMIFFMIAAEPVRQKTLKRF-----VELTRP 825
Cdd:cd05923    226 EEF--DPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLK-----LSSLRHVTFAGATMPDAVLERVnqhlpGEKVNI 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  826 YGlSQEVM--------APGYGLaencvfvgcaygkkKPilvdwqgriccGYVDpndadvDIRIVDADTG-LEVDEDGKEG 896
Cdd:cd05923    299 YG-TTEAMnslymrdaRTGTEM--------------RP-----------GFFS------EVRIVRIGGSpDEALANGEEG 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  897 EIWI--SSPSAGIGYWGKEELSQKTFRNklqkfpgRKYtRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVE 973
Cdd:cd05923    347 ELIVaaAADAAFTGYLNQPEATAKKLQD-------GWY-RTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLS 418

                          330       340
                   ....*....|....*....|.
gi 1973708721  974 ssselLRPGC--CAVISVPED 992
Cdd:cd05923    419 -----RHPGVteVVVIGVADE 434
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 671-955 2.21e-09

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 62.44  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  671 ESQPDDLCFLQFTSGSTGDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVlVSWLPQYHDMGLIGGLFTAMVCGGTailfs 749
Cdd:cd17641    154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLgHCAAYLAADPLGPGDEY-VSVLPLPWIGEQMYSVGQALVCGFI----- 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  750 pLTFIRNPLLWLQTISDykathsAGPNFAFeLVIRRLEADKAkahdyDLSSMiffMIAAEPVRQKTLKRFVELTR---PY 826
Cdd:cd17641    228 -VNFPEEPETMMEDLRE------IGPTFVL-LPPRVWEGIAA-----DVRAR---MMDATPFKRFMFELGMKLGLralDR 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 GLSQEVMAPG----YGLAENCVF-----------------VGCAYGKK-----KPILVDW-----QGRICCGYVDPNDAD 875
Cdd:cd17641    292 GKRGRPVSLWlrlaSWLADALLFrplrdrlgfsrlrsaatGGAALGPDtfrffHAIGVPLkqlygQTELAGAYTVHRDGD 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  876 VDIRIVD---ADTGLEVDEdgkEGEIWISSPSAGIGYWGKEELSQKTfrnklqkFPGRKYTRTGDLGRVIQ-GNLFITGR 951
Cdd:cd17641    372 VDPDTVGvpfPGTEVRIDE---VGEILVRSPGVFVGYYKNPEATAED-------FDEDGWLHTGDAGYFKEnGHLVVIDR 441


                   ....
gi 1973708721  952 IKDL 955
Cdd:cd17641    442 AKDV 445
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1342-1433 2.68e-09

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 57.57  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1342 VHLRGTVFLKHWfemlGARIGSSVLLDT-VDITDPSLVSIGDGAVIAEGALL--QSHEVRN---SVLRFQPIRIGRNCSV 1415
Cdd:COG0110     15 VVIGPGVRIYGG----NITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWI 90

                           90
                   ....*....|....*...
gi 1973708721 1416 GPYAVIQKGSVLGEGAEV 1433
Cdd:COG0110     91 GAGATILPGVTIGDGAVV 108
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 672-997 3.41e-09

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 61.68  E-value: 3.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMVCGGTAILfSPL 751
Cdd:cd17644    103 TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVL-RPE 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAkAHDYDLSSMIFFMIAAEPVR----QKTLKRFVELTRPYG 827
Cdd:cd17644    181 EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTI-DLPSSLRLVIVGGEAVQPELvrqwQKNVGNFIQLINVYG 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  828 LSQEVMApgyglAENCVFVGCAYGKKKPILVdwqGRICcgyvdpndADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGI 907
Cdd:cd17644    260 PTEATIA-----ATVCRLTQLTERNITSVPI---GRPI--------ANTQVYILDEN--LQPVPVGVPGELHIGGVGLAR 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  908 GYWGKEELSQKTF-RNKLQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEkTVESSSELLRPgccA 985
Cdd:cd17644    322 GYLNRPELTAEKFiSHPFNSSESERLYKTGDLARYLpDGNIEYLGRIDNQVKIRGFRIELGEIE-AVLSQHNDVKT---A 397

                          330
                   ....*....|..
gi 1973708721  986 VISVPEDVLSAK 997
Cdd:cd17644    398 VVIVREDQPGNK 409
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 734-1065 4.65e-09

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 61.10  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  734 GLFT--------AMVCGGTAILFSPLtfirNPLLWLQTISDYKATHSAG-PNFAFELvirrleADKAKAHDYD-----LS 799
Cdd:cd05913    132 GLFTgglgfhygAERLGALVIPAGGG----NTERQLQLIKDFGPTVLCCtPSYALYL------AEEAEEEGIDprelsLK 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  800 SMIFfmiAAEPVRQKTLKRF-----VELTRPYGLSqEVMAPGYGLaENCVFVGcaygkkkpiLVDWQGRIccgYVDpnda 874
Cdd:cd05913    202 VGIF---GAEPWTEEMRKRIerrlgIKAYDIYGLT-EIIGPGVAF-ECEEKDG---------LHIWEDHF---IPE---- 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  875 dvdirIVDADTGlEVDEDGKEGEIWISSpsagigyWGKEELsqktfrnklqkfPGRKYtRTGDLGRVIQG-------NLF 947
Cdd:cd05913    261 -----IIDPETG-EPVPPGEVGELVFTT-------LTKEAM------------PLIRY-RTRDITRLLPGpcpcgrtHRR 314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  948 ---ITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGCCA----VISVPE--DVLSAKGISLPDASDEVGLVVIAelkd 1018
Cdd:cd05913    315 idrITGRSDDMLIIRGVNVFPSQIEDVL-----LKIPGLGPhyqlILTRQEhlDELTIKVEVRPEADDDEKLEALK---- 385

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1973708721 1019 gkpvdKDIIKQIESRVaeehGVTVAsVKLIRPRTISKTTsGKIKRFE 1065
Cdd:cd05913    386 -----QRLERHIKSVL----GVTVE-VELVEPGSLPRSE-GKAKRVI 421
catalase cd00328
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ...
 1749-2002 4.92e-09

Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163705 [Multi-domain]  Cd Length: 433  Bit Score: 60.94  E-value: 4.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1749 RYFHRIGVSGKGYLKLYDDIQGLPEHNIFG-PGKKYTVIVRHSnSLSAD----DDARlDARGAALRILSDEKgddspLLD 1823
Cdd:cd00328      5 RVVHARGAGAFGYFTAYGDWSDISAAAFFSaIGKKTPVFVRFS-TVVGGagsaDTVR-DPHGFATKFYTEEG-----NFD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1824 LTLKTGKAFYARTISDFATWLvcglaareeH-VKRVPHVR----DAVW-------TSLRQA----------DSYAEMHYY 1881
Cdd:cd00328     78 LVGNNTPIFFIRDAIKFPDFI---------HaQKPNPQTAlpdaDRFWdflslrpESLHQVsflfsdrgipAAYRHMNGY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1882 SNicRLFRF--KDGQEMYVKFKLRPsdknigeDTGKvepSGILPPETGAIPRDANDtrpllFLAEDFQNRVKSPNGVRYI 1959
Cdd:cd00328    149 GS--HTFKLvnANGKVHYVKFHWKT-------DQGI---ANLVWEEAARLAGEDPD-----YHRQDLFEAIEAGDYPSWE 211

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1973708721 1960 FQLQVMPVPQDEAARDIALDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:cd00328    212 LYIQVMTFNDAEKFPFNPLDPTKVWPEELVPLIVVGKLVLNRN 254
PRK07208 PRK07208
hypothetical protein; Provisional
 26-75 6.36e-09

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 61.06  E-value: 6.36e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEIEGKVYDLGG 75
Cdd:PRK07208     9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 521-974 1.22e-08

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 59.91  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrGGQAL- 596
Cdd:cd12117     15 AVVYgdrSLTYAELNERANRLARRL---RAAGVGPGDVVGVLAERSPELVVALLAVLKA---------------GAAYVp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  597 ----TKIENIAKLCnavailstvgyhsavRAGSVKNLISftrksAESTAQWPNLPWLHTDSWIKSSKVlPASNIGSQSEs 672
Cdd:cd12117     77 ldpeLPAERLAFML---------------ADAGAKVLLT-----DRSLAGRAGGLEVAVVIDEALDAG-PAGNPAVPVS- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 qPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKlmRRRYRS-TSNTVLVSWLPQYHDMGLIgGLFTAMVCGGTAILFSPL 751
Cdd:cd12117    135 -PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTlGPDDRVLQTSPLAFDASTF-EIWGALLNGARLVLAPKG 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TfirnpLLWLQTISDYKATHsaGPNFAFelvirrleadkakahdydLSSMIFFMIAAE-PVRQKTLKRFVeltrpygLSQ 830
Cdd:cd12117    211 T-----LLDPDALGALIAEE--GVTVLW------------------LTAALFNQLADEdPECFAGLRELL-------TGG 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  831 EVMAP-----------------GYGLAENCVFVgCAYGKKKPilvdwqgriccgyvDPNDADVDI-RIVDADTGLEVDED 892
Cdd:cd12117    259 EVVSPphvrrvlaacpglrlvnGYGPTENTTFT-TSHVVTEL--------------DEVAGSIPIgRPIANTRVYVLDED 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  893 GK------EGEIWISSPSAGIGYWGKEELSQKTFrNKLQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYS 965
Cdd:cd12117    324 GRpvppgvPGELYVGGDGLALGYLNRPALTAERF-VADPFGPGERLYRTGDLARWLpDGRLEFLGRIDDQVKIRGFRIEL 402


                   ....*....
gi 1973708721  966 ADVEKTVES 974
Cdd:cd12117    403 GEIEAALRA 411
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 21-74 1.25e-08

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 59.86  E-value: 1.25e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEGKVYDLG 74
Cdd:COG1233      3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTFERPGFRFDVG 55
PRK12316 PRK12316
peptide synthase; Provisional
 651-940 1.51e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 60.74  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  651 TDSWIKSSKVLPASNIgsqsesQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmG 730
Cdd:PRK12316  4676 DEDWEGFPAHDPAVRL------HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-G 4748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 LIGGLFTAMVCGGTAIlfspltfIRNPLLWL-----QTISDYKATHSAGPNFAFELVIRRLEADKakahdyDLSSMIFFM 805
Cdd:PRK12316  4749 SHEGLYHPLINGASVV-------IRDDSLWDperlyAEIHEHRVTVLVFPPVYLQQLAEHAERDG------EPPSLRVYC 4815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  806 IAAEPVRQKTLKRFVELTRPYGLSQevmapGYGLAENCVFVGCaygkkkpilvdwqgRICCGYVDPNDADVDIRIVDADT 885
Cdd:PRK12316  4816 FGGEAVAQASYDLAWRALKPVYLFN-----GYGPTETTVTVLL--------------WKARDGDACGAAYMPIGTPLGNR 4876

