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Conserved domains on  [gi|1917948728|gb|KAF8012275|]
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hypothetical protein BT93_I0420 [Corymbia citriodora subsp. variegata]

Protein Classification

FAAL and catalase_like domain-containing protein( domain architecture ID 13383628)

protein containing domains PRK07208, FAAL, LbetaH, and catalase_like

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 ...
499-1071 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: 611.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  499 HWAAQeiTQNKALYTWINEGGAVGCQRTYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVI 578
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  579 PIPVLPPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVknlisftgksvkSTGQWPNLPWLHTDSWikssk 658
Cdd:cd05931     75 AVPLPPPTP----GRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVDLL----- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  659 VLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAM 738
Cdd:cd05931    134 PDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPL 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  739 ACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd05931    214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRD--EDLEGLDLSSWRVALNGAEPVRPATLRRF 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  819 VELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPILV-------------------DWQGRICCGYVDPndaDVDIRI 879
Cdd:cd05931    292 AEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQEVRI 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  880 VDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnKLQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAG 959
Cdd:cd05931    369 VDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFG-ALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRG 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  960 RNIYSADVEKTVESSSELLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAEL--RDSKLVNKDIIKQIESRVAEEH 1037
Cdd:cd05931    447 RNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREH 513
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1917948728 1038 GVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1071
Cdd:cd05931    514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
catalase_like super family cl09506
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
1720-2046 6.70e-125

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: 396.80  E-value: 6.70e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1720 EEMDPKYKKIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHDIFGPGKRYTVIVRHSNSLSADDDARL 1799
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1800 DARGAALRILS---DDSPLLDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSFADLHY 1874
Cdd:cd08151     80 DGRGAALRFLNagdDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1875 YSNTCRLFRFKDRQEMYVKFKLRPSDENIEEDIGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFHNRVKSPsGVRYIF 1954
Cdd:cd08151    160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1955 QLQVRPIPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSEKLEVNPfLRCHEVDVIRATSSSQ-SASIDHG 2033
Cdd:cd08151    239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315
                          330
                   ....*....|...
gi 1917948728 2034 RSLIYEICQHLRN 2046
Cdd:cd08151    316 RSLVYEISQRLRK 328
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
1269-1702 9.70e-27

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: 119.09  E-value: 9.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1269 GLPWLHQAsvvlLAPLSWILCIALTSISIAFFGNSFLRINYA------LTPEV-SVWSVDFVKWWALYKAQEVSSKVLav 1341
Cdd:TIGR02353   24 GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPIWGSTYLRFWTVKRLVDAAPTVL-- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1342 hLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHEVRNSILRLQPIRIGRNCSVGPYAV 1419
Cdd:TIGR02353   98 -LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFIGTRST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1420 VQKGSVLREGAEVPALQKSEGGKS-----------ALKMAKAENILK-VSPGTL-KTVQQFMGIYVVGFLsslsaatvyl 1486
Cdd:TIGR02353  175 LDIDTSIGDGAQLGHGSALQGGQSipdgerwhgspAQKTGADYRKVQpARPYTVrRRLYVAGALFVVFVL---------- 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1487 lymslsqkvpsLELLAFLCISGAlhwvpFTIVAYATMFTKAPPNPFEFAISLAIAYFAHGLVLSLLTSIFTHLLAG---K 1563
Cdd:TIGR02353  245 -----------LPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNlvlK 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1564 EKKTQTHikTWFGHQL----AIACHVRFAKLLSG-TEAFCMYLRLLGAKVGRYCSIRAINpIADPRMVSIGAGVHLGDFS 1638
Cdd:TIGR02353  309 PGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGL 385
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1639 RIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:TIGR02353  386 LMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 2.16e-15

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.56  E-value: 2.16e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN super family cl34196
Monoamine oxidase [Amino acid transport and metabolism];
19-264 4.85e-14

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: 76.88  E-value: 4.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   97 LEEM-DLHKLALIDsFTGEYHDIN-VAEDYMSLVSLTLEIQDKAKDSnhIGIHAVSDIASDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAA--LDPWAHPAAELDRESlaEWLRRNGASPSARR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMSLWKKISKSLLIKVCCNTEVQAVRRDGSDVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234
                          250
                   ....*....|....*....
gi 1917948728  246 DITNssGETEHkeFDKIII 264
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV 249
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1124-1185 7.23e-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: 7.23e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1124 EFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1185
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
2103-2302 3.00e-04

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: 46.28  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2103 LQTIVPYFLLGLIIY---FPLNLLLHCknarnMPVhwtfpFFWVSTGILAalTCAAAKYILVGKKKEdETVHIWsrGVFM 2179
Cdd:TIGR02353   16 LQWLAPLLGYNWLYEaldDVSWLYLRA-----VAL-----VFAVPVGRLG--FAIAAKWLLVGRWKP-GTYPIW--GSTY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2180 DTIWQAIRTV--FGDYFVemtSGSALFLMWMKLMGssVELDKGTYVDSMGAALNpEMVEVEGGGSVEREALLFGhvYDGE 2257
Cdd:TIGR02353   81 LRFWTVKRLVdaAPTVLL---SGSPLYSLYLRALG--AKIGKGVDIGSLPPVCT-DLLTIGAGTIVRKEVMLLG--YRAE 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1917948728 2258 GGAVKFGKIVVGEGGFVGSRAVAMPG--VESGGSLSALSLAMKGEAI 2302
Cdd:TIGR02353  153 RGRLHTGPVTLGRDAFIGTRSTLDIDtsIGDGAQLGHGSALQGGQSI 199
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
499-1071 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: 611.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  499 HWAAQeiTQNKALYTWINEGGAVGCQRTYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVI 578
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  579 PIPVLPPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVknlisftgksvkSTGQWPNLPWLHTDSWikssk 658
Cdd:cd05931     75 AVPLPPPTP----GRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVDLL----- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  659 VLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAM 738
Cdd:cd05931    134 PDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPL 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  739 ACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd05931    214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRD--EDLEGLDLSSWRVALNGAEPVRPATLRRF 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  819 VELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPILV-------------------DWQGRICCGYVDPndaDVDIRI 879
Cdd:cd05931    292 AEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQEVRI 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  880 VDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnKLQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAG 959
Cdd:cd05931    369 VDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFG-ALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRG 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  960 RNIYSADVEKTVESSSELLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAEL--RDSKLVNKDIIKQIESRVAEEH 1037
Cdd:cd05931    447 RNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREH 513
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1917948728 1038 GVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1071
Cdd:cd05931    514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
1720-2046 6.70e-125

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: 396.80  E-value: 6.70e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1720 EEMDPKYKKIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHDIFGPGKRYTVIVRHSNSLSADDDARL 1799
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1800 DARGAALRILS---DDSPLLDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSFADLHY 1874
Cdd:cd08151     80 DGRGAALRFLNagdDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1875 YSNTCRLFRFKDRQEMYVKFKLRPSDENIEEDIGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFHNRVKSPsGVRYIF 1954
Cdd:cd08151    160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1955 QLQVRPIPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSEKLEVNPfLRCHEVDVIRATSSSQ-SASIDHG 2033
Cdd:cd08151    239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315
                          330
                   ....*....|...
gi 1917948728 2034 RSLIYEICQHLRN 2046
Cdd:cd08151    316 RSLVYEISQRLRK 328
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
487-1079 3.51e-96

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 325.92  E-value: 3.51e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  487 FPNLPTLDCYLKHWAaqEITQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRVLLVHVPGL 563
Cdd:PRK07769    17 FPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQNL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  564 DFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHAAVRAgLVKNLISFTGKSVKSTGQWP 643
Cdd:PRK07769    91 DYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDD----CTPSAILTTTDSAEGVRK-FFRARPAKERPRVIAVDAVP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  644 NLpwlhtdswIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLP 723
Cdd:PRK07769   166 DE--------VGATWVPPEANE--------DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  724 QYHDMGLIGGLFTAMaCGGSAILFSPLTFIRNPLMWLQTIS----DYKATHSAGPNFAFELVIRRlEADKAKARNYDLSS 799
Cdd:PRK07769   230 FFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFEHAAAR-GLPKDGEPPLDLSN 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  800 MIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDWQ----GRIC--------- 864
Cdd:PRK07769   308 VKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRFVevpadapna 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  865 -----CGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY----------PGR 929
Cdd:PRK07769   388 vaqvsAGKVGVSEWAV---IVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaegapDDA 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  930 KYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPEEVLSAK-------GISL-P 1001
Cdd:PRK07769   464 LWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVvfddshaGLKFdP 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1002 DASDEvGLVVIAELR--DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNL----- 1074
Cdd:PRK07769   544 EDTSE-QLVIVAERApgAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLrsgyg 622

                   ....*.
gi 1917948728 1075 -NTVPD 1079
Cdd:PRK07769   623 qPAFPD 628
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
479-1074 1.91e-92

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: 314.74  E-value: 1.91e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  479 LSETSGVVFPNLPTLDCYLKHWAAQEitQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRV 555
Cdd:NF038339     6 LDENGNIRFPDGATLVDHVERNARER--ADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  556 LLVHVPGLDFIDAFFGCLRAKVIPIPVLPPD-PLQRGgqaltKIENIAKLCNAVAILSTVGYHAAVRAgLVKNLISFTGK 634
Cdd:NF038339    80 AILAPQGLDYVVSFFAAIYAGNIAVPLFDPDePGHTD-----RLHAVLGDCKPSAILTATSSAEGVRK-FFRSLPAKERP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  635 SVKSTGQWPnlpwlhtDSwIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS 714
Cdd:NF038339   154 RVIAVDAVP-------DS-VGSTWVRPDADL--------DDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  715 NTVLVSWLPQYHDMGLIGGLFTAMacGGSAILF-SPLTFIRNPLMW---LQTISDYKATHSAGPNFAFELVIRR-LEADk 789
Cdd:NF038339   218 NSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARgLPKE- 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  790 akARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDW----QGRI 863
Cdd:NF038339   295 --GEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReelnAGRI 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  864 --------------CCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY--- 926
Cdd:NF038339   373 vevdpdapnavaqvSCGYVARSQWAV---IVDPETGTEL-PDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLKSRlee 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  927 --------PGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV-----PEEVL 993
Cdd:NF038339   449 gshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVpanqlPAEVF 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  994 SAKGISL---PDASDEvGLVVIAElR---DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLK 1067
Cdd:NF038339   529 ENSHSGLkydADDSSE-QLVIVAE-RapgAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACKA 606

                   ....*..
gi 1917948728 1068 QFVDGNL 1074
Cdd:NF038339   607 AYIDGTL 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
522-1076 5.54e-86

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: 289.79  E-value: 5.54e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENI 601
Cdd:COG0318     22 GRRLTYAELDARARRLAAAL---RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE-------LAYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpddlCFLQF 681
Cdd:COG0318     92 LEDSGARALVT----------------------------------------------------------------ALILY 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTfirnplm 758
Cdd:COG0318    108 TSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLlprFDPER------- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 WLQTISDYKATHSAG-PNFAFELvirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYG 837
Cdd:COG0318    181 VLELIERERVTVLFGvPTMLARL------LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYG 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAENCVFVSCAygkkkPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:COG0318    249 LTETSPVVTVN-----PEDPGERRPGSVGRPLPG---VEVRIVDED-GREL-PPGEVGEIVVRGPNVMKGYWNDPEATAE 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  918 TFRNklqnypGrkYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLsak 996
Cdd:COG0318    319 AFRD------G--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKW--- 384
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  997 gislpdasDEVGLVVIAELRDSKLVNKDIIKQIESRVAeEHGVtvasvklirPRTIS------KTTSGKIKRFECLKQFV 1070
Cdd:COG0318    385 --------GERVVAFVVLRPGAELDAEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGKIDRRALRERYA 446

                   ....*.
gi 1917948728 1071 DGNLNT 1076
Cdd:COG0318    447 AGALEA 452
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
550-1071 1.74e-85

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: 293.87  E-value: 1.74e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  550 KPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLppDPLQRG-GQALTkieniAKL--CNAVAILSTVGYHAAVRAGLvk 626
Cdd:NF040633    84 KPGDRVAILANNSPEYIFGFLGALYAGMVPVPLY--DPNEPGhADHLR-----AVLadSGPTVVLTNKTSAPAVRAHF-- 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  627 nlisftgkSVKSTGQWP------NLPWLHTDSWIKSSKVLPASNIAFQSESQP-DDLCFLQFTSGSTSDAKGVMITHGGL 699
Cdd:NF040633   155 --------ADLPAAERPrilsvdSLPDSLAESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSI 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  700 IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGSAILFSPLTFIRNPLMWLQTIS---DYKATHSAGPNF 776
Cdd:NF040633   227 VTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNF 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  777 AFELVIRRleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPiL 856
Cdd:NF040633   306 ALELAARY--ANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERP-L 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  857 VDWQGR--ICCGYVDPNDADVD----------------IRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKT 918
Cdd:NF040633   383 FTYFDReaLAEGRAVEVAEDSEnavpfasngqvvrpqvLAIVDPETGQEL-PDGTVGEIWVHGDNMAAGYLDREEETAET 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  919 FRNKL----------QNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV 988
Cdd:NF040633   462 FRNTLgerlaensraEGAPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAV 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  989 PeevlsakgislpdASDEVGLVVIAELRDSKLVNKD--IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECL 1066
Cdd:NF040633   542 P-------------GDDVEKLVILAERDDEADESGDaeAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNA 608

                   ....*
gi 1917948728 1067 KQFVD 1071
Cdd:NF040633   609 KAYLE 613
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
526-1069 2.34e-76

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 266.36  E-value: 2.34e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltSRKPTIkpGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPlqrgGQALTKIENIAKLC 605
Cdd:NF038337    40 TWAQLYRRTLNVAHEV--RRHGTT--GDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSVPQP----GSHDERVSAVLADT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVraglvknlisftGKSVKSTGQWPNLPWLHTDSWiksskVLPASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:NF038337   112 SPSVVLTTSAAAAAV------------AEYLHRPDTGAVPAVIEIDSL-----DLDGPNSPSIRISDAPSIAYLQYTSGS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSN------TVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMW 759
Cdd:NF038337   175 TRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARW 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  760 LQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGL 838
Cdd:NF038337   255 IHAMANGSPVFSAAPNFAFELAVRKTtDADLA---GLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGL 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  839 AENCVFVSCAYGKKKPILVDWQ-GRICCGYVDPNDADVD-------------IRIVDADTGLEVdEDGKEGEIWISSPSA 904
Cdd:NF038337   332 AEATVYVASRAEGGAPEVVHFEpEKLSEGSAQRCEARTGspllsygtptsptVRIVDPDTCIEC-PAGTVGEIWVHGDNV 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  905 GIGYWGKEELSQKTFRNKLQN----YPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESsselLRP 980
Cdd:NF038337   411 AEGYWQKPEETRRTFGGVLANpspgTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQE----ITG 486
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  981 GCCAVIGVPeevlsakgislpdaSDEV-GLVVIAELR-----DSKLVNK-DIIK-QIESRVAEEHGVTVASVKLIRPRTI 1052
Cdd:NF038337   487 GRVAAISVP--------------VDETeKLVTIIELKkrgdsDEEAMRKlDAVKnNVTAAISRSHGLNVADLVLVPPGSI 552
                          570
                   ....*....|....*..
gi 1917948728 1053 SKTTSGKIKRFECLKQF 1069
Cdd:NF038337   553 PTTTSGKIRRAACVEQY 569
AMP-binding pfam00501
AMP-binding enzyme;
526-958 1.99e-69

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 240.68  E-value: 1.99e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHkLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:pfam00501   23 TYRELDERANRLAA-GLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE-------LAYILEDS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDSWIKSSKVLPASNIafqsesQPDDLCFLQFTSGS 685
Cdd:pfam00501   93 GAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP------DPDDLAYIIYTSGT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRS----TSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFiRNPLMWLQ 761
Cdd:pfam00501  167 TGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  762 TISDYKATHSAGPNFAFELVirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAPGYGLAEN 841
Cdd:pfam00501  246 LIERYKVTVLYGVPTLLNML-----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALVNGYGLTET 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  842 CVFVSCAYgkkkPILVDWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN 921
Cdd:pfam00501  315 TGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAFDE 386
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1917948728  922 KlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVA 958
Cdd:pfam00501  387 D-------GWYRTGDLGrRDEDGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
526-951 1.27e-32