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  886 GLEVDED-------GKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGR 940
Cdd:PRK12316  4877 SGYVLDGqlnplpvGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLAR 4938
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1607-1704 1.71e-08

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 55.50  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1607 GAKVGKYCSIRS-INPVadprmvSIGAGVHLGDFSRIMTGfYSQSGYIQSNV-----------HVKDNSVIGSQSLILPG 1674
Cdd:cd04645     23 GSSVWFGAVLRGdVNPI------RIGERTNIQDGSVLHVD-PGYPTIIGDNVtvghgavlhgcTIGDNCLIGMGAIILDG 95

                           90       100       110
                   ....*....|....*....|....*....|
gi 1973708721 1675 SVVEKDVILGAISVAPVNSVLQSGGVYMGS 1704
Cdd:cd04645     96 AVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1602-1688 1.79e-08

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 55.26  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1602 YLHLLGAKVGKYCSIRSINPVADPRMVSIGAGVHLGDFSRIMTGFY-----SQSGYIQSNVHVKDNSVIGSQSLILPGSV 1676
Cdd:COG0110     22 RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVT 101

                           90
                   ....*....|..
gi 1973708721 1677 VEKDVILGAISV 1688
Cdd:COG0110    102 IGDGAVVGAGSV 113
PRK12316 PRK12316
peptide synthase; Provisional
 521-969 1.83e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 60.36  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC--QR-TYAELDSNASCIAHKLltsRKPTIKPGDRVLLVHVPGLDFVDSFFGCLRAkvvpvpvlppdplqrgGQALT 597
Cdd:PRK12316  2021 AVVFgdQHlSYAELDSRANRLAHRL---RARGVGPEVRVAIAAERSFELVVALLAVLKA----------------GGAYV 2081

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KI------ENIAKL---CNAVAILSTVgyHSAVR---AGSVKNLisftrkSAESTAQWPNLPWLHtdswiksskvlpasn 665
Cdd:PRK12316  2082 PLdpnypaERLAYMledSGAALLLTQR--HLLERlplPAGVARL------PLDRDAEWADYPDTA--------------- 2138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  666 igSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYR-STSNTVLvSWLPQYHDmGLIGGLFTAMvCGGT 744
Cdd:PRK12316  2139 --PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYElSPADCEL-QFMSFSFD-GAHEQWFHPL-LNGA 2213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  745 AILfspltfIRNPLLWL--QTisdYKATHSAGPNFA-FELVIRRLEADKAkAHDYDLSSMIFFMIAAEPVRQKTLKRFVE 821
Cdd:PRK12316  2214 RVL------IRDDELWDpeQL---YDEMERHGVTILdFPPVYLQQLAEHA-ERDGRPPAVRVYCFGGEAVPAASLRLAWE 2283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  822 LTRPYGLSQevmapGYGLAENCVfvgcaygkkKPILvdWQgricCGYVDPNDA----------DVDIRIVDADtgLEVDE 891
Cdd:PRK12316  2284 ALRPVYLFN-----GYGPTEAVV---------TPLL--WK----CRPQDPCGAayvpigralgNRRAYILDAD--LNLLA 2341

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  892 DGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK12316  2342 PGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYrADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 674-993 2.21e-08

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 59.31  E-value: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLihnvkLMRRRYRS-----TSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL- 747
Cdd:PRK08008   172 TDDTAEILFTSGTTSRPKGVVITHYNL-----RFAGYYSAwqcalRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLl 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  748 --FSPLTFirnpllWLQtISDYKATHSAgpnfAFELVIRRLEADKAKAHDYD--LSSMIFFMIAAEPVRQKTLKRF-VEL 822
Cdd:PRK08008   247 ekYSARAF------WGQ-VCKYRATITE----CIPMMIRTLMVQPPSANDRQhcLREVMFYLNLSDQEKDAFEERFgVRL 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSQEVMapgyGLaencvfVGCAYGKKKpilvDWQ--GRICCGYvdpndadvDIRIVDADtGLEVDEdGKEGEIWI 900
Cdd:PRK08008   316 LTSYGMTETIV----GI------IGDRPGDKR----RWPsiGRPGFCY--------EAEIRDDH-NRPLPA-GEIGEICI 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  901 SS-PSAGI--GYWGKEELSQKTFRnklqkfpGRKYTRTGDLGRVIQGNLF-ITGRIKDLIIVAGRNIYSADVEKTVESSS 976
Cdd:PRK08008   372 KGvPGKTIfkEYYLDPKATAKVLE-------ADGWLHTGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENIIATHP 444

                          330
                   ....*....|....*..
gi 1973708721  977 ELLRpgcCAVISVPEDV 993
Cdd:PRK08008   445 KIQD---IVVVGIKDSI 458
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 521-969 2.30e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 59.13  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  521 AVVC---QRTYAELDSNASCIAHKLLTSrkpTIKPGDRVLLVHVPGLDFVDSFFGCLRAKvvpvpvlppdplqrggqaLT 597
Cdd:PRK07798    21 ALVCgdrRLTYAELEERANRLAHYLIAQ---GLGPGDHVGIYARNRIEYVEAMLGAFKAR------------------AV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  598 KI--------ENIAKL---CNAVAILstvgYHSavragsvknliSFTRKSAESTaqwPNLPWLHT--------DSWIKSS 658
Cdd:PRK07798    80 PVnvnyryveDELRYLlddSDAVALV----YER-----------EFAPRVAEVL---PRLPKLRTlvvvedgsGNDLLPG 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  659 KVLPASNIGSQS------ESQPDDLCFLqFTSGSTGDAKGVMITH--------GGL-------IHNVKLMRRRYRSTSNT 717
Cdd:PRK07798   142 AVDYEDALAAGSperdfgERSPDDLYLL-YTGGTTGMPKGVMWRQedifrvllGGRdfatgepIEDEEELAKRAAAGPGM 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  718 VLVSWLPQYHDMGLIGGlFTAMVCGGTAILFSPLTFirNPLLWLQTISDYKATHSA--GPNFAfelviRRLEADKAKAHD 795
Cdd:PRK07798   221 RRFPAPPLMHGAGQWAA-FAALFSGQTVVLLPDVRF--DADEVWRTIEREKVNVITivGDAMA-----RPLLDALEARGP 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  796 YDLSSMifFMIA--AEPVRQKTLKRFVELtrpygLSQEVMAPGYGLAENCvFVGCAYGKKKPILVDwQGRIccgyvdpnD 873
Cdd:PRK07798   293 YDLSSL--FAIAsgGALFSPSVKEALLEL-----LPNVVLTDSIGSSETG-FGGSGTVAKGAVHTG-GPRF--------T 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  874 ADVDIRIVDADTGLEVDEDGKEGeiWIS-SPSAGIGYWGKEELSQKTFRnklqKFPGRKYTRTGDLGRVIQ-GNLFITGR 951
Cdd:PRK07798   356 IGPRTVVLDEDGNPVEPGSGEIG--WIArRGHIPLGYYKDPEKTAETFP----TIDGVRYAIPGDRARVEAdGTITLLGR 429

                          490
                   ....*....|....*...
gi 1973708721  952 IKDLIIVAGRNIYSADVE 969
Cdd:PRK07798   430 GSVCINTGGEKVFPEEVE 447
Catalase smart01060
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ...
 1760-2002 2.30e-08

Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.


Pssm-ID: 215003  Cd Length: 373  Bit Score: 58.63  E-value: 2.30e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1760 GYLKLYDDIQGLPEHNIF-GPGKKYTVIVRHS----NSLSADDdARlDARGAALRILSDEK-----GDDSPLldltlktg 1829
Cdd:smart01060   53 GYFEVTEDISDYTKAAFFqKVGKKTPVFVRFStvagERGSADT-VR-DPRGFAVKFYTEEGnwdlvGNNTPV-------- 122

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1830 kaFYAR-TI--SDFAtwlvcglaareeH-VKRVP--HVRDA--VW-------TSLRQ----------ADSYAEMHYYSni 1884
Cdd:smart01060  123 --FFIRdPIkfPDFI------------HaQKRDPrtNLPDHdmFWdfwslnpESLHQvtwlmsdrgiPASYRHMNGFG-- 186

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  1885 CRLFRF--KDGQEMYVKFKLRP-----------SDKNIGEDtgkvepsgilppetgaipRDandtrpllFLAEDFQNRVK 1951
Cdd:smart01060  187 VHTFKLvnAEGERFYVKFHFKPdqgiknltweeAAKLAGKD------------------PD--------YHRRDLYEAIE 240

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721  1952 SPNGVRYIFQLQVMPvPQDEAARDI-ALDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:smart01060  241 RGDYPEWTLYVQVMP-EEDAEKFRFdPFDLTKVWPHKDYPLIEVGKMTLNRN 291
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 680-990 8.04e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 57.72  E-value: 8.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  680 LQFTSGSTGDAKGVMITHGGlihnvklmrrRYRSTSNTVlVSW-----------LPQYHDMGLIGGLFTAMVcGGTAILF 748
Cdd:PLN03102   191 LNYTSGTTADPKGVVISHRG----------AYLSTLSAI-IGWemgtcpvylwtLPMFHCNGWTFTWGTAAR-GGTSVCM 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTfirNPLLWlQTISDYKATHSAGPNFAFELVIRRLEADKAKAhdydlSSMIFFMIAAEPVRQKTLKRFVELtrpyGL 828
Cdd:PLN03102   259 RHVT---APEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPR-----SGPVHVLTGGSPPPAALVKKVQRL----GF 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 sqEVMApGYGLAEncvfvgcAYGkkkPIL-VDWQG-------------RICCGYVDPNDADVDIRivDADTGLEVDEDGK 894
Cdd:PLN03102   326 --QVMH-AYGLTE-------ATG---PVLfCEWQDewnrlpenqqmelKARQGVSILGLADVDVK--NKETQESVPRDGK 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  895 E-GEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGrVIQ--GNLFITGRIKDLIIVAGRNIYSADVEKT 971
Cdd:PLN03102   391 TmGEIVIKGSSIMKGYLKNPKATSEAFKHG--------WLNTGDVG-VIHpdGHVEIKDRSKDIIISGGENISSVEVENV 461

                          330
                   ....*....|....*....
gi 1973708721  972 VESSSELLRpgcCAVISVP 990
Cdd:PLN03102   462 LYKYPKVLE---TAVVAMP 477
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
673-841 9.62e-08

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 57.67  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILF-SPL 751
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYpSPL 870

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFIRNPLLwlqtISDYKATHSAGPNFaFelvirrLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVEltrPYGLSqe 831
Cdd:PRK06814   871 HYRIIPEL----IYDTNATILFGTDT-F------LNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWME---KFGIR-- 934

                          170
                   ....*....|
gi 1973708721  832 vMAPGYGLAE 841
Cdd:PRK06814   935 -ILEGYGVTE 943
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 13-60 1.06e-07

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 57.19  E-value: 1.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1973708721   13 KLHPCLPlDT--RIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGM 60
Cdd:PRK12771   128 KFPAPAP-DTgkRVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGM 175
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 673-920 1.35e-07

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 56.67  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMR--RRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAILF-- 748
Cdd:cd05921    163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqtYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDdg 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 --SPLTF---IRNpllwLQTIS-DYKATHSAGpnfaFELVIRRLEADKAKAHDYdLSSMIFFMIAAEPVRQKTLKRFVEL 822
Cdd:cd05921    243 kpMPGGFeetLRN----LREISpTVYFNVPAG----WEMLVAALEKDEALRRRF-FKRLKLMFYAGAGLSQDVWDRLQAL 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  823 TRPYGLSQEVMAPGYGLAENC-VFVGCAYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDEDGkegeiwis 901
Cdd:cd05921    314 AVATVGERIPMMAGLGATETApTATFTHWPTERS-----------GLIGLPAPGTELKLVPSGGKYEVRVKG-------- 374

                          250
                   ....*....|....*....
gi 1973708721  902 sPSAGIGYWGKEELSQKTF 920
Cdd:cd05921    375 -PNVTPGYWRQPELTAQAF 392
PRK12316 PRK12316
peptide synthase; Provisional
 669-1006 1.40e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 57.27  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  669 QSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMVCGGTAILf 748
Cdd:PRK12316  3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVL- 3267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 spltfiRNPLLWLQTISDYKATHSAGPNF--AFELVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELTRPY 826
Cdd:PRK12316  3268 ------AGPEDWRDPALLVELINSEGVDVlhAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLY 3341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 GLSQEVMAPgygLAENCVFVGCAYgkkKPIlvdwqgriccGYVDPNDAdvdirIVDADTGLEVDEDGKEGEIWISSPSAG 906
Cdd:PRK12316  3342 GPTEATITV---THWQCVEEGKDA---VPI----------GRPIANRA-----CYILDGSLEPVPVGALGELYLGGEGLA 3400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  907 IGYWGKEELSQKTFRNKLQKFPGRKYtRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPgccA 985
Cdd:PRK12316  3401 RGYHNRPGLTAERFVPDPFVPGERLY-RTGDLARYrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREA---V 3476

                          330       340
                   ....*....|....*....|.
gi 1973708721  986 VISVPEDVLSAKGISLPDASD 1006
Cdd:PRK12316  3477 VLAVDGRQLVAYVVPEDEAGD 3497
PRK12467 PRK12467
peptide synthase; Provisional
 652-940 1.41e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 57.48  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  652 DSWIKS-SKVLPASNIGsqsesqPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMG 730
Cdd:PRK12467  1700 DDWLEGySDSNPAVNLA------PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS 1773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  731 lIGGLFTAMVCGGTAILFSPLTFiRNPLLWLQTISDYKATHSAGPNFAFELVirrLEADKAKAHDYDLSSMIFFMIAAEP 810
Cdd:PRK12467  1774 -VWELFWPLINGARLVIAPPGAH-RDPEQLIQLIERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVCGGEALEV 1848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  811 -VRQKTLKRF--VELTRPYGLSQEVMAPGYGLAEncvfvgcaygkkkpiLVDWQGRICCGYVDPNdADVDIRIVDAdtGL 887
Cdd:PRK12467  1849 eALRPWLERLpdTGLFNLYGPTETAVDVTHWTCR---------------RKDLEGRDSVPIGQPI-ANLSTYILDA--SL 1910

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  888 EVDEDGKEGEIWISSPSAGIGYWGKEELSQKTF-RNKLQKFPGRKYtRTGDLGR 940
Cdd:PRK12467  1911 NPVPIGVAGELYLGGVGLARGYLNRPALTAERFvADPFGTVGSRLY-RTGDLAR 1963
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 23-59 1.72e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 56.34  E-value: 1.72e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGG 59
Cdd:PRK11749   142 KVAVIGAGPAGLTAAHRLARKGY-DVTIFEARDKAGG 177
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1119-1195 1.76e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 50.62  E-value: 1.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1119 SNRNIVEFLKQLVSEQTGISIQNISATESLVS-YGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLL 1195
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PRK13382 PRK13382
bile acid CoA ligase;
643-992 1.84e-07

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 56.31  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  643 WPNLPWLHTdswiksSKVLPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK--LMRRRYRSTSNTVLV 720
Cdd:PRK13382   170 WTDEDHDLT------VEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKaiLDRTPWRAEEPTVIV 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  721 SwlPQYHDMGLIGGLFTAMvcggtaiLFSPLTFIR--NPLLWLQTISDYKATHSAGPNFAFElviRRLEADKAKAHDYDL 798
Cdd:PRK13382   244 A--PMFHAWGFSQLVLAAS-------LACTIVTRRrfDPEATLDLIDRHRATGLAVVPVMFD---RIMDLPAEVRNRYSG 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  799 SSMIFFMIAAEPVRQKTLKRFVEltrPYGlsqEVMAPGYGLAEncvfVGCAYG------KKKPilvDWQGRiccgyvdPN 872
Cdd:PRK13382   312 RSLRFAAASGSRMRPDVVIAFMD---QFG---DVIYNNYNATE----AGMIATatpadlRAAP---DTAGR-------PA 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  873 DAdVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKeelSQKTFRNKlqkfpgrkYTRTGDLGRVIQ-GNLFITGR 951
Cdd:PRK13382   372 EG-TEIRILDQD-FREV-PTGEVGTIFVRNDTQFDGYTSG---STKDFHDG--------FMASGDVGYLDEnGRLFVVGR 437

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1973708721  952 IKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPED 992
Cdd:PRK13382   438 DDEMIVSGGENVYPIEVEKTLATHPDVAE---AAVIGVDDE 475
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 644-970 2.17e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 56.19  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  644 PNLPWLHTDSWIKSSKVLPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWL 723
Cdd:PRK13388   119 PGVRVLDVDTPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSM 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  724 PQYHDMGLIGGLFTAMVCGGTAIL---FSPLTFirnpllwLQTISDYKATHsagpnfaFELVIRRLE---ADKAKAHDYD 797
Cdd:PRK13388   199 PLFHSNAVMAGWAPAVASGAAVALpakFSASGF-------LDDVRRYGATY-------FNYVGKPLAyilATPERPDDAD 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  798 LSSMIFFMIAAEPvRQKTlkrfvELTRPYGLSqevMAPGYGLAENCVFV----GCAYGKkkpilvdwQGRiccgyvdpnd 873
Cdd:PRK13388   265 NPLRVAFGNEASP-RDIA-----EFSRRFGCQ---VEDGYGSSEGAVIVvrepGTPPGS--------IGR---------- 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  874 ADVDIRIVDADTGLE-----VDEDGKE-------GEIWISSPSAGI-GYWGKEELSQKTFRNklqkfpGRkYtRTGDLG- 939
Cdd:PRK13388   318 GAPGVAIYNPETLTEcavarFDAHGALlnadeaiGELVNTAGAGFFeGYYNNPEATAERMRH------GM-Y-WSGDLAy 389

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1973708721  940 RVIQGNLFITGRIKDLIIVAGRNIYSADVEK 970
Cdd:PRK13388   390 RDADGWIYFAGRTADWMRVDGENLSAAPIER 420
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 673-1063 2.62e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 55.79  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLihnVKLMRRRYRSTSNTVLVSWL---PQYHDMGlIGGLFTAMVCGGTAILF- 748
Cdd:cd12115    103 DPDDLAYVIYTSGSTGRPKGVAIEHRNA---AAFLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVVLAd 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTFIRNPLL----WLQTIsdykathsagPNFAFELVirRLEADKAKAHDYDLssmiffmiAAEPVRQKTLKRFVELtr 824
Cdd:cd12115    179 NVLALPDLPAAaevtLINTV----------PSAAAELL--RHDALPASVRVVNL--------AGEPLPRDLVQRLYAR-- 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  825 pygLSQEVMAPGYGLAENcvfvgCAYGKKKPILVDWQGRICCGYVDPND-ADVdirivdADTGLEVDEDGKEGEIWISSP 903
Cdd:cd12115    237 ---LQVERVVNLYGPSED-----TTYSTVAPVPPGASGEVSIGRPLANTqAYV------LDRALQPVPLGVPGELYIGGA 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  904 SAGIGYWGKEELSQKTFRNKlQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellRPG 982
Cdd:cd12115    303 GVARGYLGRPGLTAERFLPD-PFGPGARLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRS-----IPG 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  983 ccavisVPEDVLSAKGislpDASDEVGLVVIAELKDGKPVDKDIIKQIESRVAEEHGVTVASVKLirpRTISKTTSGKIK 1062
Cdd:cd12115    377 ------VREAVVVAIG----DAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRL---DALPLTPNGKID 443


                   .
gi 1973708721 1063 R 1063
Cdd:cd12115    444 R 444
catalase_fungal cd08157
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ...
 1745-2015 5.04e-07

Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.