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: 132.77  E-value: 1.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKL 604
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKAGAAYVPLDPAYPAER-------LAFILED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGyHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLhtdswiksskvlpasniafQSESQPDDLCFLQFTSG 684
Cdd:TIGR01733   71 AGARLLLTDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------DAPSGPDDLAYVIYTSG 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMACGGSAILFSPLTFIRNPLMWLQTIS 764
Cdd:TIGR01733  131 STGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIA 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  765 DYKATHSAGPNFAFELVirrleadkAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAENCVF 844
Cdd:TIGR01733  210 EHPVTVLNLTPSLLALL--------AAALPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTVW 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  845 VSCAYgkKKPILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN--K 922
Cdd:TIGR01733  277 STATL--VDPDDAPRESPVPIGRPLAN---TRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPdpF 349
                          410       420       430
                   ....*....|....*....|....*....|
gi 1917948728  923 LQNYPGRKYtRTGDLG-WVIQGNLFITGRI 951
Cdd:TIGR01733  350 AGGDGARLY-RTGDLVrYLPDGNLEFLGRI 378
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
1269-1702 9.70e-27

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: 119.09  E-value: 9.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1269 GLPWLHQAsvvlLAPLSWILCIALTSISIAFFGNSFLRINYA------LTPEV-SVWSVDFVKWWALYKAQEVSSKVLav 1341
Cdd:TIGR02353   24 GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPIWGSTYLRFWTVKRLVDAAPTVL-- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1342 hLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHEVRNSILRLQPIRIGRNCSVGPYAV 1419
Cdd:TIGR02353   98 -LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFIGTRST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1420 VQKGSVLREGAEVPALQKSEGGKS-----------ALKMAKAENILK-VSPGTL-KTVQQFMGIYVVGFLsslsaatvyl 1486
Cdd:TIGR02353  175 LDIDTSIGDGAQLGHGSALQGGQSipdgerwhgspAQKTGADYRKVQpARPYTVrRRLYVAGALFVVFVL---------- 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1487 lymslsqkvpsLELLAFLCISGAlhwvpFTIVAYATMFTKAPPNPFEFAISLAIAYFAHGLVLSLLTSIFTHLLAG---K 1563
Cdd:TIGR02353  245 -----------LPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNlvlK 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1564 EKKTQTHikTWFGHQL----AIACHVRFAKLLSG-TEAFCMYLRLLGAKVGRYCSIRAINpIADPRMVSIGAGVHLGDFS 1638
Cdd:TIGR02353  309 PGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGL 385
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1639 RIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:TIGR02353  386 LMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 2.16e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.56  E-value: 2.16e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
19-264 4.85e-14

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 76.88  E-value: 4.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   97 LEEM-DLHKLALIDsFTGEYHDIN-VAEDYMSLVSLTLEIQDKAKDSnhIGIHAVSDIASDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAA--LDPWAHPAAELDRESlaEWLRRNGASPSARR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMSLWKKISKSLLIKVCCNTEVQAVRRDGSDVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234
                          250
                   ....*....|....*....
gi 1917948728  246 DITNssGETEHkeFDKIII 264
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV 249
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
22-94 9.47e-14

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: 76.02  E-value: 9.47e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
32-264 5.06e-10

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: 64.43  E-value: 5.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   32 SGLSAAYALAKLGyRDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLaANSAPVIFHLAKESGTELEE--MDLHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGLEDRLvlPDPAPFYTVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  110 SFTGEYHDINVAEDYMSLVSL-----TLEIQDKAK---DSNHIGIHAVSDIASDLTPAYLEAHGIKSVPKSVQYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRlglAALASDALDEFDLDDFSLAESLLFLGRRGPGDVEVWDRLIDP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRMKGGYMSLWKKISKSLL---IKVccNTEVQAVRRDGSD 242
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRL--NTRVRSIDREGDG 236
                          250       260
                   ....*....|....*....|..
gi 1917948728  243 VNVDITNSsgetEHKEFDKIII 264
Cdd:pfam01593  237 VTVTLTDG----EVIEADAVIV 254
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1124-1185 7.23e-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: 7.23e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1124 EFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1185
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK07233 PRK07233
hypothetical protein; Provisional
23-68 6.59e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 60.67  E-value: 6.59e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEG 68
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGG 45
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1605-1686 8.84e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 53.34  E-value: 8.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRAINPIADPRMVSIGAGVHLGDFSRIITGFY-----SQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDV 1679
Cdd:COG0110     27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGA 106

                   ....*..
gi 1917948728 1680 ILGAISV 1686
Cdd:COG0110    107 VVGAGSV 113
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1118-1194 1.08e-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: 51.01  E-value: 1.08e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 1118 SNRNIVEFLKQLISEQTGISIQNISATESLVS-YGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLL 1194
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
1605-1702 1.29e-06

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: 50.10  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRA-INPIadprmvSIGAGVHLGDFSrIITGFYSQSGYIQGNV-----------DIKDNSVTGSQSLILPG 1672
Cdd:cd04645     23 GSSVWFGAVLRGdVNPI------RIGERTNIQDGS-VLHVDPGYPTIIGDNVtvghgavlhgcTIGDNCLIGMGAIILDG 95
                           90       100       110
                   ....*....|....*....|....*....|
gi 1917948728 1673 SVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:cd04645     96 AVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
22-96 5.91e-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: 51.38  E-value: 5.91e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYR---DITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLGLE 79
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1354-1432 4.69e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.57  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1354 EMLGARIGSSVLLDTVDITDPSLVSIGDGAV------------------IAEGALLQSH-EVRNSIL----------RLQ 1404
Cdd:PRK14356   241 ELLRARIVEKHLESGVLIHAPESVRIGPRATiepgaeiygpceiygasrIARGAVIHSHcWLRDAVVssgatihsfsHLE 320
                           90       100
                   ....*....|....*....|....*...
gi 1917948728 1405 PIRIGRNCSVGPYAVVQKGSVLREGAEV 1432
Cdd:PRK14356   321 GAEVGDGCSVGPYARLRPGAVLEEGARV 348
PRK06753 PRK06753
hypothetical protein; Provisional
23-178 2.12e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 46.22  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKH---KSVG---GMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKESGTE 96
Cdd:PRK06753     2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNesvKEVGagiGIGDNVIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   97 LEEM---------DLHKLALIDSFTGEYHDinvaedymSLVSLTLEIQDKAKDSNHIGIHaVSDIASDLTPAYLEAHGIK 167
Cdd:PRK06753    81 LNKVklksntlnvTLHRQTLIDIIKSYVKE--------DAIFTGKEVTKIENETDKVTIH-FADGESEAFDLCIGADGIH 151
                          170
                   ....*....|....*....
gi 1917948728  168 SV------PKS-VQY-GYT 178
Cdd:PRK06753   152 SKvrqsvnADSkVRYqGYT 170
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
2103-2302 3.00e-04

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: 46.28  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2103 LQTIVPYFLLGLIIY---FPLNLLLHCknarnMPVhwtfpFFWVSTGILAalTCAAAKYILVGKKKEdETVHIWsrGVFM 2179
Cdd:TIGR02353   16 LQWLAPLLGYNWLYEaldDVSWLYLRA-----VAL-----VFAVPVGRLG--FAIAAKWLLVGRWKP-GTYPIW--GSTY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2180 DTIWQAIRTV--FGDYFVemtSGSALFLMWMKLMGssVELDKGTYVDSMGAALNpEMVEVEGGGSVEREALLFGhvYDGE 2257
Cdd:TIGR02353   81 LRFWTVKRLVdaAPTVLL---SGSPLYSLYLRALG--AKIGKGVDIGSLPPVCT-DLLTIGAGTIVRKEVMLLG--YRAE 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1917948728 2258 GGAVKFGKIVVGEGGFVGSRAVAMPG--VESGGSLSALSLAMKGEAI 2302
Cdd:TIGR02353  153 RGRLHTGPVTLGRDAFIGTRSTLDIDtsIGDGAQLGHGSALQGGQSI 199
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
499-1071 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: 611.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  499 HWAAQeiTQNKALYTWINEGGAVGCQRTYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVI 578
Cdd:cd05931      1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  579 PIPVLPPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVknlisftgksvkSTGQWPNLPWLHTDSWikssk 658
Cdd:cd05931     75 AVPLPPPTP----GRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVDLL----- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  659 VLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAM 738
Cdd:cd05931    134 PDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPL 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  739 ACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd05931    214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRD--EDLEGLDLSSWRVALNGAEPVRPATLRRF 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  819 VELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPILV-------------------DWQGRICCGYVDPndaDVDIRI 879
Cdd:cd05931    292 AEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQEVRI 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  880 VDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnKLQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAG 959
Cdd:cd05931    369 VDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFG-ALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRG 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  960 RNIYSADVEKTVESSSELLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAEL--RDSKLVNKDIIKQIESRVAEEH 1037
Cdd:cd05931    447 RNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREH 513
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1917948728 1038 GVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1071
Cdd:cd05931    514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
1720-2046 6.70e-125

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: 396.80  E-value: 6.70e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1720 EEMDPKYKKIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHDIFGPGKRYTVIVRHSNSLSADDDARL 1799
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1800 DARGAALRILS---DDSPLLDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSFADLHY 1874
Cdd:cd08151     80 DGRGAALRFLNagdDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1875 YSNTCRLFRFKDRQEMYVKFKLRPSDENIEEDIGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFHNRVKSPsGVRYIF 1954
Cdd:cd08151    160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1955 QLQVRPIPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSEKLEVNPfLRCHEVDVIRATSSSQ-SASIDHG 2033
Cdd:cd08151    239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315
                          330
                   ....*....|...
gi 1917948728 2034 RSLIYEICQHLRN 2046
Cdd:cd08151    316 RSLVYEISQRLRK 328
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
487-1079 3.51e-96

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 325.92  E-value: 3.51e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  487 FPNLPTLDCYLKHWAaqEITQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRVLLVHVPGL 563
Cdd:PRK07769    17 FPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQNL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  564 DFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHAAVRAgLVKNLISFTGKSVKSTGQWP 643
Cdd:PRK07769    91 DYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDD----CTPSAILTTTDSAEGVRK-FFRARPAKERPRVIAVDAVP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  644 NLpwlhtdswIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLP 723
Cdd:PRK07769   166 DE--------VGATWVPPEANE--------DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  724 QYHDMGLIGGLFTAMaCGGSAILFSPLTFIRNPLMWLQTIS----DYKATHSAGPNFAFELVIRRlEADKAKARNYDLSS 799
Cdd:PRK07769   230 FFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFEHAAAR-GLPKDGEPPLDLSN 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  800 MIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDWQ----GRIC--------- 864
Cdd:PRK07769   308 VKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRFVevpadapna 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  865 -----CGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY----------PGR 929
Cdd:PRK07769   388 vaqvsAGKVGVSEWAV---IVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaegapDDA 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  930 KYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPEEVLSAK-------GISL-P 1001
Cdd:PRK07769   464 LWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVvfddshaGLKFdP 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1002 DASDEvGLVVIAELR--DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNL----- 1074
Cdd:PRK07769   544 EDTSE-QLVIVAERApgAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLrsgyg 622

                   ....*.
gi 1917948728 1075 -NTVPD 1079
Cdd:PRK07769   623 qPAFPD 628
PRK05850 PRK05850
acyl-CoA synthetase; Validated
526-1069 7.82e-95

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 319.97  E-value: 7.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPdplqRGGQALTKIENIAKLC 605
Cdd:PRK05850    37 TWSQLYRRTLNVAEELRRHGST----GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVP----QGGAHDERVSAVLRDT 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTvgyhAAVRAGLVKNLISFTGKSVKSTGQwpnLPWLHTDSWIKS-SKVLPASNIAFqsesqpddlcfLQFTSG 684
Cdd:PRK05850   109 SPSVVLTT----SAVVDDVTEYVAPQPGQSAPPVIE---VDLLDLDSPRGSdARPRDLPSTAY-----------LQYTSG 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNV-KLMRRRYRST-----SNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLM 758
Cdd:PRK05850   171 STRTPAGVMVSHRNVIANFeQLMSDYFGDTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPAR 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 WLQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYG 837
Cdd:PRK05850   251 WMQLLASNPHAFSAAPNFAFELAVRKTsDDDMA---GLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYG 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAENCVFVSCAYGKKKPILVDW--------QGRIC--------CGYVDPNDADVdiRIVDADTGLEVdEDGKEGEIWISS 901
Cdd:PRK05850   328 LAEATVYVATREPGQPPESVRFdyeklsagHAKRCetgggtplVSYGSPRSPTV--RIVDPDTCIEC-PAGTVGEIWVHG 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  902 PSAGIGYWGKEELSQKTFRNKLQN----YPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssEL 977
Cdd:PRK05850   405 DNVAAGYWQKPEETERTFGATLVDpspgTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQ---EI 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  978 LRpGCCAVIGVPEevlsakgislpDASDEvgLVVIAELR------DSKLVNKDIIK-QIESRVAEEHGVTVASVKLIRPR 1050
Cdd:PRK05850   482 TG-GRVAAISVPD-----------DGTEK--LVAIIELKkrgdsdEEAMDRLRTVKrEVTSAISKSHGLSVADLVLVAPG 547
                          570
                   ....*....|....*....
gi 1917948728 1051 TISKTTSGKIKRFECLKQF 1069
Cdd:PRK05850   548 SIPITTSGKIRRAACVEQY 566
PRK05691 PRK05691
peptide synthase; Validated
507-1200 1.42e-92

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 337.53  E-value: 1.42e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  507 QNKALYT-------WINEGGAVGCQRTYAELDSNASCVAHKLLTSrkptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIP 579
Cdd:PRK05691    16 QRRAAQTpdrlalrFLADDPGEGVVLSYRDLDLRARTIAAALQAR----ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  580 IPVLPPDPLQRGGQAltkieniaKLCNAVA-----ILSTVgyhaavrAGLVKNLISFtgksvkSTGQWPNLP-WLHTDSw 653
Cdd:PRK05691    92 VPAYPPESARRHHQE--------RLLSIIAdaeprLLLTV-------ADLRDSLLQM------EELAAANAPeLLCVDT- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  654 iksskVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYHDMGL 730
Cdd:PRK05691   150 -----LDPALAEAWQEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddVIVSWLPLYHDMGL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  731 IGGLFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLeADKAKARnYDLSSMIFFMIAAEPV 810
Cdd:PRK05691   225 IGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERV-SESALER-LDLSRWRVAYSGSEPI 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  811 RQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAY-GKKKPIL-VDWQG-------------RICCGYVDPNDAdv 875
Cdd:PRK05691   303 RQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRrGQGIPALeLDAEAlarnraepgtgsvLMSCGRSQPGHA-- 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  876 dIRIVDADTgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLI 955
Cdd:PRK05691   381 -VLIVDPQS-LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGRTWLRTGDLGFLRDGELFVTGRLKDML 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  956 IVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPEEVLSAKGISLpDASDEVGLVVIAElrdsklvnkDIIKQIESRVAE 1035
Cdd:PRK05691   455 IVRGHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAA-EISRSVQKILPPQ---------ALIKSIRQAVAE 524
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1036 EHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNLntvpDPIVTKRSLTrsfttgtcregktprSHLAKSSLAPSP 1115
Cdd:PRK05691   525 ACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----DSYALFPALQ---------------AVEAAQTAASGD 585
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1116 KLSNRNIVEFLKQLISEQtgisiqnISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLLM 1195
Cdd:PRK05691   586 ELQARIAAIWCEQLKVEQ-------VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLA 658

                   ....*
gi 1917948728 1196 KSQPH 1200
Cdd:PRK05691   659 GGGAA 663
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
479-1074 1.91e-92

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: 314.74  E-value: 1.91e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  479 LSETSGVVFPNLPTLDCYLKHWAAQEitQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRV 555
Cdd:NF038339     6 LDENGNIRFPDGATLVDHVERNARER--ADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  556 LLVHVPGLDFIDAFFGCLRAKVIPIPVLPPD-PLQRGgqaltKIENIAKLCNAVAILSTVGYHAAVRAgLVKNLISFTGK 634
Cdd:NF038339    80 AILAPQGLDYVVSFFAAIYAGNIAVPLFDPDePGHTD-----RLHAVLGDCKPSAILTATSSAEGVRK-FFRSLPAKERP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  635 SVKSTGQWPnlpwlhtDSwIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS 714
Cdd:NF038339   154 RVIAVDAVP-------DS-VGSTWVRPDADL--------DDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  715 NTVLVSWLPQYHDMGLIGGLFTAMacGGSAILF-SPLTFIRNPLMW---LQTISDYKATHSAGPNFAFELVIRR-LEADk 789
Cdd:NF038339   218 NSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARgLPKE- 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  790 akARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDW----QGRI 863
Cdd:NF038339   295 --GEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReelnAGRI 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  864 --------------CCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY--- 926
Cdd:NF038339   373 vevdpdapnavaqvSCGYVARSQWAV---IVDPETGTEL-PDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLKSRlee 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  927 --------PGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV-----PEEVL 993
Cdd:NF038339   449 gshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVpanqlPAEVF 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  994 SAKGISL---PDASDEvGLVVIAElR---DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLK 1067
Cdd:NF038339   529 ENSHSGLkydADDSSE-QLVIVAE-RapgAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACKA 606

                   ....*..
gi 1917948728 1068 QFVDGNL 1074
Cdd:NF038339   607 AYIDGTL 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
522-1076 5.54e-86

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: 289.79  E-value: 5.54e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENI 601
Cdd:COG0318     22 GRRLTYAELDARARRLAAAL---RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE-------LAYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpddlCFLQF 681
Cdd:COG0318     92 LEDSGARALVT----------------------------------------------------------------ALILY 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTfirnplm 758
Cdd:COG0318    108 TSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLlprFDPER------- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 WLQTISDYKATHSAG-PNFAFELvirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYG 837
Cdd:COG0318    181 VLELIERERVTVLFGvPTMLARL------LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYG 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAENCVFVSCAygkkkPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:COG0318    249 LTETSPVVTVN-----PEDPGERRPGSVGRPLPG---VEVRIVDED-GREL-PPGEVGEIVVRGPNVMKGYWNDPEATAE 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  918 TFRNklqnypGrkYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLsak 996
Cdd:COG0318    319 AFRD------G--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKW--- 384
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  997 gislpdasDEVGLVVIAELRDSKLVNKDIIKQIESRVAeEHGVtvasvklirPRTIS------KTTSGKIKRFECLKQFV 1070
Cdd:COG0318    385 --------GERVVAFVVLRPGAELDAEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGKIDRRALRERYA 446

                   ....*.
gi 1917948728 1071 DGNLNT 1076
Cdd:COG0318    447 AGALEA 452
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
550-1071 1.74e-85

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: 293.87  E-value: 1.74e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  550 KPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLppDPLQRG-GQALTkieniAKL--CNAVAILSTVGYHAAVRAGLvk 626
Cdd:NF040633    84 KPGDRVAILANNSPEYIFGFLGALYAGMVPVPLY--DPNEPGhADHLR-----AVLadSGPTVVLTNKTSAPAVRAHF-- 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  627 nlisftgkSVKSTGQWP------NLPWLHTDSWIKSSKVLPASNIAFQSESQP-DDLCFLQFTSGSTSDAKGVMITHGGL 699
Cdd:NF040633   155 --------ADLPAAERPrilsvdSLPDSLAESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSI 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  700 IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGSAILFSPLTFIRNPLMWLQTIS---DYKATHSAGPNF 776
Cdd:NF040633   227 VTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNF 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  777 AFELVIRRleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPiL 856
Cdd:NF040633   306 ALELAARY--ANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERP-L 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  857 VDWQGR--ICCGYVDPNDADVD----------------IRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKT 918
Cdd:NF040633   383 FTYFDReaLAEGRAVEVAEDSEnavpfasngqvvrpqvLAIVDPETGQEL-PDGTVGEIWVHGDNMAAGYLDREEETAET 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  919 FRNKL----------QNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV 988
Cdd:NF040633   462 FRNTLgerlaensraEGAPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAV 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  989 PeevlsakgislpdASDEVGLVVIAELRDSKLVNKD--IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECL 1066
Cdd:NF040633   542 P-------------GDDVEKLVILAERDDEADESGDaeAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNA 608

                   ....*
gi 1917948728 1067 KQFVD 1071
Cdd:NF040633   609 KAYLE 613
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
479-1074 1.68e-82

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 285.10  E-value: 1.68e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  479 LSETSGVVFPNLPTLDCYLKHWAAqeITQNKALYTWIN-EGGAVGC--QRTYAELDSNASCVAHKLltsrKPTIKPGDRV 555
Cdd:PRK12476    22 LDADGNIALPPGTTLISLIERNIA--NVGDTVAYRYLDhSHSAAGCavELTWTQLGVRLRAVGARL----QQVAGPGDRV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  556 LLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDpLQrgGQAlTKIENIAKLCNAVAILSTVGYHAAVRAGLVKnlisftgks 635
Cdd:PRK12476    96 AILAPQGIDYVAGFFAAIKAGTIAVPLFAPE-LP--GHA-ERLDTALRDAEPTVVLTTTAAAEAVEGFLRN--------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  636 vkstgqwpnLPWLHTDSWIKSSKVLPASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGG-------LIHNVKLMR 707
Cdd:PRK12476   163 ---------LPRLRRPRVIAIDAIPDSAGESFVpVELDTDDVSHLQYTSGSTRPPVGVEITHRAvgtnlvqMILSIDLLD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  708 RryrstsNTVLVSWLPQYHDMGLIGGLFTAMaCGGSAILFSPLTFIRNPLMWLQTISD---YKATHSAGPNFAFELVIRR 784
Cdd:PRK12476   234 R------NTHGVSWLPLYHDMGLSMIGFPAV-YGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVTAAPNFAYEWAAQR 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  785 -LEADKAkarNYDLSSMIfFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDWQ- 860
Cdd:PRK12476   307 gLPAEGD---DIDLSNVV-LIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPsvVYLDREq 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  861 ---GR--------------ICCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKL 923
Cdd:PRK12476   383 lgaGRavrvaadapnavahVSCGQVARSQWAV---IVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKL 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  924 QNY-----------PGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPeev 992
Cdd:PRK12476   459 QSRlaegshadgaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVP--- 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  993 lsakgislpdASDEVGLVVIAElRDSKLVNKD---IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQF 1069
Cdd:PRK12476   536 ----------AEDNERLVIVAE-RAAGTSRADpapAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQY 604

                   ....*
gi 1917948728 1070 VDGNL 1074
Cdd:PRK12476   605 LDGRL 609
PRK09192 PRK09192
fatty acyl-AMP ligase;
527-1072 1.23e-81

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 281.51  E-value: 1.23e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  527 YAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlpPDPLQRGGQA--LTKIENIAKL 604
Cdd:PRK09192    52 YQTLRARAEAGARRLLAL---GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMGFGGREsyIAQLRGMLAS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGyhaavraglvknLISFTGKSVKSTgqwpNLPWLHTDSWIKSskvLPASNIAFQsESQPDDLCFLQFTSG 684
Cdd:PRK09192   127 AQPAAIITPDE------------LLPWVNEATHGN----PLLHVLSHAWFKA---LPEADVALP-RPTPDDIAYLQYSSG 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNVK-------LMRRRYRStsntvlVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPL 757
Cdd:PRK09192   187 STRFPRGVIITHRALMANLRaishdglKVRPGDRC------VSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 MWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGY 836
Cdd:PRK09192   261 QWLDLISRNRGTISYSPPFGYELCARRVnSKDLA---ELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSY 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  837 GLAENCVFVSCA----------------YGKKKPILVDWQGR-----ICCGYVDPnDADVDIRivdadtglevDEDGKE- 894
Cdd:PRK09192   338 GLAEATLAVSFSplgsgivveevdrdrlEYQGKAVAPGAETRrvrtfVNCGKALP-GHEIEIR----------NEAGMPl 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 -----GEIWISSPSAGIGYWGKEElSQKTFR--NKLQnypgrkytrTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADV 967
Cdd:PRK09192   407 pervvGHICVRGPSLMSGYFRDEE-SQDVLAadGWLD---------TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDI 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  968 EKTVESSSElLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAELRDSKLVNK-DIIKQIESRVAEEHGVTVaSVKL 1046
Cdd:PRK09192   477 EWIAEQEPE-LRSGDAAAFSIAQE-------------NGEKIVLLVQCRISDEERRgQLIHALAALVRSEFGVEA-AVEL 541
                          570       580
                   ....*....|....*....|....*.
gi 1917948728 1047 IRPRTISKTTSGKIKRFECLKQFVDG 1072
Cdd:PRK09192   542 VPPHSLPRTSSGKLSRAKAKKRYLSG 567
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
525-1072 1.69e-76

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: 265.30  E-value: 1.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIENIAKL 604
Cdd:cd05906     40 QSYQDLLEDARRLAAGL---RQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGYHAAVRaglvknlisftgksvKSTGQWPNLPWlhTDSWIKSSKVLPASNIAFQSesQPDDLCFLQFTSG 684
Cdd:cd05906    117 LGSPVVLTDAELVAEFA---------------GLETLSGLPGI--RVLSIEELLDTAADHDLPQS--RPDDLALLMLTSG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMWLQTIS 764
Cdd:cd05906    178 STGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLID 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  765 DYKATHSAGPNFAFELVIRRLEADKAkaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENC-- 842
Cdd:cd05906    258 RYRVTITWAPNFAFALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCsg 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  843 --VFVSCAYGKKKPILVdwqgRICCGYVDPNdadVDIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd05906    336 viYSRSFPTYDHSQALE----FVSLGRPIPG---VSMRIVDDEGQLL--PEGEVGRLQVRGPVVTKGYYNNPEANAEAFT 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  921 NKlqnypgrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVigvpeevlsakgiSL 1000
Cdd:cd05906    407 ED-------GWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAF-------------AV 466
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1001 PDASDEVGLVVIAELRDSKLVNK--DIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDG 1072
Cdd:cd05906    467 RDPGAETEELAIFFVPEYDLQDAlsETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
526-1069 2.34e-76

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 266.36  E-value: 2.34e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltSRKPTIkpGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPlqrgGQALTKIENIAKLC 605
Cdd:NF038337    40 TWAQLYRRTLNVAHEV--RRHGTT--GDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSVPQP----GSHDERVSAVLADT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVraglvknlisftGKSVKSTGQWPNLPWLHTDSWiksskVLPASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:NF038337   112 SPSVVLTTSAAAAAV------------AEYLHRPDTGAVPAVIEIDSL-----DLDGPNSPSIRISDAPSIAYLQYTSGS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSN------TVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMW 759
Cdd:NF038337   175 TRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARW 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  760 LQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGL 838
Cdd:NF038337   255 IHAMANGSPVFSAAPNFAFELAVRKTtDADLA---GLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGL 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  839 AENCVFVSCAYGKKKPILVDWQ-GRICCGYVDPNDADVD-------------IRIVDADTGLEVdEDGKEGEIWISSPSA 904
Cdd:NF038337   332 AEATVYVASRAEGGAPEVVHFEpEKLSEGSAQRCEARTGspllsygtptsptVRIVDPDTCIEC-PAGTVGEIWVHGDNV 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  905 GIGYWGKEELSQKTFRNKLQN----YPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESsselLRP 980
Cdd:NF038337   411 AEGYWQKPEETRRTFGGVLANpspgTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQE----ITG 486
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  981 GCCAVIGVPeevlsakgislpdaSDEV-GLVVIAELR-----DSKLVNK-DIIK-QIESRVAEEHGVTVASVKLIRPRTI 1052
Cdd:NF038337   487 GRVAAISVP--------------VDETeKLVTIIELKkrgdsDEEAMRKlDAVKnNVTAAISRSHGLNVADLVLVPPGSI 552
                          570
                   ....*....|....*..
gi 1917948728 1053 SKTTSGKIKRFECLKQF 1069
Cdd:NF038337   553 PTTTSGKIRRAACVEQY 569
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
670-1062 1.84e-75

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 262.62  E-value: 1.84e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGGLFTAMACGGSAILFS 748
Cdd:PRK07768   148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVT 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  749 PLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLS 828
Cdd:PRK07768   228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRR-QAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLR 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  829 QEVMAPGYGLAENCVFVSCAygkkkpilvdwqgRICCGY-VDPNDADV---DIRIVDAD--------------TGLE--- 887
Cdd:PRK07768   307 PEAILPAYGMAEATLAVSFS-------------PCGAGLvVDEVDADLlaaLRRAVPATkgntrrlatlgpplPGLEvrv 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  888 VDEDGKE------GEIWISSPSAGIGYwgkeeLSQKTFRnKLQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGR 960
Cdd:PRK07768   374 VDEDGQVlpprgvGVIELRGESVTPGY-----LTMDGFI-PAQDADG--WLDTGDLGYLTEeGEVVVCGRVKDVIIMAGR 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  961 NIYSADVEKTVeSSSELLRPGCCAVIGVPeevlsakgisLPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVT 1040
Cdd:PRK07768   446 NIYPTDIERAA-ARVEGVRPGNAVAVRLD----------AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVR 514
                          410       420
                   ....*....|....*....|..
gi 1917948728 1041 VASVKLIRPRTISKTTSGKIKR 1062
Cdd:PRK07768   515 PRNVVVLGPGSIPKTPSGKLRR 536
AMP-binding pfam00501
AMP-binding enzyme;
526-958 1.99e-69

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 240.68  E-value: 1.99e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHkLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:pfam00501   23 TYRELDERANRLAA-GLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE-------LAYILEDS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDSWIKSSKVLPASNIafqsesQPDDLCFLQFTSGS 685
Cdd:pfam00501   93 GAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP------DPDDLAYIIYTSGT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRS----TSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFiRNPLMWLQ 761
Cdd:pfam00501  167 TGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  762 TISDYKATHSAGPNFAFELVirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAPGYGLAEN 841
Cdd:pfam00501  246 LIERYKVTVLYGVPTLLNML-----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALVNGYGLTET 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  842 CVFVSCAYgkkkPILVDWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN 921
Cdd:pfam00501  315 TGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAFDE 386
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1917948728  922 KlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVA 958
Cdd:pfam00501  387 D-------GWYRTGDLGrRDEDGYLEIVGRKKDQIKLG 417
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
675-1061 8.71e-65

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: 224.47  E-value: 8.71e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdMGLIGGLFTAMACGGSAILFSPltfiR 754
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPK----F 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAP 834
Cdd:cd04433     76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAG-----YDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVN 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLevDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd04433    145 GYGLTETGGTVATGPPDDDARKPGSVGRPV--------PGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGYWNNPEA 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  915 SQKTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevl 993
Cdd:cd04433    215 TAAVDED--------GWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPD--- 280
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728  994 sakgislPDASDEVGLVViaELRDSKLVNKDIIKQIesrVAEEHGVTVASVKLIRPRTISKTTSGKIK 1061
Cdd:cd04433    281 -------PEWGERVVAVV--VLRPGADLDAEELRAH---VRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
526-1072 2.76e-62

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: 222.75  E-value: 2.76e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlPPDPLQRGGQALTKIENIAklc 605
Cdd:cd05908     17 SYRHLREEALGYLGAL---QELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV-SIGSNEEHKLKLNKVWNTL--- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhaavraglvknlisftgksvkstgqwpNLPWLhtdswIKSSKVLpasniafqsESQPDDLCFLQFTSGS 685
Cdd:cd05908     90 --------------------------------------KNPYL-----ITEEEVL---------CELADELAFIQFSSGS 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMWLQTISD 765
Cdd:cd05908    118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATHSAGPNFAFELVIRRLEADKAKarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFV 845
Cdd:cd05908    198 HKATIVSSPNFGYKYFLKTLKPEKAN--DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGA 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  846 SCA-----------------YGKKKPiLVDWQGRICCGYVDPNDA--DVDIRIVDADTglEVDEDGKEGEIWISSPSAGI 906
Cdd:cd05908    276 SLPkaqspfktitlgrrhvtHGEPEP-EVDKKDSECLTFVEVGKPidETDIRICDEDN--KILPDGYIGHIQIRGKNVTP 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  907 GYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellrpgccaVI 986
Cdd:cd05908    353 GYYNNPEATAKVFTDD-------GWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEE-----------LE 414
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  987 GVpeevlsakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVA-------------SVKLIRP-RTI 1052
Cdd:cd05908    415 GV-----------------ELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGkkikkhlnkrggwQINEVLPiRRI 477
                          570       580
                   ....*....|....*....|
gi 1917948728 1053 SKTTSGKIKRFECLKQFVDG 1072
Cdd:cd05908    478 PKTTSGKVKRYELAQRYQSG 497
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
511-1078 2.00e-55