Pssm-ID: 163713 [Multi-domain]  Cd Length: 451  Bit Score: 54.66  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1745 KVKSRYFHRIGVSGKGYLKLYDDIQGLPEHNIF-GPGKKYTVIVRHSN----SLSADDdARlDARGAALRILSDEkGDds 1819
Cdd:cd08157     17 RIPERVVHAKGAGAYGEFEVTDDISDITSADMLqGVGKKTPCLVRFSTvggeKGSADT-VR-DPRGFAVKFYTEE-GN-- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1820 plLDLTLKTGKAFYARTISDFATWLvcglaareeHV-KRVP--HVRDA--VWTSLRQ-----------------ADSYAE 1877
Cdd:cd08157     92 --WDWVFNNTPVFFIRDPIKFPHFI---------HSqKRDPqtNLKDStmFWDYLSQnpesihqvmilfsdrgtPASYRS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1878 MHYYSNicRLFRF--KDGQEMYVKFKLRPsdknigeDTGkvePSGILPPETGAIPRDANDtrpllFLAEDFQNRVKSPNG 1955
Cdd:cd08157    161 MNGYSG--HTYKWvnPDGSFKYVQFHLKS-------DQG---PKFLTGEEAARLAGSNPD-----YATKDLFEAIERGDY 223

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1956 VRYIFQLQVMPVPQDEAARDIALDCTKPWDESQFPYIDVGEVIINENLTK--EGSERLEFNP 2015
Cdd:cd08157    224 PSWTVYVQVMTPEQAEKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNyfAEIEQAAFSP 285
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 23-111 5.10e-07

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 54.85  E-value: 5.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYR-DITVIEKHNTVGGMCESVEIEGKVYDLGgqvlaansaPVIFHLAKESGTQLeemd 101
Cdd:PRK11883     2 KVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFPIELG---------PESFLARKPSAPAL---- 68

                           90
                   ....*....|
gi 1973708721  102 LHKLALIDSL 111
Cdd:PRK11883    69 VKELGLEDEL 78
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 649-994 5.62e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 54.61  E-value: 5.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  649 LHTDSWiksskvlpasniGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHD 728
Cdd:PRK07787   114 LHARSW------------HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHV 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  729 MGLIGGLFTAMVCGGTAI---LFSPltfirnpllwlqtiSDYKATHSAGPN--FAFELVIRRLEADKAKAHDYDLSSMIF 803
Cdd:PRK07787   182 HGLVLGVLGPLRIGNRFVhtgRPTP--------------EAYAQALSEGGTlyFGVPTVWSRIAADPEAARALRGARLLV 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  804 FMIAAEPVrqKTLKRFVELTrpyglSQEVMAPgYGLAENCVFVGC-AYGKKKPilvdwqgriccGYVDPNDADVDIRIVD 882
Cdd:PRK07787   248 SGSAALPV--PVFDRLAALT-----GHRPVER-YGMTETLITLSTrADGERRP-----------GWVGLPLAGVETRLVD 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  883 aDTGLEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRnklqkfpGRKYTRTGDLGrVIQ--GNLFITGRIK-DLIIV 958
Cdd:PRK07787   309 -EDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFT-------ADGWFRTGDVA-VVDpdGMHRIVGREStDLIKS 379

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1973708721  959 AGRNIYSADVEKTVessseLLRPGC--CAVISVPEDVL 994
Cdd:PRK07787   380 GGYRIGAGEIETAL-----LGHPGVreAAVVGVPDDDL 412
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 21-54 6.49e-07

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 53.79  E-value: 6.49e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVIEKH 54
Cdd:COG0654      3 RTDVLIVGGGPAGLALALALARAGIR-VTVVERA 35
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 622-956 6.52e-07

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 54.74  E-value: 6.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  622 RAGSVKNLISFTRKSAESTaqwpnLPWLHTDSWIKSSkVLPASNIGSQSESQPD-----DLCFLQFTSGSTGDAKGVMIT 696
Cdd:PLN02387   198 QLETVKRVIYMDDEGVDSD-----SSLSGSSNWTVSS-FSEVEKLGKENPVDPDlpspnDIAVIMYTSGSTGLPKGVMMT 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  697 HGGLIHNVK-LMRRRYRSTSNTVLVSWLPQYHDMGLIGGlfTAMVCGGTAILF-SPLTFIR----------------NPL 758
Cdd:PLN02387   272 HGNIVATVAgVMTVVPKLGKNDVYLAYLPLAHILELAAE--SVMAAVGAAIGYgSPLTLTDtsnkikkgtkgdasalKPT 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  759 LW------LQTISD--YKATHSAGP------NFAFElviRRLEA-DKAKAHDYDLSSMIFFMIAAEPVRqKTLK---RFV 820
Cdd:PLN02387   350 LMtavpaiLDRVRDgvRKKVDAKGGlakklfDIAYK---RRLAAiEGSWFGAWGLEKLLWDALVFKKIR-AVLGgriRFM 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  821 eLTRPYGLS---QEVM-----AP---GYGLAENCvfVGCAYGKKKPILVdwqGRIC----CGYvdpndadvdIRIVDADT 885
Cdd:PLN02387   426 -LSGGAPLSgdtQRFIniclgAPigqGYGLTETC--AGATFSEWDDTSV---GRVGpplpCCY---------VKLVSWEE 490

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  886 G--LEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQkfpGRKYTRTGDLGRV-IQGNLFITGRIKDLI 956
Cdd:PLN02387   491 GgyLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDER---GMRWFYTGDIGQFhPDGCLEIIDRKKDIV 561
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
874-1081 9.80e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 54.02  E-value: 9.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  874 ADVDIRIVDADTGLEvDEDGKEGEIWISSPSAGIGYW----GKEELSQKTFRNKLQKFPGRKYT-----RTGDLGRVIQ- 943
Cdd:PRK05620   365 ASLEYRIVNDGQVME-STDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFTadgwlRTGDVGSVTRd 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  944 GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVISVPEDvlsaKGISLPDAsdevgLVVIAelkDGKPVD 1023
Cdd:PRK05620   444 GFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE---CAVIGYPDD----KWGERPLA-----VTVLA---PGIEPT 508

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1024 KDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGTLN--TVPDP 1081
Cdd:PRK05620   509 RETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADGDFEiiKLKGP 568
PLN02654 PLN02654
acetate-CoA ligase
 889-1088 1.11e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 54.13  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  889 VDEDGKE--GE------IWISSPSAGIGYWGKEELSQKTFrnkLQKFPGrkYTRTGD-LGRVIQGNLFITGRIKDLIIVA 959
Cdd:PLN02654   468 VDEKGKEieGEcsgylcVKKSWPGAFRTLYGDHERYETTY---FKPFAG--YYFSGDgCSRDKDGYYWLTGRVDDVINVS 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  960 GRNIYSADVEktvesSSELLRPGC--CAVISVPEDVlsaKGislpdasdeVGLVVIAELKDGKPVDKDIIKQIESRVAEE 1037
Cdd:PLN02654   543 GHRIGTAEVE-----SALVSHPQCaeAAVVGIEHEV---KG---------QGIYAFVTLVEGVPYSEELRKSLILTVRNQ 605

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721 1038 HGVTVASVKLIRPRTISKTTSGKIKRfECLKQFVD------GTLNTVPDPIVTKRLL 1088
Cdd:PLN02654   606 IGAFAAPDKIHWAPGLPKTRSGKIMR-RILRKIASrqldelGDTSTLADPGVVDQLI 661
PRK12316 PRK12316
peptide synthase; Provisional
 674-969 1.20e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 54.19  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSwLPQYHDMGlIGGLFTAMVCGGTAILFSPlT 752
Cdd:PRK12316   654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYgLGVGDTVLQK-TPFSFDVS-VWEFFWPLMSGARLVVAAP-G 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FIRNPLLWLQTIsdykATHSAGpnfAFELVIRRLEADKAKAHDYDLSSMIFFMIAAEPVRQKTLKRFVELtrpygLSQEV 832
Cdd:PRK12316   731 DHRDPAKLVELI----NREGVD---TLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAK-----LPQAG 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  833 MAPGYGLAENCVFVGC-----AYGKKKPIlvdwqGRICcgyvdpndADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGI 907
Cdd:PRK12316   799 LYNLYGPTEAAIDVTHwtcveEGGDSVPI-----GRPI--------ANLACYILDAN--LEPVPVGVLGELYLAGRGLAR 863

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721  908 GYWGKEELSQKTFRNKLQKFPGRKYtRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK12316   864 GYHGRPGLTAERFVPSPFVAGERMY-RTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIE 925
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
661-770 1.37e-06

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 53.89  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  661 LPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMV 740
Cdd:PRK10252   584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFI 662

                           90       100       110
                   ....*....|....*....|....*....|
gi 1973708721  741 CGGTAILFSPLTFiRNPLLWLQTISDYKAT 770
Cdd:PRK10252   663 AGAKLVMAEPEAH-RDPLAMQQFFAEYGVT 691
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 673-996 2.41e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 52.79  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQ---YHDMGLIgglftAMVCGGTAILF- 748
Cdd:PLN02736   219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLahiYERVNQI-----VMLHYGVAVGFy 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 --------------SPLTFIRNPLLWlQTISD--YKATHSAGP------NFAFELVIRRLEADKAKAHDYDlsSMIFFMI 806
Cdd:PLN02736   294 qgdnlklmddlaalRPTIFCSVPRLY-NRIYDgiTNAVKESGGlkerlfNAAYNAKKQALENGKNPSPMWD--RLVFNKI 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  807 AAepvRQKTLKRFVeLTRPYGLSQEVM-----------APGYGLAE-NCVFVGCAygkkkpilvdwQGRICCGYVDPNDA 874
Cdd:PLN02736   371 KA---KLGGRVRFM-SSGASPLSPDVMeflricfggrvLEGYGMTEtSCVISGMD-----------EGDNLSGHVGSPNP 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  875 DVDIRIVDADTGLEVDEDG--KEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRVIQ-GNLFITGR 951
Cdd:PLN02736   436 ACEVKLVDVPEMNYTSEDQpyPRGEICVRGPIIFKGYYKDEVQTREVIDED-------GWLHTGDIGLWLPgGRLKIIDR 508

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973708721  952 IKDLIIVA-GRNIYSADVEKTVESS---------SELLRPGCCAVISVPEDVLSA 996
Cdd:PLN02736   509 KKNIFKLAqGEYIAPEKIENVYAKCkfvaqcfvyGDSLNSSLVAVVVVDPEVLKA 563
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1086-1188 2.77e-06

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 51.67  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1086 RLLTRSFTTGTCREGNTPRSHLAKSSLPPSPKLSNRNIVEFLKQLVSEQTGISIQNISATESLVSYGIDSIGVVRAAQKL 1165
Cdd:COG3433    183 ALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERW 262

                           90       100
                   ....*....|....*....|...
gi 1973708721 1166 SDfLGVPVGAVDIFTATCIADLA 1188
Cdd:COG3433    263 RK-AGLDVSFADLAEHPTLAAWW 284
PRK13984 PRK13984
putative oxidoreductase; Provisional
 16-60 3.54e-06

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 52.46  E-value: 3.54e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1973708721   16 PCLPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGM 60
Cdd:PRK13984   278 EPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGV 321
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 22-94 3.56e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 52.15  E-value: 3.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYR---DITVIEKHNTVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLG 77
PLN02479 PLN02479
acetate-CoA ligase
 680-1065 4.04e-06

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 52.15  E-value: 4.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  680 LQFTSGSTGDAKGVMITHGGlihnVKLMrrryrSTSNTVLvsW-----------LPQYHDMGLIGGLFTAMVCGgTAILF 748
Cdd:PLN02479   200 LGYTSGTTASPKGVVLHHRG----AYLM-----ALSNALI--WgmnegavylwtLPMFHCNGWCFTWTLAALCG-TNICL 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLTfirnPLLWLQTISDYKATHSAGPNFAFELVIRRLEADKAkahdYDLSSMIFFMIA-AEP---VRQKTLKRFVELTR 824
Cdd:PLN02479   268 RQVT----AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI----LPLPRVVHVMTAgAAPppsVLFAMSEKGFRVTH 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  825 PYGLSQEvmapgYGLAENCVFvgcaygkkKP----ILVDWQGRICC----GYVDPNDADVdiriVDADTGLEVDEDGKE- 895
Cdd:PLN02479   340 TYGLSET-----YGPSTVCAW--------KPewdsLPPEEQARLNArqgvRYIGLEGLDV----VDTKTMKPVPADGKTm 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  896 GEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLG-RVIQGNLFITGRIKDLIIVAGRNIYSADVEKT--- 971
Cdd:PLN02479   403 GEIVMRGNMVMKGYLKNPKANEEAFANG--------WFHSGDLGvKHPDGYIEIKDRSKDIIISGGENISSLEVENVvyt 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  972 ---VESSSELLRP------GCCAVISVPEDVlsakgislpDASDEVGLVviaelkdgkpvdKDIIKQIESRVAeehGVTV 1042
Cdd:PLN02479   475 hpaVLEASVVARPderwgeSPCAFVTLKPGV---------DKSDEAALA------------EDIMKFCRERLP---AYWV 530

                          410       420
                   ....*....|....*....|...
gi 1973708721 1043 ASVKLIRPrtISKTTSGKIKRFE 1065
Cdd:PLN02479   531 PKSVVFGP--LPKTATGKIQKHV 551
PRK05691 PRK05691
peptide synthase; Validated
 649-1021 4.13e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 52.48  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  649 LHTDSWIKSSKVLPASNigsqsesqpDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHD 728
Cdd:PRK05691  1256 LHLDSWPSQAPGLHLHG---------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD 1326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  729 MGlIGGLFTAMVCGGTAILFSPLTFiRNPLLWLQTISDYKAT--HSAGPnfAFELVIRrlEADKAKAHDYDLssmIFFMI 806
Cdd:PRK05691  1327 VS-VWECFWPLITGCRLVLAGPGEH-RDPQRIAELVQQYGVTtlHFVPP--LLQLFID--EPLAAACTSLRR---LFSGG 1397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  807 AAEP--VRQKTLKRF--VELTRPYGLSQEvmapgyglAENCVFVGC--AYGKKKPIlvdwqGR----ICCgyvdpndadv 876
Cdd:PRK05691  1398 EALPaeLRNRVLQRLpqVQLHNRYGPTET--------AINVTHWQCqaEDGERSPI-----GRplgnVLC---------- 1454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  877 diRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQKFPGRKYTRTGDLGR-VIQGNLFITGRIKDL 955
Cdd:PRK05691  1455 --RVLDAE--LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARwNADGALEYLGRLDQQ 1530

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  956 IIVAGRNIYSADVEKTVessseLLRPGCC-AVISVPEDVLSAKGI---SLPDASDEVGLVVIAELKDGKP 1021
Cdd:PRK05691  1531 VKLRGFRVEPEEIQARL-----LAQPGVAqAAVLVREGAAGAQLVgyyTGEAGQEAEAERLKAALAAELP 1595
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1372-1433 4.22e-06

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 47.45  E-value: 4.22e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1372 ITDPSLVSIGDGAVIAEGALLQSH--------EVRNSVLRFQPIRIGRNCSVGPYAVIQKGSVLGEGAEV 1433
Cdd:cd04647     16 ISAGGGITIGDNVLIGPNVTIYDHnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 662-771 4.61e-06

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 51.80  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  662 PASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITH----------GGLIhnvklmrrryRSTSNTVLVSWLPQYHDMGL 731
Cdd:PRK08279   186 PTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLL----------RLTPDDVLYCCLPLYHNTGG 255

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1973708721  732 IGGLFTAMVCGGTAIL---FSPLTFirnpllWLQtISDYKATH 771
Cdd:PRK08279   256 TVAWSSVLAAGATLALrrkFSASRF------WDD-VRRYRATA 291
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1342-1433 4.79e-06

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 51.57  E-value: 4.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1342 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIaegalLQSHeVRNSVlrfqpirIGRNCSVGPYAV 1420
Cdd:COG1207    279 VILEGKTVIGE-----GVVIGPnCTLKDST---------IGDGVVI-----KYSV-IEDAV-------VGAGATVGPFAR 331

                           90
                   ....*....|...
gi 1973708721 1421 IQKGSVLGEGAEV 1433
Cdd:COG1207    332 LRPGTVLGEGVKI 344
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 834-969 4.82e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 51.53  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  834 APGYGLAENCVFVgCAYgkkKPilvD--WQGRICCGYVDPNdADVDIRivdadtglevdeDGKEGEIWISSPSAGIGYWG 911
Cdd:PRK07445   258 APTYGMTETASQI-ATL---KP---DdfLAGNNSSGQVLPH-AQITIP------------ANQTGNITIQAQSLALGYYP 317

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  912 keelsqktfrnklQKFPGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK07445   318 -------------QILDSQGIFETDDLGYLDaQGYLHILGRNSQKIITGGENVYPAEVE 363
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1608-1700 6.23e-06

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.33  E-value: 6.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1608 AKVGKYCSIrsinpvaDPrMVSIGAGVHLGDFSRIMtgfysqsgyiqSNVHVKDNSVIGSQSLILPGSVVEKDVILGAis 1687
Cdd:cd03352      2 AKIGENVSI-------GP-NAVIGEGVVIGDGVVIG-----------PGVVIGDGVVIGDDCVIHPNVTIYEGCIIGD-- 60

                           90
                   ....*....|...
gi 1973708721 1688 vapvNSVLQSGGV 1700
Cdd:cd03352     61 ----RVIIHSGAV 69
PRK12467 PRK12467
peptide synthase; Provisional
 673-941 6.29e-06

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 52.09  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMVCGGTAIlfsplt 752
Cdd:PRK12467  3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLV------ 3307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 fIRNPLLW--LQTISDYKATHSAGPNFAFELVIRRLE-ADKAKAHdyDLSSMIFFMIAAEPVRQKTLKRFVE---LTRPY 826
Cdd:PRK12467  3308 -VRDNDLWdpEELWQAIHAHRISIACFPPAYLQQFAEdAGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKprgLTNGY 3384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  827 GLSQEVMAPgygLAENCVFVGCAYGKKKPILVDWQGRICcgYVdpndadvdirivdADTGLEVDEDGKEGEIWISSPSAG 906
Cdd:PRK12467  3385 GPTEAVVTV---TLWKCGGDAVCEAPYAPIGRPVAGRSI--YV-------------LDGQLNPVPVGVAGELYIGGVGLA 3446

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1973708721  907 IGYWGKEELSQKTF-RNKLQKFPGRKYtRTGDLGRV 941
Cdd:PRK12467  3447 RGYHQRPSLTAERFvADPFSGSGGRLY-RTGDLARY 3481
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 21-59 8.11e-06

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 50.63  E-value: 8.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVIEKHNTVGG 59
Cdd:COG2072      6 HVDVVVIGAGQAGLAAAYHLRRAG-IDFVVLEKADDVGG 43
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 880-1063 1.52e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 50.14  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  880 IVDaDTGLEVdEDGKEGEIWISSPSAGI--GYWGKEELSQKTFrnkLQKFPGRKYTrtGDLGRVIQ-GNLFITGRIKDLI 956
Cdd:PRK00174   437 VVD-EEGNPL-EGGEGGNLVIKDPWPGMmrTIYGDHERFVKTY---FSTFKGMYFT--GDGARRDEdGYYWITGRVDDVL 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  957 IVAGRNIYSADVEKTV---ESSSEllrpgcCAVISVPEDVlsaKGISLpdasdeVGLVViaeLKDGKPVDKDIIKQIESR 1033
Cdd:PRK00174   510 NVSGHRLGTAEIESALvahPKVAE------AAVVGRPDDI---KGQGI------YAFVT---LKGGEEPSDELRKELRNW 571

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1973708721 1034 VAEEHGvTVASVKLIR-----PrtisKTTSGKIKR 1063
Cdd:PRK00174   572 VRKEIG-PIAKPDVIQfapglP----KTRSGKIMR 601
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1608-1688 1.57e-05

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 44.93  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1608 AKVGKYCSIRSINPVADPrmVSIGAGVHLGDFSRIMTGFYSQSGYIqsnVHVKDNSVIGSQSLILPGSVVEKDVILGAIS 1687
Cdd:cd00208      1 VFIGEGVKIHPKAVIRGP--VVIGDNVNIGPGAVIGAATGPNEKNP---TIIGDNVEIGANAVIHGGVKIGDNAVIGAGA 75


                   .
gi 1973708721 1688 V 1688
Cdd:cd00208     76 V 76
Catalase pfam00199
Catalase;
1873-2002 1.91e-05

Catalase;


Pssm-ID: 459708  Cd Length: 383  Bit Score: 49.30  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1873 DSYAEMHYYSniCRLFRF--KDGQEMYVKFKLRP-----------SDKNIGEDtgkvepsgilppetgaipRDandtrpl 1939
Cdd:pfam00199  180 RSYRHMNGFG--VHTFKLvnADGERVYVKFHFKTdqgiknltweeAQKLAGKD------------------PD------- 232

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721 1940 lFLAEDFQNRVKSPNGVRYIFQLQVMPVPQDEAAR-DIaLDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:pfam00199  233 -YHTRDLYEAIERGDYPSWTLYVQVMTEEDAEKFRfNP-FDLTKVWPHKDYPLIEVGKMVLNRN 294
PLN02576 PLN02576
protoporphyrinogen oxidase
 21-94 1.91e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 49.63  E-value: 1.91e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYRDITVIEKHNTVGGMCESVEIEGKVYDLGgqvlaANS---APVIFHLAKESG 94
Cdd:PLN02576    12 SKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEG-----PNSfqpSDPELTSAVDSG 83
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1658-1705 2.42e-05