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: 204.50  E-value: 2.00e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  511 LYTWINEGGAVGCQRTYAELDSNASCVAHKLLTsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQR 590
Cdd:cd05905      1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQK--KVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  591 GGQALTkIENIAKLCNAVAILstvgyhaavRAGLVKNLISFT-GKSVKSTGqWPNLPWLHTdswIKSSKVLPASNIAFQS 669
Cdd:cd05905     79 LGFLLG-TCKVRVALTVEACL---------KGLPKKLLKSKTaAEIAKKKG-WPKILDFVK---IPKSKRSKLKKWGPHP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSP 749
Cdd:cd05905    145 PTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPP 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  750 LTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKA--KARNYDLSSMIFFMIAAE-PVRQKTLKRFVELTRPFG 826
Cdd:cd05905    225 ELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLAslKNRDVNLSSLRMCMVPCEnRPRISSCDSFLKLFQTLG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  827 LSQEVMAPGYGlaenCVFVScaygkkkpiLVDWQG----RICCGYVDPN------------DA-------DVDIRIVDAD 883
Cdd:cd05905    305 LSPRAVSTEFG----TRVNP---------FICWQGtsgpEPSRVYLDMRalrhgvvrlderDKpnslplqDSGKVLPGAQ 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  884 TGLeVDEDGKE-------GEIWISSPSAGIGYWG--KEELSQKTFRNKLQNYPGRK---YTRTGDLGWVIQGN------- 944
Cdd:cd05905    372 VAI-VNPETKGlckdgeiGEIWVNSPANASGYFLldGETNDTFKVFPSTRLSTGITnnsYARTGLLGFLRPTKctdlnve 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  945 ----LFITGRIKDLIIVAGRNIYSADVEKTVEsSSELLRPGCCavigvpeeVLSAKGIslpdasdevgLVVIAELRD-SK 1019
Cdd:cd05905    451 ehdlLFVVGSIDETLEVRGLRHHPSDIEATVM-RVHPYRGRCA--------VFSITGL----------VVVVAEQPPgSE 511
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1020 LVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNLNTVP 1078
Cdd:cd05905    512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIY 570
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
527-1073 4.75e-50

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 187.28  E-value: 4.75e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  527 YAELDSNASCVAHKLLTSRKPTIkpgdrVLLVHVPGLDFIDAFFGCLRA----KVIPIPVLPPDPLQRGGQALTKIENIA 602
Cdd:PRK05851    34 WPEVHGRAENVAARLLDRDRPGA-----VGLVGEPTVELVAAIQGAWLAgaavSILPGPVRGADDGRWADATLTRFAGIG 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 klcnAVAILSTVGYHAAVRA---GLVKNLISFTGKSVKSTGQWPnlpwlhtdswiksskvLPASNIAFqsesqpddlcfL 679
Cdd:PRK05851   109 ----VRTVLSHGSHLERLRAvdsSVTVHDLATAAHTNRSASLTP----------------PDSGGPAV-----------L 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  680 QFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGgLFTAmACGGSAILFSPLT-FIRNPL 757
Cdd:PRK05851   158 QGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAF-LLTA-ALAGAPLWLAPTTaFSASPF 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 MWLQTISDYKATHSAGPNFAFELV---IRRLeadkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAP 834
Cdd:PRK05851   236 RWLSWLSDSRATLTAAPNFAYNLIgkyARRV-------SDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAP 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENcvfvSCAYGKKKP---------ILVDWQGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKeGEIWISSPSAG 905
Cdd:PRK05851   309 SYGLAES----TCAVTVPVPgiglrvdevTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAGREI-GEIEIRGASMM 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 IGYWGKEELSqktfrnklqnyPGrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKtVESSSELLRPGCCAV 985
Cdd:PRK05851   384 SGYLGQAPID-----------PD-DWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER-VAAQVRGVREGAVVA 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  986 IGVPEevlsakgislpdASDEVGLVVIAELR--DSKLVNKDIIKqiesRVAEEHGVTVASVKLIRPRTISKTTSGKIKRF 1063
Cdd:PRK05851   451 VGTGE------------GSARPGLVIAAEFRgpDEAGARSEVVQ----RVASECGVVPSDVVFVAPGSLPRTSSGKLRRL 514
                          570
                   ....*....|
gi 1917948728 1064 ECLKQFVDGN 1073
Cdd:PRK05851   515 AVKRSLEAAD 524
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
526-1062 2.65e-49

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: 183.53  E-value: 2.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGgqalTKIENIAKLC 605
Cdd:cd05936     26 TYRELDALAEAFAAGLQNL---GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL---NPLYTP----RELEHILNDS 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAGlvknlisftgksvKSTGQWPNLPwlhtdswiksskvlpasniafqsesqPDDLCFLQFTSGS 685
Cdd:cd05936     96 GAKALIVAVSFTDLLAAG-------------APLGERVALT--------------------------PEDVAVLQYTSGT 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRY--RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmwL 760
Cdd:cd05936    137 TGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLiprFRPIGV-------L 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevmAP---GYG 837
Cdd:cd05936    210 KEIRKHRVTIFPGVPTMYIALLNAPEFKK-----RDFSSLRLCISGGAPLPVEVAERFEELTG---------VPiveGYG 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAENCVFVSC--AYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd05936    276 LTETSPVVAVnpLDGPRKP-----------GSIGIPLPGTEVKIVDDD-GEEL-PPGEVGELWVRGPQVMKGYWNRPEET 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  916 QKTFRNklqnypGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPEev 992
Cdd:cd05936    343 AEAFVD------G--WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVL-----YEHPAVaeAAVVGVPD-- 407
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728  993 lsakgislPDASDEV-GLVVIAElrDSKLVNKDIIKQiesrvAEEHgvtVASVKliRPRTIS------KTTSGKIKR 1062
Cdd:cd05936    408 --------PYSGEAVkAFVVLKE--GASLTEEEIIAF-----CREQ---LAGYK--VPRQVEfrdelpKSAVGKILR 464
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
526-1060 5.17e-43

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: 165.46  E-value: 5.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVI--PI-PVLPPDPLQRggqaLTKIENiA 602
Cdd:cd05911     12 TYAQLRTLSRRLAAGL---RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIfsAAnPIYTADELAH----QLKISK-P 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 K-LCNAVAILSTVgYHAAVRAGLVKNLISFTGK--SVKSTGQWPNLPWLHTDSWIKSSKVLPasniafqsesqPDDLCFL 679
Cdd:cd05911     84 KvIFTDPDGLEKV-KEAAKELGPKDKIIVLDDKpdGVLSIEDLLSPTLGEEDEDLPPPLKDG-----------KDDTAAI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  680 QFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRST--SNTVLVSWLPQYHDMGLIgGLFTAMACGGSAIL---FSPLTFir 754
Cdd:cd05911    152 LYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLF-TTLASLLNGATVIImpkFDSELF-- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 nplmwLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVrqktLKRFVELTRPFGLSQEVMaP 834
Cdd:cd05911    229 -----LDLIEKYKITFLYLVPPIAAALAKSPLLDK-----YDLSSLRVILSGGAPL----SKELQELLAKRFPNATIK-Q 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENCVFVSCAygkkkPILVDWQGriCCGYVDPNdadVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd05911    294 GYGMTETGGILTVN-----PDGDDKPG--SVGRLLPN---VEAKIVDDDGK-DSLGPNEPGEICVRGPQVMKGYYNNPEA 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  915 SQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesssELLR--PGC--CAVIGVP 989
Cdd:cd05911    363 TKETFDED-------GWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELE-------AVLLehPGVadAAVIGIP 428
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728  990 EEVlsakgislpdaSDEV--GLVVIAElrDSKLVNKDIIKQIESRVAEEH----GVTVASvklirprTISKTTSGKI 1060
Cdd:cd05911    429 DEV-----------SGELprAYVVRKP--GEKLTEKEVKDYVAKKVASYKqlrgGVVFVD-------EIPKSASGKI 485
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
525-1060 4.41e-42

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: 161.62  E-value: 4.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTKIEN--IA 602
Cdd:cd17631     21 LTYAELDERVNRLAHAL---RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL---------NFRLTPPEVayIL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAILstvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpDDLCFLQFT 682
Cdd:cd17631     89 ADSGAKVLF--------------------------------------------------------------DDLALLMYT 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  683 SGSTSDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVswLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnpl 757
Cdd:cd17631    107 SGTTGRPKGAMLTHRNLLWNAvnALAALDLGPDDVLLVV--APLFHIGGLGVFTLPTLLRGGTVVIlrkFDPETV----- 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 mwLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVEltrpFGLsqeVMAPGYG 837
Cdd:cd17631    180 --LDLIERHRVTSFFLVPTMIQALLQHPRFAT-----TDLSSLRAVIYGGAPMPERLLRALQA----RGV---KFVQGYG 245
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAEnCVFVSCAYGKKkpilvDWQGRI-CCGYVDPNdadVDIRIVDADtGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd17631    246 MTE-TSPGVTFLSPE-----DHRRKLgSAGRPVFF---VEVRIVDPD-GREVP-PGEVGEIVVRGPHVMAGYWNRPEATA 314
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  917 KTFRNklqnypGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsa 995
Cdd:cd17631    315 AAFRD------G--WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAE---VAVIGVPDE---- 379
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728  996 KGIslpdasdEVGLVVIAELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTI------SKTTSGKI 1060
Cdd:cd17631    380 KWG-------EAVVAVVVPRPGAELDEDELIAHCRER--------LARYK--IPKSVefvdalPRNATGKI 433
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
510-1072 6.70e-41

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 161.05  E-value: 6.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  510 ALYtWINEGGAVGcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLvHVP-GLDFIDAFFGCLRAKVIPIPV---LPP 585
Cdd:COG0365     27 ALI-WEGEDGEER-TLTYAELRREVNRFANAL---RALGVKKGDRVAI-YLPnIPEAVIAMLACARIGAVHSPVfpgFGA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  586 DPLqrggqaLTKIENiaklCNAVAILSTVGYH------------AAVRAGL--VKNLISF--TGKSVkstgQWPNLPWLH 649
Cdd:COG0365    101 EAL------ADRIED----AEAKVLITADGGLrggkvidlkekvDEALEELpsLEHVIVVgrTGADV----PMEGDLDWD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  650 TdswiksskVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGG-LIHNVKLMRR--------RYRSTSNtvlV 719
Cdd:COG0365    167 E--------LLAAASAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYvldlkpgdVFWCTAD---I 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  720 SWLpqyhdMGLIGGLFTAMACGGSAILF--SPLTfiRNPLMWLQTISDYKATH-SAGPNFafelvIRRLE-ADKAKARNY 795
Cdd:COG0365    236 GWA-----TGHSYIVYGPLLNGATVVLYegRPDF--PDPGRLWELIEKYGVTVfFTAPTA-----IRALMkAGDEPLKKY 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  796 DLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYGLAE-NCVFVSCAYGKK-KPilvdwqGRICC---GYvdp 870
Cdd:COG0365    304 DLSSLRLLGSAGEPLNPEVWEWWYEA---VGV---PIVDGWGQTEtGGIFISNLPGLPvKP------GSMGKpvpGY--- 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  871 ndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAG--IGYWGKEELSQKTFRNKlqnYPGrkYTRTGDLGWVIQ-GNLFI 947
Cdd:COG0365    369 -----DVAVVD-EDGNPV-PPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGR---FPG--WYRTGDGARRDEdGYFWI 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIK 1027
Cdd:COG0365    437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAE---AAVVGVPDEI---RGQVV------KAFVV---LKPGVEPSDELAK 501
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1028 QIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRFEcLKQFVDG 1072
Cdd:COG0365    502 ELQAHVREE----LGPYA--YPREIEfvdelpKTRSGKIMRRL-LRKIAEG 545
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
526-1062 7.54e-41

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: 159.40  E-value: 7.54e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplqrggqALTKIE---NIA 602
Cdd:cd05926     16 TYADLAELVDDLARQL---AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP---------AYKKAEfefYLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAILSTVGYHAAVRA-----GLVKNL--ISFTGKSVKSTGQWPNLPWLHTdswiksskvlpasNIAFQSESQPDD 675
Cdd:cd05926     84 DLGSKLVLTPKGELGPASRAasklgLAILELalDVGVLIRAPSAESLSNLLADKK-------------NAKSEGVPLPDD 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  676 LCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS--NTVLVswLPQYHDMGLIGGLFTAMACGGSAIL---FSPL 750
Cdd:cd05926    151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPddRTLVV--MPLFHVHGLVASLLSTLAAGGSVVLpprFSAS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFirnplmWlQTISDYKAT-HSAGPNFaFELVIRRLEADKAKArnydLSSMIFFMIAAEPVRQKTLKRfveltrpfgLSQ 829
Cdd:cd05926    229 TF------W-PDVRDYNATwYTAVPTI-HQILLNRPEPNPESP----PPKLRFIRSCSASLPPAVLEA---------LEA 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  830 EVMAP---GYGLAENCVFVSC---AYGKKKPILVdwqGRiccgyvdPNdaDVDIRIVDADTglEVDEDGKEGEIWISSPS 903
Cdd:cd05926    288 TFGAPvleAYGMTEAAHQMTSnplPPGPRKPGSV---GK-------PV--GVEVRILDEDG--EILPPGVVGEICLRGPN 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  904 AGIGYWGKEELSQK-TFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-P 980
Cdd:cd05926    354 VTRGYLNNPEANAEaAFKD--------GWFRTGDLGYLDAdGYLFLTGRIKELINRGGEKISPLEVDGV------LLShP 419
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  981 GC--CAVIGVPEEVLsakgislpdaSDEVGLVVIAELrDSKLVNKDIIKQIESRVAEehgVTVASvKLIRPRTISKTTSG 1058
Cdd:cd05926    420 AVleAVAFGVPDEKY----------GEEVAAAVVLRE-GASVTEEELRAFCRKHLAA---FKVPK-KVYFVDELPKTATG 484

                   ....
gi 1917948728 1059 KIKR 1062
Cdd:cd05926    485 KIQR 488
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
524-1072 1.57e-40

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 159.20  E-value: 1.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDplqrggqaltKIEN 600
Cdd:PRK06187    31 RTTYAELDERVNRLANALRAL---GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInirLKPE----------EIAY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 IAKLCNAVAIL---STVGYHAAVRAGL--VKNLISFTGKSVKSTGQwpnlPWLHTDSWIKSskvlpASNIAFQSESQPDD 675
Cdd:PRK06187    98 ILNDAEDRVVLvdsEFVPLLAAILPQLptVRTVIVEGDGPAAPLAP----EVGEYEELLAA-----ASDTFDFPDIDEND 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  676 LCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLigGL-FTAMACGGSAILfsPLTFIR 754
Cdd:PRK06187   169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLpYLALMAGAKQVI--PRRFDP 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLmwLQTISDYKATHSAGPNFAFELVIRRLEAdkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSqevMAP 834
Cdd:PRK06187   245 ENL--LDLIETERVTFFFAVPTIWQMLLKAPRA-----YFVDFSSLRLVIYGGAALPPALLREFKEK---FGID---LVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENCVFVSCAY-------GKKKPILvdwQGRICCGyvdpndadVDIRIVDADtGLEVDEDGKE-GEIWISSPSAGI 906
Cdd:PRK06187   312 GYGMTETSPVVSVLPpedqlpgQWTKRRS---AGRPLPG--------VEARIVDDD-GDELPPDGGEvGEIIVRGPWLMQ 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  907 GYWGKEELSQKTFRNklqnypGrkYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC- 982
Cdd:PRK06187   380 GYWNRPEATAETIDG------G--WLHTGDVG-YIdeDGYLYITDRIKDVIISGGENIYPRELE------DALYGhPAVa 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  983 -CAVIGVPEEvlsakgislpdASDEVGLVVIaELRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------K 1054
Cdd:PRK06187   445 eVAVIGVPDE-----------KWGERPVAVV-VLKPGATLDaKELRAFLRGRLA----------KFKLPKRIAfvdelpR 502
                          570
                   ....*....|....*...
gi 1917948728 1055 TTSGKIKRFECLKQFVDG 1072
Cdd:PRK06187   503 TSVGKILKRVLREQYAEG 520
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
487-1062 7.05e-37

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: 147.77  E-value: 7.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  487 FPNLPTLDCYLkHWAAQEITQNKALytwINegGAVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFI 566
Cdd:cd05904      1 LPTDLPLDSVS-FLFASAHPSRPAL---ID--AATGRALTYAELERRVRRLAAGL---AKRGGRKGDVVLLLSPNSIEFP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  567 DAFFGCLRAKVIPIPVLP---PDPLQRggQAltkieniaKLCNAVAILSTvgyhaavrAGLVKNLISFtGKSVKSTGQWP 643
Cdd:cd05904     72 VAFLAVLSLGAVVTTANPlstPAEIAK--QV--------KDSGAKLAFTT--------AELAEKLASL-ALPVVLLDSAE 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  644 NLPWLHTDSWIKSSKVLPasniaFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS---NTVLVS 720
Cdd:cd05904    133 FDSLSFSDLLFEADEAEP-----PVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdseDVFLCV 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  721 wLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFIRNplmwlqtISDYKATH-SAGPNFAFELVirrleaDKAKARNYD 796
Cdd:cd05904    208 -LPMFHIYGLSSFALGLLRLGATVVVmprFDLEELLAA-------IERYKVTHlPVVPPIVLALV------KSPIVDKYD 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  797 LSSMIFFMIAAEPVRQKTLKRFVEltrPFGLSQEVMapGYGLAE-NCVFVSCAYGKKKPILVDwqgriCCGYVDPNdadV 875
Cdd:cd05904    274 LSSLRQIMSGAAPLGKELIEAFRA---KFPNVDLGQ--GYGMTEsTGVVAMCFAPEKDRAKYG-----SVGRLVPN---V 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  876 DIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDL 954
Cdd:cd05904    341 EAKIVDPETG-ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-------GWLHTGDLCYIDEdGYLFIVDRLKEL 412
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  955 IIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsaKGISLPdasdeVGLVVIAelRDSKLVNKDIIKQIESRva 1034
Cdd:cd05904    413 IKYKGFQVAPAELEALLLSHPEILD---AAVIPYPDE----EAGEVP-----MAFVVRK--PGSSLTEDEIMDFVAKQ-- 476
                          570       580       590
                   ....*....|....*....|....*....|..
gi 1917948728 1035 eehgvtVASVKLIRPRT----ISKTTSGKIKR 1062
Cdd:cd05904    477 ------VAPYKKVRKVAfvdaIPKSPSGKILR 502
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
526-1062 1.55e-36

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: 144.93  E-value: 1.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltSRKpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplqrggqaltkieniaklc 605
Cdd:cd05935      3 TYLELLEVVKKLASFL--SNK-GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP--------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhaavraglvkNLISFtgksvkstgqwpNLPWLHTDSWIKSSKVLpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd05935     59 ---------------------MLKER------------ELEYILNDSGAKVAVVG----------SELDDLALIPYTSGT 95
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSplTFIRNPLmwLQTISD 765
Cdd:cd05935     96 TGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA--RWDRETA--LELIEK 171
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATHS-AGPNFAFELVirrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSqevmapGYGLAEncvf 844
Cdd:cd05935    172 YKVTFWtNIPTMLVDLL------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVE------GYGLTE---- 235
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  845 vSCAYGKKKPILVdwQGRICCGYVdpnDADVDIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQ 924
Cdd:cd05935    236 -TMSQTHTNPPLR--PKLQCLGIP---*FGVDARVIDIETGRELP-PNEVGEIVVRGPQIFKGYWNRPEETEESF----I 304
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  925 NYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsakgislpDA 1003
Cdd:cd05935    305 EIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E---VCVISVPDE----------RV 371
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 1004 SDEV-GLVVIAELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTIS------KTTSGKIKR 1062
Cdd:cd05935    372 GEEVkAFIVLRPEYRGKVTEEDIIEWAREQ--------MAAYK--YPREVEfvdelpRSASGKILW 427
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
526-968 1.19e-34

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 141.64  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltSRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK--VIPI-PVLPPDPLqrggqaltkiENIA 602
Cdd:PRK08314    37 SYRELLEEAERLAGYL--QQECGVRKGDRVLLYMQNSPQFVIAYYAILRANavVVPVnPMNREEEL----------AHYV 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAILSTVGYHAAVRAGL----VKNLI--SFTGkSVKSTGQWPNLPWLHT---------DSWIKSSKVLPASNIAF 667
Cdd:PRK08314   105 TDSGARVAIVGSELAPKVAPAVgnlrLRHVIvaQYSD-YLPAEPEIAVPAWLRAepplqalapGGVVAWKEALAAGLAPP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  668 QSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILF 747
Cdd:PRK08314   184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 SpltfirnplMW-----LQTISDYKATH-----------SAGPNFAfelvirrleadkakarNYDLSSMIFfmI----AA 807
Cdd:PRK08314   264 P---------RWdreaaARLIERYRVTHwtniptmvvdfLASPGLA----------------ERDLSSLRY--IggggAA 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  808 EP--VRQKTLKRFveltrpfGLS-QEvmapGYGLAENCVFVscaygkkkpilvdwqgriccgYVDPNDA----------- 873
Cdd:PRK08314   317 MPeaVAERLKELT-------GLDyVE----GYGLTETMAQT---------------------HSNPPDRpklqclgiptf 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  874 DVDIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQNYPGRKYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK08314   365 GVDARVIDPETLEELP-PGEVGEIVVHGPQVFKGYWNRPEATAEAF----IEIDGKRFFRTGDLGRMdEEGYFFITDRLK 439
                          490
                   ....*....|....*.
gi 1917948728  953 DLIIVAGRNIYSADVE 968
Cdd:PRK08314   440 RMINASGFKVWPAEVE 455
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
673-1064 4.00e-33

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: 132.79  E-value: 4.00e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLftaMAC--GGSAILFSPL 750
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGV---LACltHGATMVFPSP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFirNPLMWLQTISDYKATHSAGPNFAFelvIRRLEADKAKarNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSQE 830
Cdd:cd05917     78 SF--DPLAVLEAIEKEKCTALHGVPTMF---IAELEHPDFD--KFDLSSLRTGIMAGAPCPPELMKRVIEV---MNMKDV 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  831 VMApgYGLAENCVfVSCAYGKKKPILVdwqgRI-CCGYVDPndaDVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:cd05917    148 TIA--YGMTETSP-VSTQTRTDDSIEK----RVnTVGRIMP---HTEAKIVDPEGG-IVPPVGVPGELCIRGYSVMKGYW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  910 GKEELSQKTFRNKlqnypgrKYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIG 987
Cdd:cd05917    217 NDPEKTAEAIDGD-------GWLHTGDLA-VMdeDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSD---VQVVG 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  988 VPEEVLsakgislpdaSDEVGLVVIaeLRD-SKLVNKDIIKQIESRVAeEHGVtvasvklirPRTI------SKTTSGKI 1060
Cdd:cd05917    286 VPDERY----------GEEVCAWIR--LKEgAELTEEDIKAYCKGKIA-HYKV---------PRYVffvdefPLTVSGKI 343

                   ....
gi 1917948728 1061 KRFE 1064
Cdd:cd05917    344 QKFK 347
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
526-951 1.27e-32

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: 132.77  E-value: 1.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKL 604
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKAGAAYVPLDPAYPAER-------LAFILED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGyHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLhtdswiksskvlpasniafQSESQPDDLCFLQFTSG 684
Cdd:TIGR01733   71 AGARLLLTDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------DAPSGPDDLAYVIYTSG 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMACGGSAILFSPLTFIRNPLMWLQTIS 764
Cdd:TIGR01733  131 STGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIA 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  765 DYKATHSAGPNFAFELVirrleadkAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAENCVF 844
Cdd:TIGR01733  210 EHPVTVLNLTPSLLALL--------AAALPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTVW 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  845 VSCAYgkKKPILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN--K 922
Cdd:TIGR01733  277 STATL--VDPDDAPRESPVPIGRPLAN---TRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPdpF 349
                          410       420       430
                   ....*....|....*....|....*....|
gi 1917948728  923 LQNYPGRKYtRTGDLG-WVIQGNLFITGRI 951
Cdd:TIGR01733  350 AGGDGARLY-RTGDLVrYLPDGNLEFLGRI 378
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
525-1063 2.36e-32

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: 134.03  E-value: 2.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQrggQALTkiENI 601
Cdd:cd05959     30 LTYAELEAEARRVAGAL---RALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlLTPDDYA---YYLE--DSR 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AK-LCNAVAILSTVGYHAAVRAGLVKNLISFTGKsvkstGQWPNLPWLhTDSWIKSSKVLPASNiafqseSQPDDLCFLQ 680
Cdd:cd05959    102 ARvVVVSGELAPVLAAALTKSEHTLVVLIVSGGA-----GPEAGALLL-AELVAAEAEQLKPAA------THADDPAFWL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGVMITHGGLIHNVKLMRRR-YRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFS--PltfirNPL 757
Cdd:cd05959    170 YSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPerP-----TPA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 MWLQTISDYKATHSAG-PNFAFELvirrLEADKAKARnyDLSSMIFFMIAAEPVRQKTLKRFvelTRPFGLSqevMAPGY 836
Cdd:cd05959    245 AVFKRIRRYRPTVFFGvPTLYAAM----LAAPNLPSR--DLSSLRLCVSAGEALPAEVGERW---KARFGLD---ILDGI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  837 GLAENC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd05959    313 GSTEMLhIFLSNRPGRVRY---GTTGKPVPGY--------EVELRD-EDGGDV-ADGEPGELYVRGPSSATMYWNNRDKT 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  916 QKTFRNKLqNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:cd05959    380 RDTFQGEW-TRTGDKYVRDDD------GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGVEDED--- 446
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728  996 kGISLPDAsdevgLVVIA-ELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTI------SKTTSGKIKRF 1063
Cdd:cd05959    447 -GLTKPKA-----FVVLRpGYEDSEALEEELKEFVKDR--------LAPYK--YPRWIvfvdelPKTATGKIQRF 505
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
522-1009 3.57e-32

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 134.74  E-value: 3.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLV--HVPglDFIDAFFGCLRAKVIPI---PVLPPDPLQ------- 589
Cdd:PRK05605    55 GATTTYAELGKQVRRAAAGL---RALGVRPGDRVAIVlpNCP--QHIVAFYAVLRLGAVVVehnPLYTAHELEhpfedhg 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  590 --------RGGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPN-LPWlhtdSWIKSSKVL 660
Cdd:PRK05605   130 arvaivwdKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRLALRLPIPALRKARAALTGPAPGtVPW----ETLVDAAIG 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVkLMRRRY----RSTSNTVLVSwLPQYHDMGLIGGLFT 736
Cdd:PRK05605   206 GDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWvpglGDGPERVLAA-LPMFHAYGLTLCLTL 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  737 AMACGGSAILF-SPltfiRNPLMwLQTISDYKATHSAG-PNfafelVIRRLeADKAKARNYDLSSMIFFMIAAEPVRQKT 814
Cdd:PRK05605   284 AVSIGGELVLLpAP----DIDLI-LDAMKKHPPTWLPGvPP-----LYEKI-AEAAEERGVDLSGVRNAFSGAMALPVST 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  815 LKRFVELTRpfGLSQEvmapGYGLAENCVFVSCaygkkKPILVDWQGriccGYVDPNDADVDIRIVDADTGLEVDEDGKE 894
Cdd:PRK05605   353 VELWEKLTG--GLLVE----GYGLTETSPIIVG-----NPMSDDRRP----GYVGVPFPDTEVRIVDPEDPDETMPDGEE 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 GEIWISSPSAGIGYWGKEELSQKTFrnklqnYPGrkYTRTGDLGwVIQGNLFIT--GRIKDLIIVAGRNIYSADVEktve 972
Cdd:PRK05605   418 GELLVRGPQVFKGYWNRPEETAKSF------LDG--WFRTGDVV-VMEEDGFIRivDRIKELIITGGFNVYPAEVE---- 484
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1917948728  973 sssELLR--PGC--CAVIGVP-----EEVLSAkgISLPDAS--DEVGL 1009
Cdd:PRK05605   485 ---EVLRehPGVedAAVVGLPredgsEEVVAA--VVLEPGAalDPEGL 527
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
525-1064 4.51e-32

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: 132.12  E-value: 4.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  525 RTYAELDSNASCVAHKLLTSRkptIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIPIPVLPpdplqrggqALTKIEniak 603
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALG---VGPGDVVA-FQLPNwWEFAVLYLACLRIGAVTNPILP---------FFREHE---- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 lcnAVAILStvgyHAAVRAGLVknlisftgksvkstgqwpnlpwlhTDSWIKsskvlpasniaFQSESQPDDLCFLQFTS 683
Cdd:cd05903     65 ---LAFILR----RAKAKVFVV------------------------PERFRQ-----------FDPAAMPDAVALLLFTS 102
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltfIRNPLMWLQTI 763
Cdd:cd05903    103 GTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALALM 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  764 SDYKATHSAG-PNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYGLAENC 842
Cdd:cd05903    179 REHGVTFMMGaTPFLTDLLNAVEEAGE------PLSRLRTFVCGGATVPRSLARRAAEL---LGA---KVCSAYGSTECP 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  843 vfvsCAYGKKKPILVDwqgRICC--GYVDPNdadVDIRIVDaDTGLEVDEdGKEGEIWISSPSAGIGYWGKEELsqkTFR 920
Cdd:cd05903    247 ----GAVTSITPAPED---RRLYtdGRPLPG---VEIKVVD-DTGATLAP-GVEGELLSRGPSVFLGYLDRPDL---TAD 311
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  921 nklqNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIGVPEE----- 991
Cdd:cd05903    312 ----AAPEGWF-RTGDLArLDEDGYLRITGRSKDIIIRGGENIPVLEVE------DLLLGhPGVieAAVVALPDErlger 380
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  992 ---VLSAKGISLPDASDevglvvIAELRDSKLVNKDIIKqiesrvaeEHGVTVASVklirPRtiskTTSGKIKRFE 1064
Cdd:cd05903    381 acaVVVTKSGALLTFDE------LVAYLDRQGVAKQYWP--------ERLVHVDDL----PR----TPSGKVQKFR 434
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
526-1062 1.19e-31

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 132.34  E-value: 1.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP-------PDPLQRGGqaltki 598
Cdd:PRK07656    32 TYAELNARVRRAAAALAAL---GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTrytadeaAYILARGD------ 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  599 eniAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQwPNLPWlhtDSWIKsskvlPASNIAFQSESQPDDLCF 678
Cdd:PRK07656   103 ---AKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTE-KMKTF---TDFLA-----AGDPAERAPEVDPDDVAD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  679 LQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirn 755
Cdd:PRK07656   171 ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPlpvFDPDEV--- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  756 plmwLQTISDYKATHSAGP----NFAFelvirrleaDKAKARNYDLSSMIFFMI--AAEPVRqkTLKRFVELtrpFGLsq 829
Cdd:PRK07656   248 ----FRLIETERITVLPGPptmyNSLL---------QHPDRSAEDLSSLRLAVTgaASMPVA--LLERFESE---LGV-- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  830 EVMAPGYGLAENCVFVS-CAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGY 908
Cdd:PRK07656   308 DIVLTGYGLSEASGVTTfNRLDDDRKTVAGTIGTAI--------AGVENKIVNEL-GEEV-PVGEVGELLVRGPNVMKGY 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  909 WGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PGC--CA 984
Cdd:PRK07656   378 YDDPEATAAAIDAD-------GWLHTGDLGRLDEeGYLYIVDRKKDMFIVGGFNVYPAEVEEV------LYEhPAVaeAA 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  985 VIGVPEEVLSakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSG 1058
Cdd:PRK07656   445 VIGVPDERLG-----------EVGKAYVVLKPGAELTEEELIAYCREHLA----------KYKVPRSIEfldelpKNATG 503

                   ....
gi 1917948728 1059 KIKR 1062
Cdd:PRK07656   504 KVLK 507
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
673-1064 1.81e-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: 127.33  E-value: 1.81e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACG-------GSAI 745
Cdd:cd05907     86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGariyfasSAET 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  746 L------FSPLTFIRNPLMWlQTISDyKATHSAGPNFafelviRRLEADKAKarnydLSSMIFFMIAAEPVRQKTLKRFv 819
Cdd:cd05907    166 LlddlseVRPTVFLAVPRVW-EKVYA-AIKVKAVPGL------KRKLFDLAV-----GGRLRFAASGGAPLPAELLHFF- 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  820 eltRPFGLsqeVMAPGYGLAENCVFVSCAygkkkpilVDWQGRI-CCGYVDPndaDVDIRIVDadtglevdedgkEGEIW 898
Cdd:cd05907    232 ---RALGI---PVYEGYGLTETSAVVTLN--------PPGDNRIgTVGKPLP---GVEVRIAD------------DGEIL 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  899 ISSPSAGIGYWGKEElsqKTFRNKLQNypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS-- 974
Cdd:cd05907    283 VRGPNVMLGYYKNPE---ATAEALDAD----GWLHTGDLGEIdEDGFLHITGRKKDLIITSgGKNISPEPIENALKASpl 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  975 -SELL-----RPGCCAVIGVPEEVLSA----KGISLPDASDevglvviaelrdsKLVNKDIIKQIESRVAEE-HGVT-VA 1042
Cdd:cd05907    356 iSQAVvigdgRPFLVALIVPDPEALEAwaeeHGIAYTDVAE-------------LAANPAVRAEIEAAVEAAnARLSrYE 422
                          410       420
                   ....*....|....*....|....*....
gi 1917948728 1043 SVK----LIRPRTIS---KTTSGKIKRFE 1064
Cdd:cd05907    423 QIKkfllLPEPFTIEngeLTPTLKLKRPV 451
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
526-993 1.27e-29