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.94  E-value: 2.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1973708721 1658 HVKDNSVIGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGSQ 1705
Cdd:COG0663     90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSP 137
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 1353-1431 2.43e-05

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 45.29  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1353 WFEMLGAR--IGSSVLLDTVDitdpsLVSIGDGAVIAEGALL--QSHEVRNSVLRF--QPIRIGRNCSVGPYAVIQKGSV 1426
Cdd:cd05825      2 WNLTIGDNswIGEGVWIYNLA-----PVTIGSDACISQGAYLctGSHDYRSPAFPLitAPIVIGDGAWVAAEAFVGPGVT 76


                   ....*
gi 1973708721 1427 LGEGA 1431
Cdd:cd05825     77 IGEGA 81
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1609-1688 2.50e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 45.14  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1609 KVGKYCSIRSINPVADPRMVSIGAGVHLGDFSRIMT---GFYSQSGYIQSN-----VHVKDNSVIGSQSLILPGSVVEKD 1680
Cdd:cd04647      3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDhnhDIDDPERPIEQGvtsapIVIGDDVWIGANVVILPGVTIGDG 82


                   ....*...
gi 1973708721 1681 VILGAISV 1688
Cdd:cd04647     83 AVVGAGSV 90
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
23-264 3.23e-05

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 48.96  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKlgYRDITVIEKHNTVGGMCESVEIegkvyDLGGQVLAANSAPVIF------HLakesgtq 96
Cdd:COG2907      5 RIAVIGSGISGLTAAWLLSR--RHDVTLFEANDRLGGHTHTVDV-----DLDGRTVPVDTGFIVFnertypNL------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 leemdlhkLALIDSLtgeyhDINVAEDYMSL-VSL-------------TLDIQDK----------AKDTNRIGIHAVSEI 152
Cdd:COG2907     71 --------TALFAEL-----GVPTQPSDMSFsVSLdgggleyagsnlnGLFAQRRnllrprfwrmLRDILRFNREAPALL 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  153 ASDLTP-----AYLEAHGIksvPKSVQYGY-----TA---SGYGFVQDMPYAYIHEFTRT----SMAGKI--RRMKGG-- 211
Cdd:COG2907    138 EAGSDDdltlgEFLDRNGY---SEAFRDHYllpmgAAiwsCPPDDMLDFPARFFVRFFHNhgllSVTDRPqwRTVKGGsr 214

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  212 -YMnlwKKISESLLIKVCCNTEVQAVRRNGSGvnVDITNSSGETEHkeFDKIII 264
Cdd:COG2907    215 eYV---RRLTAGLKDRIRLNTPVRSVRRDADG--VEVRTADGEEER--FDHVVF 261
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 674-744 3.28e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 49.27  E-value: 3.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLM---RRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGT 744
Cdd:PRK12582   219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQeqlRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGT 292
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 674-992 4.00e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 48.62  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDL-CFLQFTSGSTGDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMVCGGTAILFSPL 751
Cdd:PRK07786   172 PNDSpALIMYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGI-GSMLPGLLLGAPTVIYPLG 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  752 TFirNPLLWLQTISDYKATHsagpnfAFeLVIRRLEA--DKAKAHDYDLSsMIFFMIAAEPVRQKTLKRFVElTRPYGL- 828
Cdd:PRK07786   251 AF--DPGQLLDVLEAEKVTG------IF-LVPAQWQAvcAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAA-TFPEAQi 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  829 ----SQEVMAPgyglaENCVFVG-------CAYGKKKPILvdwQGRIccgyVDPNDADVDIrivdadtglevdedGKEGE 897
Cdd:PRK07786   320 laafGQTEMSP-----VTCMLLGedairklGSVGKVIPTV---AARV----VDENMNDVPV--------------GEVGE 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  898 IWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrkYTRTGDLGRV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 976
Cdd:PRK07786   374 IVYRAPTLMSGYWNNPEATAEAFAGG--------WFHSGDLVRQdEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHP 445

                          330
                   ....*....|....*.
gi 1973708721  977 ELLRpgcCAVISVPED 992
Cdd:PRK07786   446 DIVE---VAVIGRADE 458
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 23-59 4.37e-05

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 48.16  E-value: 4.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGG 59
Cdd:pfam01266    1 DVVVIGGGIVGLSTAYELARRGL-SVTLLERGDDPGS 36
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 22-95 4.87e-05

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 48.31  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIEgkvyDLG-----GQ--VLAANSApvIFHLAKESG 94
Cdd:COG3349      4 PRVVVVGGGLAGLAAAVELAEAGFR-VTLLEARPRLGGRARSFPDP----DTGlpidnGQhvLLGCYRN--TLDLLRRIG 76


                   .
gi 1973708721   95 T 95
Cdd:COG3349     77 A 77
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
18-60 4.90e-05

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.32  E-value: 4.90e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1973708721   18 LPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGM 60
Cdd:COG1148    137 VPVNKRALVIGGGIAGMTAALELAEQGY-EVYLVEKEPELGGR 178
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 23-60 4.92e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 48.57  E-value: 4.92e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGM 60
Cdd:PRK12814   195 KVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGM 231
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
21-60 5.08e-05

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 48.41  E-value: 5.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYR--DITVIEKHNTVG-GM 60
Cdd:COG4529      5 RKRIAIIGGGASGTALAIHLLRRAPEplRITLFEPRPELGrGV 47
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 676-1023 5.80e-05

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 48.12  E-value: 5.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  676 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMVCGGTAIL---FSPLT 752
Cdd:cd05940     82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASN 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  753 FirnpllWlQTISDYKAThsagpnfAFELV---IRRLEADKAKAHDYDLSsmiFFMIAAEPVRQKTLKRFveLTRpYGLS 829
Cdd:cd05940    162 F------W-DDIRKYQAT-------IFQYIgelCRYLLNQPPKPTERKHK---VRMIFGNGLRPDIWEEF--KER-FGVP 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  830 QevMAPGYGLAE-NCVFVGCAyGKKKPIlvdwqGRIccGYVDPNDADVDIRIVDADTGLEV-DEDGK-----EGEIW--- 899
Cdd:cd05940    222 R--IAEFYAATEgNSGFINFF-GKPGAI-----GRN--PSLLRKVAPLALVKYDLESGEPIrDAEGRcikvpRGEPGlli 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  900 --ISSPSAGIGYWGKEELSQKTFRNKLQKfpGRKYTRTGDLGRVI-QGNLFITGRIKDLIIVAGRNIYSADVEktvesss 976
Cdd:cd05940    292 srINPLEPFDGYTDPAATEKKILRDVFKK--GDAWFNTGDLMRLDgEGFWYFVDRLGDTFRWKGENVSTTEVA------- 362

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1973708721  977 ellrpgccAVISVPEDVLSAK--GISLPDASDEVGLVVIAeLKDGKPVD 1023
Cdd:cd05940    363 --------AVLGAFPGVEEANvyGVQVPGTDGRAGMAAIV-LQPNEEFD 402
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 675-955 6.32e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.43  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  675 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRS-----TSNTVLVSWLPQYHDMGLigGLFTAMVCGGTAILF- 748
Cdd:PTZ00216   264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligppEEDETYCSYLPLAHIMEF--GVTNIFLARGALIGFg 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 SPLT----FIR--------NPLLWL------QTISdyKATHSAGP----------NFAFELVIRRLEADK---------- 790
Cdd:PTZ00216   342 SPRTltdtFARphgdltefRPVFLIgvprifDTIK--KAVEAKLPpvgslkrrvfDHAYQSRLRALKEGKdtpywnekvf 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  791 AKAHDYDLSSMIFFMIAAEPVRQKTlKRFVELTrpYGLsqevMAPGYGLAENCvfvgCAYGKKKPilvdwqGRICCGYVD 870
Cdd:PTZ00216   420 SAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNVV--FGM----VIQGWGLTETV----CCGGIQRT------GDLEPNAVG 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  871 PNDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqkfpgrKYTRTGDLGRV-IQGNLFIT 949
Cdd:PTZ00216   483 QLLKGVEMKLLDTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDED-------GWFHTGDVGSIaANGTLRII 555


                   ....*.
gi 1973708721  950 GRIKDL 955
Cdd:PTZ00216   556 GRVKAL 561
catalase_clade_3 cd08156
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1760-2002 6.52e-05

Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163712 [Multi-domain]  Cd Length: 429  Bit Score: 47.91  E-value: 6.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1760 GYLKLYDDIQGLPEHNIFGP-GKKYTVIVRHSN----SLSADddARLDARGAALRILSDEK-----GDDSPLldltlktg 1829
Cdd:cd08156     16 GTFEVTHDITKYTKAKIFSEvGKKTPVFVRFSTvageRGSAD--TERDPRGFALKFYTEEGnwdlvGNNTPV-------- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1830 kaFYAR---TISDFAtwlvcglaareeH-VKRVP--HVRDA-----VWT----SLRQA----------DSYAEMHYYSNI 1884
Cdd:cd08156     86 --FFIRdpiKFPDFI------------HtQKRNPqtNLKDPdmfwdFWSlspeSLHQVtilfsdrgipDGYRHMNGYGSH 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1885 CRLFRFKDGQEMYVKFKLRpSD---KNIGEDTGKvepsgilppETGAIPRDandtrpllFLAEDFQNRVKSPNGVRYIFQ 1961
Cdd:cd08156    152 TFSLVNAKGERFWVKFHFK-TDqgiKNLTNEEAA---------ELAGEDPD--------YAQRDLFEAIERGDFPSWTLY 213

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1973708721 1962 LQVMPVPQDEAARDIALDCTKPWDESQFPYIDVGEVIINEN 2002
Cdd:cd08156    214 VQVMPEEDAEKYRFNPFDLTKVWPHKDYPLIEVGKLELNRN 254
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1607-1700 6.63e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 47.32  E-value: 6.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1607 GAKVGKYCSIrsinpvaDPrMVSIGAGVHLGDFSRIMtgfysqsgyiqSNVHVKDNSVIGSQSLILPGSVVEKDVILGAi 1686
Cdd:COG1044    108 SAKIGEGVSI-------GP-FAVIGAGVVIGDGVVIG-----------PGVVIGDGVVIGDDCVLHPNVTIYERCVIGD- 167

                           90
                   ....*....|....
gi 1973708721 1687 svapvNSVLQSGGV 1700
Cdd:COG1044    168 -----RVIIHSGAV 176
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 674-952 8.49e-05