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: 126.41  E-value: 1.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLtsrKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPdplQRGgqalTKIENIAKL 604
Cdd:COG1021     52 SYAELDRRADRLAAGLL---ALGLRPGDRVV-VQLPnVAEFVIVFFALFRAGAIPVFALPA---HRR----AEISHFAEQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILST--------VGYHAAVRAGL--VKNLISftgksVKSTGQWPNLpwlhtDSWIKSskvlPASniAFQSESQPD 674
Cdd:COG1021    121 SEAVAYIIPdrhrgfdyRALARELQAEVpsLRHVLV-----VGDAGEFTSL-----DALLAA----PAD--LSEPRPDPD 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLFTAMACGGSAIL---FSPL 750
Cdd:COG1021    185 DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLapdPSPD 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFIrnPLmwlqtISDYKATHSA-GPnfafELVIRRLEAdkAKARNYDLSSMIFFMI-----AAEPVRQktlkrfvelTRP 824
Cdd:COG1021    265 TAF--PL-----IERERVTVTAlVP----PLALLWLDA--AERSRYDLSSLRVLQVggaklSPELARR---------VRP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  825 -FGLS-QEVmapgYGLAE---NCVfvscaygkkKP-----ILVDWQGR-ICcgyvdPNDadvDIRIVDaDTGLEVdEDGK 893
Cdd:COG1021    323 aLGCTlQQV----FGMAEglvNYT---------RLddpeeVILTTQGRpIS-----PDD---EVRIVD-EDGNPV-PPGE 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  894 EGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypGrkYTRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEkt 970
Cdd:COG1021    380 VGELLTRGPYTIRGYYRAPEHNARAFTPD-----G--FYRTGDL--VRRtpdGYLVVEGRAKDQINRGGEKIAAEEVE-- 448
                          490       500
                   ....*....|....*....|....*.
gi 1917948728  971 vessSELLR-PGC--CAVIGVPEEVL 993
Cdd:COG1021    449 ----NLLLAhPAVhdAAVVAMPDEYL 470
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
522-951 3.61e-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: 123.41  E-value: 3.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRV-LLVHvPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIEN 600
Cdd:cd05930     10 DQSLTYAELDARANRLARYL---RERGVGPGDLVaVLLE-RSLEMVVAILAVLKAGAAYVPLDPSYPAER-------LAY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 IAKLCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQ 680
Cdd:cd05930     79 ILEDSGAKLVLT-----------------------------------------------------------DPDDLAYVI 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWL 760
Cdd:cd05930    100 YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEEV-RKDPEALA 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAGPNFAFELVIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAE 840
Cdd:cd05930    178 DLLAEEGITVLHLTPSLLRLLLQELELA-------ALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTE 245
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NCVFVSCAYGKKKPILVDwqgRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd05930    246 ATVDATYYRVPPDDEEDG---RVPIGRPIPN---TRVYVLDEN--LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFV 317
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1917948728  921 NkLQNYPGRKYTRTGDLG-WVIQGNLFITGRI 951
Cdd:cd05930    318 P-NPFGPGERMYRTGDLVrWLPDGNLEFLGRI 348
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
526-1064 6.16e-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: 122.40  E-value: 6.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplQRGGQALTkieniaklc 605
Cdd:cd05934      5 TYAELLRESARIAAALAAL---GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT----ALRGDELA--------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navAILSTVGYHAAVRaglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpdDLCFLQFTSGS 685
Cdd:cd05934     69 ---YIIDHSGAQLVVV-----------------------------------------------------DPASILYTSGT 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmWLQt 762
Cdd:cd05934     93 TGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlprFSASRF------WSD- 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYKAT--HSAGPNFAFELVIRRLEADKA-KARnydlssmiffMIAAEPVRQKTLKRFVEltRpFGLsqeVMAPGYGLA 839
Cdd:cd05934    166 VRRYGATvtNYLGAMLSYLLAQPPSPDDRAhRLR----------AAYGAPNPPELHEEFEE--R-FGV---RLLEGYGMT 229
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  840 ENCVFVSCAYGKKKPILvdwqgriCCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWI-SSPSAGI--GYWGKEELSQ 916
Cdd:cd05934    230 ETIVGVIGPRDEPRRPG-------SIGRPAP---GYEVRIVDDD-GQEL-PAGEPGELVIrGLRGWGFfkGYYNMPEATA 297
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  917 KTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:cd05934    298 EAMRN--------GWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE---AAVVAVPDEV--- 363
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  996 kgislpdASDEVGLVVIaeLRD-SKLVNKDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKIKRFE 1064
Cdd:cd05934    364 -------GEDEVKAVVV--LRPgETLDPEELFAFCEGQLA----------YFKVPRYIRfvddlpKTPTEKVAKAQ 420
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
526-993 4.38e-28

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: 120.09  E-value: 4.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLqrggqaltkieniaklc 605
Cdd:cd05941     13 TYADLVARAARLANRLLALGK--DLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL----------------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhaavraglvknlisftgksvkstgqwPNLPWLHTDSwiKSSKVLpasniafqsesqpdDLCFLQFTSGS 685
Cdd:cd05941     74 -------------------------------------AELEYVITDS--EPSLVL--------------DPALILYTSGT 100
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLT----------- 751
Cdd:cd05941    101 TGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFlpkFDPKEvaisrlmpsit 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  752 -FIRNPLMWLQTISDYKAtHSAGPNFAFELVIRRLEadkakarnydlssmifFMI---AAEPVrqKTLKRFVELTRPFGL 827
Cdd:cd05941    181 vFMGVPTIYTRLLQYYEA-HFTDPQFARAAAAERLR----------------LMVsgsAALPV--PTLEEWEAITGHTLL 241
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  828 SQevmapgYGLAENCVFVSCAY-GKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDEdGKEGEIWISSPSAGI 906
Cdd:cd05941    242 ER------YGMTEIGMALSNPLdGERRP-----------GTVGMPLPGVQARIVDEETGEPLPR-GEVGEIQVRGPSVFK 303
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  907 GYWGKEELSQKTFRnklqnypGRKYTRTGDLGWV-IQGNLFITGRIKDLII-VAGRNIYSADVEKTVESssellRPGC-- 982
Cdd:cd05941    304 EYWNKPEATKEEFT-------DDGWFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLA-----HPGVse 371
                          490
                   ....*....|.
gi 1917948728  983 CAVIGVPEEVL 993
Cdd:cd05941    372 CAVIGVPDPDW 382
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
549-1064 4.16e-27

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 119.00  E-value: 4.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  549 IKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTKIENIAKLCNAVA--------ILS 612
Cdd:PRK08974    71 LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPlytPRELEHqlndsGAKAIVIVSNFAHTLEKVVfktpvkhvILT 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  613 TVGYHAAVRAGlvkNLISFTGKSVKSTGQWPNLPwlHTDSWIKS-SK------VLPasniafqsESQPDDLCFLQFTSGS 685
Cdd:PRK08974   151 RMGDQLSTAKG---TLVNFVVKYIKRLVPKYHLP--DAISFRSAlHKgrrmqyVKP--------ELVPEDLAFLQYTGGT 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVK--------LMRRRYRstsntVLVSWLPQYHDMGLIGGLFTAMACGGSAILfspltfIRNPL 757
Cdd:PRK08974   218 TGVAKGAMLTHRNMLANLEqakaaygpLLHPGKE-----LVVTALPLYHIFALTVNCLLFIELGGQNLL------ITNPR 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 ---MWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSqevmap 834
Cdd:PRK08974   287 dipGFVKELKKYPFTAITGVNTLFNALLNNEEFQEL-----DFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE------ 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENCVFVSCAygkkkPI-LVDWQGRIccGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:PRK08974   356 GYGLTECSPLVSVN-----PYdLDYYSGSI--GLPVPS---TEIKLVD-DDGNEV-PPGEPGELWVKGPQVMLGYWQRPE 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  914 LSQKTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEV 992
Cdd:PRK08974   424 ATDEVIKD--------GWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE---VAAVGVPSEV 492
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  993 lsakgislpdaSDE-VGLVVIAelRDSKLVNKDIIKQiesrvAEEH--GVTVAsvKLIRPRT-ISKTTSGKIKRFE 1064
Cdd:PRK08974   493 -----------SGEaVKIFVVK--KDPSLTEEELITH-----CRRHltGYKVP--KLVEFRDeLPKSNVGKILRRE 548
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
1269-1702 9.70e-27

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: 119.09  E-value: 9.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1269 GLPWLHQAsvvlLAPLSWILCIALTSISIAFFGNSFLRINYA------LTPEV-SVWSVDFVKWWALYKAQEVSSKVLav 1341
Cdd:TIGR02353   24 GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPIWGSTYLRFWTVKRLVDAAPTVL-- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1342 hLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHEVRNSILRLQPIRIGRNCSVGPYAV 1419
Cdd:TIGR02353   98 -LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFIGTRST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1420 VQKGSVLREGAEVPALQKSEGGKS-----------ALKMAKAENILK-VSPGTL-KTVQQFMGIYVVGFLsslsaatvyl 1486
Cdd:TIGR02353  175 LDIDTSIGDGAQLGHGSALQGGQSipdgerwhgspAQKTGADYRKVQpARPYTVrRRLYVAGALFVVFVL---------- 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1487 lymslsqkvpsLELLAFLCISGAlhwvpFTIVAYATMFTKAPPNPFEFAISLAIAYFAHGLVLSLLTSIFTHLLAG---K 1563
Cdd:TIGR02353  245 -----------LPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNlvlK 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1564 EKKTQTHikTWFGHQL----AIACHVRFAKLLSG-TEAFCMYLRLLGAKVGRYCSIRAINpIADPRMVSIGAGVHLGDFS 1638
Cdd:TIGR02353  309 PGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGL 385
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1639 RIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:TIGR02353  386 LMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
PRK08316 PRK08316
acyl-CoA synthetase; Validated
524-992 1.68e-26

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 116.57  E-value: 1.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTK--IENI 601
Cdd:PRK08316    36 SWTYAELDAAVNRVAAALLDL---GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV---------NFMLTGeeLAYI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDSWIKSskvlpASNIAFQSESQPDDLCFLQF 681
Cdd:PRK08316   104 LDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEA-----GSVAEPDVELADDDLAQILY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNvklmrrrYRST-------SNTVLVSWLPQYHDMGLIGGLFTAMACGG-SAILFSPltfi 753
Cdd:PRK08316   179 TSGTESLPKGAMLTHRALIAE-------YVSCivagdmsADDIPLHALPLYHCAQLDVFLGPYLYVGAtNVILDAP---- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  754 rNPLMWLQTISDYKATHSagpnFAFELV----IRRLEADKakarnYDLSSM--IFF--MIAAEPVRQKTLKRF--VELTR 823
Cdd:PRK08316   248 -DPELILRTIEAERITSF----FAPPTVwislLRHPDFDT-----RDLSSLrkGYYgaSIMPVEVLKELRERLpgLRFYN 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  824 PFGlsQEVMAPgygLAEncvfV-----------SCAygkkKPILvdwqgriccgyvdpndaDVDIRIVDADtGLEVdEDG 892
Cdd:PRK08316   318 CYG--QTEIAP---LAT----VlgpeehlrrpgSAG----RPVL-----------------NVETRVVDDD-GNDV-APG 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  893 KEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK08316   366 EVGEIVHRSPQLMLGYWDDPEKTAEAFRG--------GWFHSGDLG-VMdeEGYITVVDRKKDMIKTGGENVASREVEEA 436
                          490       500
                   ....*....|....*....|....*
gi 1917948728  971 V---ESSSELlrpgccAVIGVPEEV 992
Cdd:PRK08316   437 LythPAVAEV------AVIGLPDPK 455
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
526-1064 1.91e-26

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 116.66  E-value: 1.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAhKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTK 597
Cdd:PRK07059    50 TYGELDELSRALA-AWLQSRG--LAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPlytPRELEHqlkdsGAEAIVV 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  598 IENIAKLCNAVaILSTVGYHAAVRA-----GLVKNLISFTGKSVKSTGQWPNLPwlhtdSWIKSSKVLPA-SNIAFQSES 671
Cdd:PRK07059   127 LENFATTVQQV-LAKTAVKHVVVASmgdllGFKGHIVNFVVRRVKKMVPAWSLP-----GHVRFNDALAEgARQTFKPVK 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  672 Q-PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM-------RRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGS 743
Cdd:PRK07059   201 LgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpaFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  744 AILfspltfIRNPL---MWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFF----MIAAEPVRqktlK 816
Cdd:PRK07059   281 NIL------IPNPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKL-----DFSKLIVAngggMAVQRPVA----E 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  817 RFVELTRPFglsqevMAPGYGLAENCVFVSCaygkkKPILVD-WQGRIccGYVDPNdADVDIRivdadtglevDEDGKE- 894
Cdd:PRK07059   346 RWLEMTGCP------ITEGYGLSETSPVATC-----NPVDATeFSGTI--GLPLPS-TEVSIR----------DDDGNDl 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 -----GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK07059   402 plgepGEICIRGPQVMAGYWNRPDETAKVMTAD-------GFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  969 KTVESSSELLRpgcCAVIGVPEEvlsakgislpDASDEVGLVVIAelRDSKLVNKDIIKQIESRvaeehgvtVASVKliR 1048
Cdd:PRK07059   475 EVVASHPGVLE---VAAVGVPDE----------HSGEAVKLFVVK--KDPALTEEDVKAFCKER--------LTNYK--R 529
                          570       580
                   ....*....|....*....|..
gi 1917948728 1049 PRTIS------KTTSGKIKRFE 1064
Cdd:PRK07059   530 PKFVEfrtelpKTNVGKILRRE 551
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
526-1027 2.55e-26

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: 114.71  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17653     24 TYGELDAASNALANRL---LQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR-------IQAILRTS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd17653     94 GATLLLTT---------------------------------------------------------DSPDDLAYIIFTSGS 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRST-SNTVLvswlpQYHDMGL---IGGLFTAMACGGSAILfspltfiRNPLMWLQ 761
Cdd:cd17653    117 TGIPKGVMVPHRGVLNYVSQPPARLDVGpGSRVA-----QVLSIAFdacIGEIFSTLCNGGTLVL-------ADPSDPFA 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  762 TISDYKATHSAGPNFAFELvirrleadkaKARNYDLSSMIFFmiAAEPVRQKTLKRFVEltrpfglsQEVMAPGYGLAEn 841
Cdd:cd17653    185 HVARTVDALMSTPSILSTL----------SPQDFPNLKTIFL--GGEAVPPSLLDRWSP--------GRRLYNAYGPTE- 243
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  842 CVfVSCAYGKKKPIlvdwqGRICCGYVDPNdadVDIRIVDADTgLEVDEdGKEGEIWISSPSAGIGYWGKEELSQKTFRN 921
Cdd:cd17653    244 CT-ISSTMTELLPG-----QPVTIGKPIPN---STCYILDADL-QPVPE-GVVGEICISGVQVARGYLGNPALTASKFVP 312
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  922 kLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPgccAVIGVPEEVLSAkgISL 1000
Cdd:cd17653    313 -DPFWPGSRMYRTGDYGrWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQ---AAAIVVNGRLVA--FVT 386
                          490       500
                   ....*....|....*....|....*...
gi 1917948728 1001 PDASDEVGL-VVIAELRDSKLVNKDIIK 1027
Cdd:cd17653    387 PETVDVDGLrSELAKHLPSYAVPDRIIA 414
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
526-1064 2.69e-26

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: 114.48  E-value: 2.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPI---PVLPPDPLqrggqaltkiENIA 602
Cdd:cd05919     12 TYGQLHDGANRLGSAL---RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDDY----------AYIA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAIlstvgyhaaVRAGlvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpDDLCFLQFT 682
Cdd:cd05919     79 RDCEARLV---------VTSA--------------------------------------------------DDIAYLLYS 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  683 SGSTSDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLtfiRNPLMWLQ 761
Cdd:cd05919    100 SGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW---PTAERVLA 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  762 TISDYKATHSAG-PNFafelvIRRLEADKAKARNyDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSqevMAPGYGLAE 840
Cdd:cd05919    177 TLARFRPTVLYGvPTF-----YANLLDSCAGSPD-ALRSLRLCVSAGEALPRGLGERWMEH---FGGP---ILDGIGATE 244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTF 919
Cdd:cd05919    245 VGhIFLSNRPGAWRL---GSTGRPVPGY--------EIRLVD-EEGHTI-PPGEEGDLLVRGPSAAVGYWNNPEKSRATF 311
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  920 RNKLQnYPGRKYTRTGDlGWVIQgnlfiTGRIKDLIIVAGRNIYSADVEKTVesssellrpgcCAVIGVPEEVLsakgIS 999
Cdd:cd05919    312 NGGWY-RTGDKFCRDAD-GWYTH-----AGRADDMLKVGGQWVSPVEVESLI-----------IQHPAVAEAAV----VA 369
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1000 LPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEehgvTVASVKliRPRTIS------KTTSGKIKRFE 1064
Cdd:cd05919    370 VPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLE----RLSAHK--VPRRIAfvdelpRTATGKLQRFK 434
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
671-1063 3.51e-26

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: 114.85  E-value: 3.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  671 SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILfspL 750
Cdd:cd05914     86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVF---L 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFIRNPLMWLQtiSDYKATHSAG---PNFAFELVIRRLEADKAKARN-YDLSSMIFFMIAAEPVRQKTLKRFVELTRPF- 825
Cdd:cd05914    163 DKIPSAKIIAL--AFAQVTPTLGvpvPLVIEKIFKMDIIPKLTLKKFkFKLAKKINNRKIRKLAFKKVHEAFGGNIKEFv 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  826 ----GLSQEV----------MAPGYGLAENCVFVScaYGKKKPILVDwqgriCCGYVDPNdadVDIRIVDADTGLEvded 891
Cdd:cd05914    241 iggaKINPDVeeflrtigfpYTIGYGMTETAPIIS--YSPPNRIRLG-----SAGKVIDG---VEVRIDSPDPATG---- 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  892 gkEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIV-AGRNIYSADVEK 969
Cdd:cd05914    307 --EGEIIVRGPNVMKGYYKNPEATAEAFDKD-------GWFHTGDLGkIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEA 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  970 TVESSSELLRpgccAVIGVPEEVLSAKGISLPDASDEvglvviaelrdSKLVNKDIIKQIESRVAEEHGVTVASVK---- 1045
Cdd:cd05914    378 KINNMPFVLE----SLVVVQEKKLVALAYIDPDFLDV-----------KALKQRNIIDAIKWEVRDKVNQKVPNYKkisk 442
                          410
                   ....*....|....*....
gi 1917948728 1046 -LIRPRTISKTTSGKIKRF 1063
Cdd:cd05914    443 vKIVKEEFEKTPKGKIKRF 461
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
665-991 1.18e-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: 113.58  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  665 IAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSA 744
Cdd:cd05909    138 IFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  745 IL-FSPLtfirNPLMWLQTISDYKATHSAG-PNFaFELVIRRleadkakARNYDLSSMIFFMIAAEPVRQKTLKRFVELt 822
Cdd:cd05909    218 VFhPNPL----DYKKIPELIYDKKATILLGtPTF-LRGYARA-------AHPEDFSSLRLVVAGAEKLKDTLRQEFQEK- 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  823 rpFGLsqeVMAPGYGLAENCVFVSCaygkKKPILVDWQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKEGEIWISSP 902
Cdd:cd05909    285 --FGI---RILEGYGTTECSPVISV----NTPQSPNKEG--TVGRPLPG---MEVKIVSVETHEEVPI-GEGGLLLVRGP 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  903 SAGIGYWGKEELSQKTFrnklqnypGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvESSSELLRP- 980
Cdd:cd05909    350 NVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIE---DILSEILPEd 418
                          330
                   ....*....|.
gi 1917948728  981 GCCAVIGVPEE 991
Cdd:cd05909    419 NEVAVVSVPDG 429
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
526-951 1.32e-25

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: 116.49  E-value: 1.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK---VipiPVLPPDPLQRggqaltkIENIA 602
Cdd:COG1020    503 TYAELNARANRLAHHL---RALGVGPGDLVGVCLERSLEMVVALLAVLKAGaayV---PLDPAYPAER-------LAYML 569
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAILSTvgyhAAVRAGLvknlisftgksvkstgQWPNLPWLHTDSWIKSSkvLPASNIAfqSESQPDDLCFLQFT 682
Cdd:COG1020    570 EDAGARLVLTQ----SALAARL----------------PELGVPVLALDALALAA--EPATNPP--VPVTPDDLAYVIYT 625
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  683 SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:COG1020    626 SGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEA-RRDPAALAEL 703
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYKATHSagpNF---AFELVirrLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLA 839
Cdd:COG1020    704 LARHRVTVL---NLtpsLLRAL---LDAAPE-----ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPT 767
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  840 ENCVFVSCAygkkkPILVD--WQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:COG1020    768 ETTVDSTYY-----EVTPPdaDGGSVPIGRPIAN---TRVYVLDAH--LQPVPVGVPGELYIGGAGLARGYLNRPELTAE 837
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1917948728  918 TFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRI 951
Cdd:COG1020    838 RFVADPFGFPGARLYRTGDLArWLPDGNLEFLGRA 872
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
522-1064 2.91e-25

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 112.92  E-value: 2.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLvHVPGL-DFIDAFFGCLRAKVIPIPVLPpdplQRGGQALTKIEN 600
Cdd:PRK06087    47 GASYTYSALDHAASRLANWLLAK---GIEPGDRVAF-QLPGWcEFTIIYLACLKVGAVSVPLLP----SWREAELVWVLN 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 iakLCNAVAILSTVGYHAAVRAGLVKNLISftgksvkstgQWPNL-PWLHTDSWIKSSKVLPASNIAFQSES-------Q 672
Cdd:PRK06087   119 ---KCQAKMFFAPTLFKQTRPVDLILPLQN----------QLPQLqQIVGVDKLAPATSSLSLSQIIADYEPlttaittH 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltf 752
Cdd:PRK06087   186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD---- 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 IRNPLMWLQTISDYKATHSAGPN-FAFELvIRRLEADKakarnYDLSSMIFFMIAAEPVRqktlKRFVELTRPFGLsqeV 831
Cdd:PRK06087   262 IFTPDACLALLEQQRCTCMLGATpFIYDL-LNLLEKQP-----ADLSALRFFLCGGTTIP----KKVARECQQRGI---K 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  832 MAPGYGLAENCVFVSCAYGKKKPILVDWQGRICCGyvdpndadVDIRIVDADTGlEVDEdGKEGEIWISSPSAGIGYWGK 911
Cdd:PRK06087   329 LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAG--------VEIKVVDEARK-TLPP-GCEGEEASRGPNVFMGYLDE 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  912 EELSQKTFRNKlqnypGRKYtrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVIGVPE 990
Cdd:PRK06087   399 PELTARALDEE-----GWYY--SGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDIL---LQHPKIHDACVVAMPD 468
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728  991 EVLSAKGISLPDASDEVGLVVIAELRdSKLVNKDIIKqiesRVAEEHGVTVASvklirprtISKTTSGKIKRFE 1064
Cdd:PRK06087   469 ERLGERSCAYVVLKAPHHSLTLEEVV-AFFSRKRVAK----YKYPEHIVVIDK--------LPRTASGKIQKFL 529
catalase_like cd08150
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
1747-2045 3.61e-24

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: 104.95  E-value: 3.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1747 RYFHRIGVSGKGYLKLYDDIQGLPEHDIFGPGKRYTVIVRHSNSLSADDDARlDARGAALRI-LSDDSPLLDLTLKTGKA 1825
Cdd:cd08150      3 RGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKP-DIRGFAIKFtGVADAGTLDFVLNNTPV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1826 FYARTISDFATWLV---------CGLAAREEHVKRVPH-VRDAVWTSLRQADSFADLHYYSNTCRLFRFKDRQEMYVKFK 1895
Cdd:cd08150     82 FFIRNTSDYEDFVAefarsargePPLDFIAWYVEKRPEdLPNLLGARSQVPDSYAAARYFSQVTFAFINGAGKYRVVRSK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1896 LRPSDENIEEDIGKVEpsgilppetgaiprdandTRPLLFLAEDFHNRV-KSPsgVRYIFQLQVRPiPQDEAARDialDC 1974
Cdd:cd08150    162 DNPVDGIPSLEDHELE------------------ARPPDYLREELTERLqRGP--VVYDFRIQLND-DTDATTID---NP 217
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1975 TKPWDESQfPYIDVGEVIINENLTKEGSEKLEVNPFLRCHEVDVIRATSssqsaSIDHGRSLIYEICQHLR 2045
Cdd:cd08150    218 TILWPTEH-PVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLG-----PILEVRRRVYTSSQGLR 282
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
520-991 4.09e-24

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 109.47  E-value: 4.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  520 AVGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIpipVLPPDPL---------- 588
Cdd:PRK05677    45 NLGKTLTYGELYKLSGAFAAWL--QQHTDLKPGDRIA-VQLPNvLQYPVAVFGAMRAGLI---VVNTNPLytaremehqf 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  589 -QRGGQALTKIENIAKLCNAV--------AILSTVG-YHAAVRAGLVKNLISFTGKSVkstgqwpnlPWLHTDSWIKSSK 658
Cdd:PRK05677   119 nDSGAKALVCLANMAHLAEKVlpktgvkhVIVTEVAdMLPPLKRLLINAVVKHVKKMV---------PAYHLPQAVKFND 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  659 VLPA-SNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSN---TVLVSWLPQYHDMGLIGG 733
Cdd:PRK05677   190 ALAKgAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNegcEILIAPLPLYHIYAFTFH 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  734 LFTAMACGGSAILfspltfIRNPL---MWLQTISDYKATHSAGPNFAFELVIRRleadkAKARNYDLSSMIFFMIAAEPV 810
Cdd:PRK05677   270 CMAMMLIGNHNIL------ISNPRdlpAMVKELGKWKFSGFVGLNTLFVALCNN-----EAFRKLDFSALKLTLSGGMAL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  811 RQKTLKRFVELTrpfGLSqevMAPGYGLAENCVFVScaygkkkpilVDWQGRICCGYVDPNDADVDIRIVDaDTGLEVDE 890
Cdd:PRK05677   339 QLATAERWKEVT---GCA---ICEGYGMTETSPVVS----------VNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPL 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  891 dGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGwVIQ--GNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK05677   402 -GEVGELCVKGPQVMKGYWQRPEATDEILDSD-------GWLKTGDIA-LIQedGYMRIVDRKKDMILVSGFNVYPNELE 472
                          490       500
                   ....*....|....*....|...
gi 1917948728  969 KTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK05677   473 DVLAALPGVLQ---CAAIGVPDE 492
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
551-1062 6.20e-24

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: 107.91  E-value: 6.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  551 PGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVL-PPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVKNLI 629
Cdd:cd05922     17 RGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvPLNP----TLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  630 SFTgksvkstgqwpnlpWLHTDSWIKSSKVLPASniafqsESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRR 709
Cdd:cd05922     93 PGT--------------VLDADGIRAARASAPAH------EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  710 YRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFS----PLTFIRnplmwlqTISDYKATHSAGPNFAFELvIRRL 785
Cdd:cd05922    153 LGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNdgvlDDAFWE-------DLREHGATGLAGVPSTYAM-LTRL 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  786 EADKAKarnydLSSMIFFMIAAEPVRQKTLKRFVELTRpfGLSQEVMapgYGLAEncVFVSCAY-----GKKKPilvdwq 860
Cdd:cd05922    224 GFDPAK-----LPSLRYLTQAGGRLPQETIARLRELLP--GAQVYVM---YGQTE--ATRRMTYlpperILEKP------ 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  861 GRICCGYvdPNDAdvdIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWGKEELSQKtfrnklqnyPGRKYTR--TGDLG 938
Cdd:cd05922    286 GSIGLAI--PGGE---FEILDDDGTPT--PPGEPGEIVHRGPNVMKGYWNDPPYRRK---------EGRGGGVlhTGDLA 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  939 WVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCAVIGVPeevlsakgislPDASDEVGLVVIAelrD 1017
Cdd:cd05922    350 RRDEdGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI---IEAAAVGLP-----------DPLGEKLALFVTA---P 412
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1917948728 1018 SKLVNKDIIkqiesRVAEEHGVTVASVKLIRP-RTISKTTSGKIKR 1062
Cdd:cd05922    413 DKIDPKDVL-----RSLAERLPPYKVPATVRVvDELPLTASGKVDY 453
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
526-989 1.10e-23

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: 106.95  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAKlc 605
Cdd:cd05945     18 TYRELKERADALAAALASL---GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER----IREILDAAK-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlPASNIAFqsesqPDDLCFLQFTSGS 685
Cdd:cd05945     89 -------------------------------------------------------PALLIAD-----GDDNAYIIFTSGS 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFsPLTFIRNPLMWLQTISD 765
Cdd:cd05945    109 TGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPV-PRDATADPKQLFRFLAE 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKAT--HSAgPNFAfELVIRRlEADKAKArnydLSSMIFFMIAAEPVRQKTLKRFVELtrpfglsqevmAPG------YG 837
Cdd:cd05945    187 HGITvwVST-PSFA-AMCLLS-PTFTPES----LPSLRHFLFCGEVLPHKTARALQQR-----------FPDariyntYG 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAENCvfVSCAYGKKKPILVDWQGRICCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:cd05945    249 PTEAT--VAVTYIEVTPEVLDGYDRLPIGYAKP---GAKLVILDED-GRPV-PPGEKGELVISGPSVSKGYLNNPEKTAA 321
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728  918 TFRnklqNYPGRKYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCAVIGVP 989
Cdd:cd05945    322 AFF----PDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV---KEAVVVPKY 387
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
672-1035 1.32e-23