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 47.95  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYH------DMGLI---GGlfTAMVCG 742
Cdd:PRK08180   208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHtfggnhNLGIVlynGG--TLYIDD 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  743 G--TAILFSplTFIRNpllwLQTISdykathsagPNF------AFELVIRRLEADKAKAHDYdLSSMIFFMIAAEPVRQK 814
Cdd:PRK08180   286 GkpTPGGFD--ETLRN----LREIS---------PTVyfnvpkGWEMLVPALERDAALRRRF-FSRLKLLFYAGAALSQD 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  815 TLKRFVELTRPYGLSQEVMAPGYGLAENCVFVGCAYGkkkpiLVDWQGRIccGYVDPNdadVDIRIVDADTGLEVDEDGk 894
Cdd:PRK08180   350 VWDRLDRVAEATCGERIRMMTGLGMTETAPSATFTTG-----PLSRAGNI--GLPAPG---CEVKLVPVGGKLEVRVKG- 418

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1973708721  895 egeiwissPSAGIGYWGKEELSQKTFRNKlqkfpGrkYTRTGDLGRVI------QGNLFiTGRI 952
Cdd:PRK08180   419 --------PNVTPGYWRAPELTAEAFDEE-----G--YYRSGDAVRFVdpadpeRGLMF-DGRI 466
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1355-1433 1.06e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.41  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1355 EMLGARIGSSVLLDTVDITDPSLVSIGDGAV------------------IAEGALLQSH-EVRNSVL----------RFQ 1405
Cdd:PRK14356   241 ELLRARIVEKHLESGVLIHAPESVRIGPRATiepgaeiygpceiygasrIARGAVIHSHcWLRDAVVssgatihsfsHLE 320

                           90       100
                   ....*....|....*....|....*...
gi 1973708721 1406 PIRIGRNCSVGPYAVIQKGSVLGEGAEV 1433
Cdd:PRK14356   321 GAEVGDGCSVGPYARLRPGAVLEEGARV 348
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
21-54 1.11e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 46.82  E-value: 1.11e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVIEKH 54
Cdd:COG0665      2 TADVVVIGGGIAGLSTAYHLARRG-LDVTVLERG 34
PRK10502 PRK10502
putative acyl transferase; Provisional
 1348-1434 1.22e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 44.94  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1348 VFLKHWFemlGARIGSSVLLD-TVDITDPSLVSIGDGAVIAEGALL---------------Q-------SHEVRNSV--L 1402
Cdd:PRK10502    44 AFLLRLF---GAKIGKGVVIRpSVRITYPWKLTIGDYAWIGDDVWLynlgeitigahcvisQksylctgSHDYSDPHfdL 120

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1973708721 1403 RFQPIRIGR------NCSVGPYAVIQKGSVLGEGAEVL 1434
Cdd:PRK10502   121 NTAPIVIGEgcwlaaDVFVAPGVTIGSGAVVGARSSVF 158
PLN03000 PLN03000
amine oxidase
 5-97 1.52e-04

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 47.32  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721    5 KSVEDQFsklhPCLPLDTRIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMCESVEIE----GKVYDLGGQVLAA 80
Cdd:PLN03000   172 QAIKDKF----PAQSSKSSVVIVGAGLSGLAAARQLMRFGFK-VTVLEGRKRPGGRVYTKKMEanrvGAAADLGGSVLTG 246

                           90
                   ....*....|....*..
gi 1973708721   81 NSAPVIFHLAKESGTQL 97
Cdd:PLN03000   247 TLGNPLGIIARQLGSSL 263
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 23-59 1.59e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 46.70  E-value: 1.59e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGG 59
Cdd:PRK12810   145 KVAVVGSGPAGLAAADQLARAGH-KVTVFERADRIGG 180
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 1342-1433 1.80e-04

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 44.72  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1342 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIaegallqsheVRNSVLRFQpiRIGRNCSVGPYAV 1420
Cdd:cd03353     28 VILEGKTVIGE-----DCVIGPnCVIKDST---------IGDGVVI----------KASSVIEGA--VIGNGATVGPFAH 81

                           90
                   ....*....|...
gi 1973708721 1421 IQKGSVLGEGAEV 1433
Cdd:cd03353     82 LRPGTVLGEGVHI 94
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 667-959 1.82e-04

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 46.94  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  667 GSQSE---SQPDDLCFLQFTSGSTGDAKGVMITH-------GGLIHNVKLMRRRYrsTSNTVLVSWLPQYHDMGLIggLF 736
Cdd:PLN02614   212 GKQYDlpiKKKSDICTIMYTSGTTGDPKGVMISNesivtliAGVIRLLKSANAAL--TVKDVYLSYLPLAHIFDRV--IE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  737 TAMVCGGTAILF---------------SPLTFIRNPLLWLQTISDYKATHSAG---PNFAFELVIRRLEADKAKAHDYDL 798
Cdd:PLN02614   288 ECFIQHGAAIGFwrgdvklliedlgelKPTIFCAVPRVLDRVYSGLQKKLSDGgflKKFVFDSAFSYKFGNMKKGQSHVE 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  799 SSMIFFMIAAEPVRQ---KTLKRFVELTRPYGLSQE----VMA-----PGYGLAENCVFVGCAYGKKKPILvdwqgricc 866
Cdd:PLN02614   368 ASPLCDKLVFNKVKQglgGNVRIILSGAAPLASHVEsflrVVAcchvlQGYGLTESCAGTFVSLPDELDML--------- 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  867 GYVDPNDADVDIRIvDADTGLEVDEDGK--EGEIWISSPSAGIGYWGKEELSQKTFRNklqkfpgrKYTRTGDLGR-VIQ 943
Cdd:PLN02614   439 GTVGPPVPNVDIRL-ESVPEMEYDALAStpRGEICIRGKTLFSGYYKREDLTKEVLID--------GWLHTGDVGEwQPN 509

                          330
                   ....*....|....*.
gi 1973708721  944 GNLFITGRIKDLIIVA 959
Cdd:PLN02614   510 GSMKIIDRKKNIFKLS 525
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 22-54 2.02e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 46.17  E-value: 2.02e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYRdITVIEKH 54
Cdd:PRK12409     2 SHIAVIGAGITGVTTAYALAQRGYQ-VTVFDRH 33
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 623-727 3.31e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 45.96  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  623 AGSVKNLISFTRKSAESTAQWPNLPwLHTDSWIKSSKvLPASNIGSQSESQPDDLCFLQFTSGSTGDAKGVMITH---GG 699
Cdd:PLN02430   170 AKRLKAIVSFTSVTEEESDKASQIG-VKTYSWIDFLH-MGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHeavAT 247

                           90       100       110
                   ....*....|....*....|....*....|
gi 1973708721  700 LIHNVKLMRRRY--RSTSNTVLVSWLPQYH 727
Cdd:PLN02430   248 FVRGVDLFMEQFedKMTHDDVYLSFLPLAH 277
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1608-1700 3.42e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1608 AKVGKYCSIrsinpvaDPrMVSIGAGVHLGDFSRIMtgfysqsgyiqSNVHVKDNSVIGSQSLILPGSVVEKDVILGAis 1687
Cdd:PRK00892   113 AKIGEGVSI-------GP-NAVIGAGVVIGDGVVIG-----------AGAVIGDGVKIGADCRLHANVTIYHAVRIGN-- 171

                           90
                   ....*....|...
gi 1973708721 1688 vapvNSVLQSGGV 1700
Cdd:PRK00892   172 ----RVIIHSGAV 180
PRK06753 PRK06753
hypothetical protein; Provisional
 23-178 4.47e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 45.06  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCESVEIEGKV------YDLGGQVLAANSAPVIFHLAKESGTQ 96
Cdd:PRK06753     2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNESVKEVGAGIGIGDNVikklgnHDLAKGIKNAGQILSTMNLLDDKGTL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721   97 LEEM---------DLHKLALIDSLTGEYHDinvaedymSLVSLTLDIQDKAKDTNRIGIHaVSEIASDLTPAYLEAHGIK 167
Cdd:PRK06753    81 LNKVklksntlnvTLHRQTLIDIIKSYVKE--------DAIFTGKEVTKIENETDKVTIH-FADGESEAFDLCIGADGIH 151

                          170
                   ....*....|....*....
gi 1973708721  168 SV------PKS-VQY-GYT 178
Cdd:PRK06753   152 SKvrqsvnADSkVRYqGYT 170
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 1378-1433 4.77e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 42.96  E-value: 4.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973708721 1378 VSIGDGAVIAEGALLQShevrnsvlrfqPIRIGRNCSVGPYAVIQKGSVLGEGAEV 1433
Cdd:cd05636     18 VWIGEGAIVRSGAYIEG-----------PVIIGKGCEIGPNAYIRGYTVLGDGCVV 62
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
26-61 4.81e-04

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 45.15  E-value: 4.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRdITVIEKHNTVGGMC 61
Cdd:PRK05249    10 VIGSGPAGEGAAMQAAKLGKR-VAVIERYRNVGGGC 44
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 1607-1703 5.54e-04

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 5.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1607 GAKVGKYCSIRSinpvadprMVSIGAGVHLGD---------FS--RIMTGFYSQSGYIQSnVHVKDNSVIGSQSLILPGS 1675
Cdd:cd03358     16 DVKIGDNVKIQS--------NVSIYEGVTIEDdvfigpnvvFTndLYPRSKIYRKWELKG-TTVKRGASIGANATILPGV 86

                           90       100
                   ....*....|....*....|....*...
gi 1973708721 1676 VVEKDVILGAISVapVNSVLQSGGVYMG 1703
Cdd:cd03358     87 TIGEYALVGAGAV--VTKDVPPYALVVG 112
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 1607-1704 5.82e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 43.24  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1607 GAKVGKYCSIrsiNPVAdprmvSIGAGVHLGDFSRIMTGfYSQSGyiqsNVHVKDNSVIGSQSLILPGSVVEKDVILGAI 1686
Cdd:cd03360    114 DARIGDNVII---NTGA-----VIGHDCVIGDFVHIAPG-VVLSG----GVTIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                           90
                   ....*....|....*...
gi 1973708721 1687 SVapVNSVLQSGGVYMGS 1704
Cdd:cd03360    181 AV--VTKDVPDGSVVVGN 196
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 649-745 8.02e-04

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 44.75  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  649 LHTDSWIKSSKVLPASNIGSqsESQPDDLCFLQFTSGSTGDAKGVMITHggliHNVKLMRRRYRST-----SNTVLVSWL 723
Cdd:cd17632    199 TLTLIAVRGRDLPPAPLFRP--EPDDDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIqdirpPASITLNFM 272

                           90       100
                   ....*....|....*....|..
gi 1973708721  724 PQYHDMGLIgGLFTAMVCGGTA 745
Cdd:cd17632    273 PMSHIAGRI-SLYGTLARGGTA 293
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
29-58 8.24e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.80  E-value: 8.24e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1973708721   29 GGPSGLSAAYALAKLGYrDITVIEKHNTVG 58
Cdd:COG0644      1 AGPAGSAAARRLARAGL-SVLLLEKGSFPG 29
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
25-60 8.58e-04

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 41.88  E-value: 8.58e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1973708721   25 GIVGGGPSGLSAAYALAKLGYR---DITVIEKHNTVGGM 60
Cdd:pfam13454    1 AIVGGGPSGLALLERLLARAPKrplEITLFDPSPPGAGG 39
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 22-61 9.76e-04

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 44.08  E-value: 9.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGyRDITVIEKhNTVGGMC 61
Cdd:PRK07845     2 TRIVIIGGGPGGYEAALVAAQLG-ADVTVIER-DGLGGAA 39
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 674-711 1.24e-03

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 43.93  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1973708721  674 PDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMRRRY 711
Cdd:cd17648     93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY 130
catalase_clade_1 cd08154
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1962-2015 1.41e-03

Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 1 catalases are found in bacteria, algae, and plants; they have a relatively small subunit size of 55 to 69 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163710 [Multi-domain]  Cd Length: 469  Bit Score: 43.82  E-value: 1.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1973708721 1962 LQVMPvPQDEAARDI-ALDCTKPWDESQFPYIDVGEVIIN---ENLTKEgSERLEFNP 2015
Cdd:cd08154    256 VQIMD-PKDLDKLDFdPLDDTKIWPEDQFPLKPVGKMTLNknpDNFFAE-VEQVAFSP 311
PRK06185 PRK06185
FAD-dependent oxidoreductase;
20-56 1.42e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 43.31  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   20 LDTRIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNT 56
Cdd:PRK06185     5 ETTDCCIVGGGPAGMMLGLLLARAGV-DVTVLEKHAD 40
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 23-59 1.54e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 43.96  E-value: 1.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGG 59
Cdd:PRK12778   433 KVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 26-60 1.58e-03

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 43.37  E-value: 1.58e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1973708721   26 IVGGGPSGLSAAYALAKLGyRDITVIEKHNTVGGM 60
Cdd:pfam12831    4 VVGGGPAGVAAAIAAARAG-AKVLLVERRGFLGGM 37
PRK08401 PRK08401
L-aspartate oxidase; Provisional
 21-51 1.85e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 43.25  E-value: 1.85e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYrDITVI 51
Cdd:PRK08401     1 MMKVGIVGGGLAGLTAAISLAKKGF-DVTII 30
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 23-62 1.92e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 39.11  E-value: 1.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGMCE 62
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGS-KVTVVERRDRLLPGFD 39
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 21-56 2.05e-03

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 42.70  E-value: 2.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1973708721   21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVIEKHNT 56
Cdd:pfam01494    1 ETDVLIVGGGPAGLMLALLLARAGVR-VVLVERHAT 35
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1378-1433 2.09e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.93  E-value: 2.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973708721 1378 VSIGDGAVI-----AEGAllqshevrnsvlrfqpiRIGRNCSVGPYAVIQKGSVLGEGAEV 1433
Cdd:PRK14353   287 VTVASGAVIhafshLEGA-----------------HVGEGAEVGPYARLRPGAELGEGAKV 330
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 24-59 2.12e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 42.07  E-value: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1973708721   24 IGIVGGGPSGLSAAYALAKLGYRDITVIEKHNTVGG 59
Cdd:pfam01946   20 VVIVGAGSSGLTAAYYLAKNRGLKVAIIERSVSPGG 55
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1378-1431 2.30e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.70  E-value: 2.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973708721 1378 VSIGDGAVIAEGAllqshevrnsvlrfqpiRIGRNCSVGPYAVIQKGSVLGEGA 1431
Cdd:COG1044    115 VSIGPFAVIGAGV-----------------VIGDGVVIGPGVVIGDGVVIGDDC 151
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
26-58 2.56e-03

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 42.83  E-value: 2.56e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRDITVIEKHNTVG 58
Cdd:COG0579      9 IIGAGIVGLALARELSRYEDLKVLVLEKEDDVA 41
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 861-969 2.86e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 42.77  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  861 QGRICCGyvdpndadVDIRIVDADtGLEVDEDGKE-GEIWISSPSAGIGYWGKEElsqktfrNKLQK--FPgrkytrTGD 937
Cdd:PRK07008   358 QGRVIYG--------VDMKIVGDD-GRELPWDGKAfGDLQVRGPWVIDRYFRGDA-------SPLVDgwFP------TGD 415

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1973708721  938 LGRV-IQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK07008   416 VATIdADGFMQITDRSKDVIKSGGEWISSIDIE 448
PRK05691 PRK05691
peptide synthase; Validated
 672-703 3.50e-03

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 42.85  E-value: 3.50e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1973708721  672 SQPDDLCFLQFTSGSTGDAKGVMITHGGLIHN 703
Cdd:PRK05691  3866 SGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN 3897
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 23-60 3.58e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 41.90  E-value: 3.58e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGGM 60
Cdd:PRK12770    20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGL 56
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
26-67 3.92e-03

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 41.64  E-value: 3.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1973708721   26 IVGGGPSGLSAAYALAKLGyRDITVIEKhNTVGGMC-ESVEIE 67
Cdd:COG0492      5 IIGAGPAGLTAAIYAARAG-LKTLVIEG-GEPGGQLaTTKEIE 45
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 664-727 4.02e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 42.52  E-value: 4.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721  664 SNIGSQSESQP----DDLCFLQFTSGSTGDAKGVMITHGGLIHNV----KLMRRRYRS-TSNTVLVSWLPQYH 727
Cdd:PLN02861   205 SLMGSLDCELPpkqkTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstdHLLKVTDRVaTEEDSYFSYLPLAH 277
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1359-1429 4.62e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 4.62e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1973708721 1359 ARIGSSVLLDtvditdpSLVSIGDGAVIAEGALLQSHEV--RNSvlrfqpiRIGRNCSVGPYAVIQKGSVLGE 1429
Cdd:PRK00892   113 AKIGEGVSIG-------PNAVIGAGVVIGDGVVIGAGAVigDGV-------KIGADCRLHANVTIYHAVRIGN 171
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1384-1435 4.63e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.54  E-value: 4.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973708721 1384 AVIAEGAllqshevrnsvlrfqpiRIGRNCSVGPYAVIQKGSVLGEGAEVLA 1435
Cdd:COG1044    103 AVIDPSA-----------------KIGEGVSIGPFAVIGAGVVIGDGVVIGP 137
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1123-1190 4.87e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 38.00  E-value: 4.87e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973708721  1123 IVEFLKQLVSEQTGISI-QNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANF 1190
Cdd:smart00823   13 LLDLVREQVAAVLGHAAaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1603-1685 5.12e-03

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.47  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721 1603 LHLLGAKVGKYCSIRSINPVADPRmVSIGAGVHLGDFSRImtgfysqsgYIQSNVHVKDNSVIGSQSLILPGS------- 1675
Cdd:COG0110      4 LLLFGARIGDGVVIGPGVRIYGGN-ITIGDNVYIGPGVTI---------DDPGGITIGDNVLIGPGVTILTGNhpiddpa 73

                           90
                   ....*....|....*....
gi 1973708721 1676 ---------VVEKDVILGA 1685
Cdd:COG0110     74 tfplrtgpvTIGDDVWIGA 92
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 673-970 5.60e-03

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 41.78  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  673 QPDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK----LMRRryrSTSNTVLVSwLPQYHDMGLiGGLFTAMVCGGTailf 748
Cdd:PRK09029   133 QPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEgvlsLMPF---TAQDSWLLS-LPLFHVSGQ-GIVWRWLYAGAT---- 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  749 spLTfIRNPLLWLQTISDykATHSAgpnfafeLV---IRRLEADKAkahdydlssmiffmiaaEPVrqkTLKRF------ 819
Cdd:PRK09029   204 --LV-VRDKQPLEQALAG--CTHAS-------LVptqLWRLLDNRS-----------------EPL---SLKAVllggaa 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  820 --VELT---RPYGLSQEVmapGYGLAENCVFVgCAygkKKpilVDwqGRICCGYVDPNDadvDIRIVDadtglevdedgk 894
Cdd:PRK09029   252 ipVELTeqaEQQGIRCWC---GYGLTEMASTV-CA---KR---AD--GLAGVGSPLPGR---EVKLVD------------ 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973708721  895 eGEIWISSPSAGIGYWGKEEL-----SQKTFRNKlqkfpgrkytrtgDLGRVIQGNLFITGRIKDLIIVAGRNIYSADVE 969
Cdd:PRK09029   305 -GEIWLRGASLALGYWRQGQLvplvnDEGWFATR-------------DRGEWQNGELTILGRLDNLFFSGGEGIQPEEIE 370


                   .
gi 1973708721  970 K 970
Cdd:PRK09029   371 R 371
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 26-58 7.06e-03

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 40.77  E-value: 7.06e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRdITVIEKHNTVG 58
Cdd:TIGR02032    5 VVGAGPAGASAAYRLADKGLR-VLLLEKKSFPR 36
PRK12831 PRK12831
putative oxidoreductase; Provisional
 23-59 7.62e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.16  E-value: 7.62e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   23 RIGIVGGGPSGLSAAYALAKLGYrDITVIEKHNTVGG 59
Cdd:PRK12831   142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGG 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1378-1430 7.78e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 7.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1973708721 1378 VSIGDGAVIAEGAllqshevrnsvlrfqpiRIGRNCSVGPYAVIQKGSVLGEG 1430
Cdd:PRK00892   119 VSIGPNAVIGAGV-----------------VIGDGVVIGAGAVIGDGVKIGAD 154
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
22-56 8.47e-03

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 40.89  E-value: 8.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1973708721   22 TRIGIVGGGPSGLSAAYALAKLGYRD--ITVIEKHNT 56
Cdd:COG1252      2 KRIVIVGGGFAGLEAARRLRKKLGGDaeVTLIDPNPY 38
GIDA pfam01134
Glucose inhibited division protein A;
26-60 8.47e-03

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 41.00  E-value: 8.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1973708721   26 IVGGGPSGLSAAYALAKLGYRDITVIEKHNTVGGM 60
Cdd:pfam01134    4 VIGGGHAGCEAALAAARMGAKVLLITHNTDTIAEL 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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