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 108.26  E-value: 1.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGS-AILFSPL 750
Cdd:COG1022    181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-ALAAGATvAFAESPD 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFIRN------------PLMW---LQTISDyKATHSAGP-----NFAFELVIRRLEA----------DKAKARNYDLssM 800
Cdd:COG1022    260 TLAEDlrevkptfmlavPRVWekvYAGIQA-KAEEAGGLkrklfRWALAVGRRYARArlagkspsllLRLKHALADK--L 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  801 IFfmiaaEPVRQKT---LKRFV--------ELTRPF---GLsqeVMAPGYGLAENCVFVSC-AYGKKKPILVdwqGRICC 865
Cdd:COG1022    337 VF-----SKLREALggrLRFAVsggaalgpELARFFralGI---PVLEGYGLTETSPVITVnRPGDNRIGTV---GPPLP 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  866 GyvdpndadVDIRIvdadtglevdedGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqnypgrkyT-----RTGDLGWV 940
Cdd:COG1022    406 G--------VEVKI------------AEDGEILVRGPNVMKGYYKNPEATAEAF------------DadgwlHTGDIGEL 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  941 I-QGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---SELL-----RPGCCAVIgVP-----EEVLSAKGISLPDASD 1005
Cdd:COG1022    454 DeDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASpliEQAVvvgdgRPFLAALI-VPdfealGEWAEENGLPYTSYAE 532
                          410       420       430
                   ....*....|....*....|....*....|
gi 1917948728 1006 EVGlvviaelrdsklvNKDIIKQIESRVAE 1035
Cdd:COG1022    533 LAQ-------------DPEVRALIQEEVDR 549
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
526-1062 2.46e-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: 2.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVipiPVLPPDPLQRGGQALTKIENIAKlc 605
Cdd:TIGR01923    1 TWQDLDCEAAHLAKAL---KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGA---EIAMLNTRLTENERTNQLEDLDV-- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhaavraGLVKNLISFTGKSVKSTgqwpNLPWLHTDSwiksskvlpASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:TIGR01923   73 -----------------QLLLTDSLLEEKDFQAD----SLDRIEAAG---------RYETSLSASFNMDQIATLMFTSGT 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFSPLTFIrnplmwLQTISD 765
Cdd:TIGR01923  123 TGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQL------LEMIAN 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATH-SAGPNfafeLVIRRLEADkakARNYDLSSmifFMIAAEPVRQKTLKRFVELTRPFGLsqevmapGYGLAENCVF 844
Cdd:TIGR01923  196 ERVTHiSLVPT----QLNRLLDEG---GHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYL-------SYGMTETCSQ 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  845 VsCAygkkKPILVDwQGRICCGYVDPNdadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklq 924
Cdd:TIGR01923  259 V-TT----ATPEML-HARPDVGRPLAG---REIKI-------KVDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQ--- 319
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  925 nypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevlsakgislpda 1003
Cdd:TIGR01923  320 -----GWFNTGDIGeLDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE---AVVVPKPD------------- 378
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1004 sDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVASVKLirpRTISKTTSGKIKR 1062
Cdd:TIGR01923  379 -AEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKL---DELPYNASGKILR 433
PRK06178 PRK06178
acyl-CoA synthetase; Validated
496-991 5.85e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 105.89  E-value: 5.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  496 YLKHWAaQEITQNKALYTWineggavGCQRTYAELDSNASCVAhKLLTSRKptIKPGDRV--LLVHVPglDFIDAFFGCL 573
Cdd:PRK06178    38 YLRAWA-RERPQRPAIIFY-------GHVITYAELDELSDRFA-ALLRQRG--VGAGDRVavFLPNCP--QFHIVFFGIL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  574 RAKVIPIPVlppDPLQRGGQALTKIeNIAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQwPNLPW------ 647
Cdd:PRK06178   105 KLGAVHVPV---SPLFREHELSYEL-NDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAE-PTLPLpdslra 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  648 --LHTDSWIKSSKVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLI------HNVKLmrrryRSTSNTVL 718
Cdd:PRK06178   180 prLAAAGAIDLLPALRACTAPVPLPPpALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaaYAVAV-----VGGEDSVF 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  719 VSWLPQY----HDMGLIGGLFtamaCGGSAILFS---PLTFirnplmwLQTISDYKATHSAGP-NFAFELVirrleaDKA 790
Cdd:PRK06178   255 LSFLPEFwiagENFGLLFPLF----SGATLVLLArwdAVAF-------MAAVERYRVTRTVMLvDNAVELM------DHP 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  791 KARNYDLSSM-----IFFMIAAEPV-RQktlkRFVELTrpfglsqevmapGYGLAEncvfvsCAYGKKKPILVDwqgRIC 864
Cdd:PRK06178   318 RFAEYDLSSLrqvrvVSFVKKLNPDyRQ----RWRALT------------GSVLAE------AAWGMTETHTCD---TFT 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  865 CGYVDpNDADV--------------DIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrK 930
Cdd:PRK06178   373 AGFQD-DDFDLlsqpvfvglpvpgtEFKICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--------G 442
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728  931 YTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK06178   443 WLHTGDIG-KIdeQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG---SAVVGRPDP 501
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
524-993 2.14e-22

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: 103.56  E-value: 2.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPpdplqrgGQALTKIENIA 602
Cdd:cd05920     40 RLTYRELDRRADRLAAGL---RGLGIRPGDRVV-VQLPnVAEFVVLFFALLRLGAVPVLALP-------SHRRSELSAFC 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 KLCNAVAilstvgYHAAVRAGLVKNLisftgksvkstgqwpnlpwlhtdswiksskvlpasNIAFQS-ESQPDdLCFLQF 681
Cdd:cd05920    109 AHAEAVA------YIVPDRHAGFDHR-----------------------------------ALARELaESIPE-VALFLL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLFTAMACGGSAILFSPLTfirnPLMWL 760
Cdd:cd05920    147 SGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPS----PDAAF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAgpnfafeLV--IRRLEADKAKARNYDLSSMIFFMIAAEPVrQKTLKRFVELTRPFGLsQEVmapgYGL 838
Cdd:cd05920    223 PLIEREGVTVTA-------LVpaLVSLWLDAAASRRADLSSLRLLQVGGARL-SPALARRVPPVLGCTL-QQV----FGM 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  839 AENCVFVScAYGKKKPILVDWQGRiccgyvdPNDADVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYWGKEELSQKT 918
Cdd:cd05920    290 AEGLLNYT-RLDDPDEVIIHTQGR-------PMSPDDEIRVVDEE-GNPVPP-GEEGELLTRGPYTIRGYYRAPEHNARA 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  919 FrnklqNYPGrkYTRTGDLgwvIQ----GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIGVPEE 991
Cdd:cd05920    360 F-----TPDG--FYRTGDL---VRrtpdGYLVVEGRIKDQINRGGEKIAAEEVE------NLLLRhPAVhdAAVVAMPDE 423

                   ..
gi 1917948728  992 VL 993
Cdd:cd05920    424 LL 425
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
526-1064 7.60e-22

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 102.65  E-value: 7.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTK 597
Cdd:PRK08751    52 TYREADQLVEQFAAYLLGELQ--LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPlytPRELKHqlidsGASVLVV 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  598 IENiakLCNAVA-ILSTVGYHAAVRAGL-------VKNLISFTGKSVKSTgqwpnLPWLHTDSWIK--------SSKVLP 661
Cdd:PRK08751   130 IDN---FGTTVQqVIADTPVKQVITTGLgdmlgfpKAALVNFVVKYVKKL-----VPEYRINGAIRfrealalgRKHSMP 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  662 ASNIAfqsesqPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS-----NTVLVSWLPQYHDMGLIGGLFT 736
Cdd:PRK08751   202 TLQIE------PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleegCEVVITALPLYHIFALTANGLV 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  737 AMACGGSAILFS-PltfiRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTL 815
Cdd:PRK08751   276 FMKIGGCNHLISnP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVA 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  816 KRFVELTrpfGLSqevMAPGYGLAEncvfVSCAYGKKKPILVDWQGRIccGYVDPNdADVDIRIvDADTGLEVdedGKEG 895
Cdd:PRK08751   347 ERWKQVT---GLT---LVEAYGLTE----TSPAACINPLTLKEYNGSI--GLPIPS-TDACIKD-DAGTVLAI---GEIG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  896 EIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESS 974
Cdd:PRK08751   410 ELCIKGPQVMKGYWKRPEETAKVM-------DADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  975 SELLRpgcCAVIGVPEEvlsakgislpdASDEVGLVVIAElRDSKLVNKDIikqiesrvaEEHGVT-VASVKLIR----P 1049
Cdd:PRK08751   483 PGVLE---VAAVGVPDE-----------KSGEIVKVVIVK-KDPALTAEDV---------KAHARAnLTGYKQPRiiefR 538
                          570
                   ....*....|....*
gi 1917948728 1050 RTISKTTSGKIKRFE 1064
Cdd:PRK08751   539 KELPKTNVGKILRRE 553
PRK09274 PRK09274
peptide synthase; Provisional
500-1050 1.11e-21

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 101.90  E-value: 1.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  500 WAAQEITQNKALY---TWINEGGAVGCQRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:PRK09274    14 RAAQERPDQLAVAvpgGRGADGKLAYDELSFAELDARSDAIAHGLNAA---GIGRGMRAVLMVTPSLEFFALTFALFKAG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  577 VIPIPVlppDPlqrgGQAltkIENIAKlcnavaILSTVGYHAAV---RAGLVKNLISFTGKSVK---STGQwpnlpwlht 650
Cdd:PRK09274    91 AVPVLV---DP----GMG---IKNLKQ------CLAEAQPDAFIgipKAHLARRLFGWGKPSVRrlvTVGG--------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  651 dSWIKSSKVL-----PASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQ 724
Cdd:PRK09274   146 -RLLWGGTTLatllrDGAAAPFPmADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  725 YhdmgligGLFtAMACGGSAILfSPLTFIR----NPLMWLQTISDYKATHSAGpNFAfelVIRRLeADKAKARNYDLSSM 800
Cdd:PRK09274   225 F-------ALF-GPALGMTSVI-PDMDPTRpatvDPAKLFAAIERYGVTNLFG-SPA---LLERL-GRYGEANGIKLPSL 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  801 IFFMIAAEPVRQKTLKRFVELTRPFGlsqEVMAPgYGLAEncVFVSCAYGKKKPILVDWQ-----GRICCGYVDPndaDV 875
Cdd:PRK09274   291 RRVISAGAPVPIAVIERFRAMLPPDA---EILTP-YGATE--ALPISSIESREILFATRAatdngAGICVGRPVD---GV 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  876 DIRIVDADTGL--EVDED-----GKEGEIWISSPSAGIGYWGKEELSQKtfrNKLQNYPGRKYTRTGDLGWV-IQGNLFI 947
Cdd:PRK09274   362 EVRIIAISDAPipEWDDAlrlatGEIGEIVVAGPMVTRSYYNRPEATRL---AKIPDGQGDVWHRMGDLGYLdAQGRLWF 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevlsaKGISLPdasdevglVVIAELRDSKLVNKDIIK 1027
Cdd:PRK09274   439 CGRKAHRVETAGGTLYTIPCERIFNTHPGVKR---SALVGVGV-----PGAQRP--------VLCVELEPGVACSKSALY 502
                          570       580
                   ....*....|....*....|....*.
gi 1917948728 1028 QiESRV-AEEHGVTvASVK--LIRPR 1050
Cdd:PRK09274   503 Q-ELRAlAAAHPHT-AGIErfLIHPS 526
PRK07514 PRK07514
malonyl-CoA synthase; Validated
672-1034 1.33e-21

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 101.11  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FS 748
Cdd:PRK07514   154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFlpkFD 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  749 PLTFIRnpLMwlqtisdYKATHSAG-PNFafelVIRRLEA---DKAKARNydlssMIFFMIAAEPVRQKTLKRFVELT-- 822
Cdd:PRK07514   234 PDAVLA--LM-------PRATVMMGvPTF----YTRLLQEprlTREAAAH-----MRLFISGSAPLLAETHREFQERTgh 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  823 ----RpfglsqevmapgYGLAENCVFVSCAY-GKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVdEDGKEGEI 897
Cdd:PRK07514   296 aileR------------YGMTETNMNTSNPYdGERRA-----------GTVGFPLPGVSLRVTDPETGAEL-PPGEIGMI 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  898 WISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEK------- 969
Cdd:PRK07514   352 EVKGPNVFKGYWRMPEKTAEEFRAD-------GFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGeidelpg 424
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728  970 TVESssellrpgccAVIGVPEevlsakgislPDASDEVGLVVIAElRDSKLVNKDIIKQIESRVA 1034
Cdd:PRK07514   425 VVES----------AVIGVPH----------PDFGEGVTAVVVPK-PGAALDEAAILAALKGRLA 468
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
521-991 1.44e-21

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 101.44  E-value: 1.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  521 VGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIpipVLPPDPL----------- 588
Cdd:PRK12492    46 LGVTLSYAELERHSAAFAAYL--QQHTDLVPGDRIA-VQMPNvLQYPIAVFGALRAGLI---VVNTNPLytaremrhqfk 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  589 QRGGQALTKIENIAKLCNAVAILSTVGYHAAVRAG---------LVKNLISFTGKSVkstgqwpnlPWLHTDSWIKSSKV 659
Cdd:PRK12492   120 DSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGdllpaakgwLVNTVVDKVKKMV---------PAYHLPQAVPFKQA 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  660 LP-ASNIAFQSESQP-DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRST----------SNTVLVSWLPQYHD 727
Cdd:PRK12492   191 LRqGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEVMIAPLPLYHI 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  728 MGLIGGLFTAMACGGSAILfspLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIrrleaDKAKARNYDLSSMIFFMIAA 807
Cdd:PRK12492   271 YAFTANCMCMMVSGNHNVL---ITNPRDIPGFIKELGKWRFSALLGLNTLFVALM-----DHPGFKDLDFSALKLTNSGG 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  808 EPVRQKTLKRFVELTrpfGLSqevMAPGYGLAEnCVFVSCA--YGKkkpilvdwQGRIccGYVDPNDADVDIRIVDaDTG 885
Cdd:PRK12492   343 TALVKATAERWEQLT---GCT---IVEGYGLTE-TSPVASTnpYGE--------LARL--GTVGIPVPGTALKVID-DDG 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  886 LEVDEdGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGwVIQGNLF--ITGRIKDLIIVAGRNIY 963
Cdd:PRK12492   405 NELPL-GERGELCIKGPQVMKGYWQQPEATAEAL-------DAEGWFKTGDIA-VIDPDGFvrIVDRKKDLIIVSGFNVY 475
                          490       500
                   ....*....|....*....|....*...
gi 1917948728  964 SADVEKTVESSSELlrpGCCAVIGVPEE 991
Cdd:PRK12492   476 PNEIEDVVMAHPKV---ANCAAIGVPDE 500
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
526-992 4.11e-21

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 99.96  E-value: 4.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIpipVLPPDPlqrggqALTKIENIAKL- 604
Cdd:PRK05852    45 SYRDLARLVDDLAGQL---TRSGLLPGDRVALRMGSNAEFVVALLAASRADLV---VVPLDP------ALPIAEQRVRSq 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 ---CNAVAILST-VGYHAAVRAGLVKNLISFTGksvkSTGQWPNLPWLHTDSwikssKVLPASNIAFQSESQPDDlCFLQ 680
Cdd:PRK05852   113 aagARVVLIDADgPHDRAEPTTRWWPLTVNVGG----DSGPSGGTLSVHLDA-----ATEPTPATSTPEGLRPDD-AMIM 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL-----FSPLTFirn 755
Cdd:PRK05852   183 FTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpargrFSAHTF--- 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  756 plmWlQTISDYKAT-HSAGPNFaFELVIRRLEADKAKARNYDLSsmiFFMIAAEPVRQKTLKrfveltrpfGLSQEVMAP 834
Cdd:PRK05852   260 ---W-DDIKAVGATwYTAVPTI-HQILLERAATEPSGRKPAALR---FIRSCSAPLTAETAQ---------ALQTEFAAP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 gyglaencvfVSCAYGKKKPI------LVDWQGR-----ICCGYVDPNDAdVDIRIVDADtGLEVDEDgKEGEIWISSPS 903
Cdd:PRK05852   323 ----------VVCAFGMTEAThqvtttQIEGIGQtenpvVSTGLVGRSTG-AQIRIVGSD-GLPLPAG-AVGEVWLRGTT 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  904 AGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgc 982
Cdd:PRK05852   390 VVRGYLGDPTITAANFTDG--------WLRTGDLGSLSAaGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME--- 458
                          490
                   ....*....|
gi 1917948728  983 CAVIGVPEEV 992
Cdd:PRK05852   459 AAVFGVPDQL 468
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
1229-1686 6.24e-21

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: 100.21  E-value: 6.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1229 RIWSFQLLALLYISFILVFPAYLSISTFQILVSASHKLIDGLPWLHQASVVLLAPLSWILCIALTSISIAFFGNSFLRIN 1308
Cdd:TIGR02353  229 RRRLYVAGALFVVFVLLPPLAFLFAIPVAITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNLVLK 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1309 YALTPEVSVWsvdfvkWWALYKAQEV--SSKVLAVHLRGTVFLKHWFEMLGARIGSSVLLDTVDITDPSLVSIGDGAVIA 1386
Cdd:TIGR02353  309 PGRYYVHSGF------YYQAWTVQQLmdNSRVLLFPLYASSYIPHWYRALGAKIGKVAEISSAQHEVPDLTDIGEETFIA 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1387 EGALLQSHEVRNSILRLQPIRIGRNCSVGPYAVVQKGSVLREGAEVpalqkseGGKSAL----KMAKAENILKVSPGTLK 1462
Cdd:TIGR02353  383 DGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLL-------GVLSMTpkdgKVREGVGWLGSPPFELP 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1463 TVQQfmgiyVVGFLSSL-SAATVYLLYMSLSqkVPSLELLAFLCISGALHWVPFTIVAYATMFTKAppNPFEFAISLAIA 1541
Cdd:TIGR02353  456 RRVN-----RDDELEALtFEPDPRRRLARKN--VENLRIILPFLLVQWAMLFALVVLDLQALDDYT--EWGAVALLAALI 526
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1542 YFAHGLVLSLLTSIFTHLLAGKEKKTQTHIKTWF--GHQLAIA-----CHVRFAKLLSGTEAFCMYLRLLGAKVGRYCSI 1614
Cdd:TIGR02353  527 LMAVGVGAFLILVERKWLVFGRLKPQEHPLWSPFvwLHELHWKlyesvAVPNFLRPFRGTPFLPAILRLLGVKIGRGVYI 606
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1615 RAINpIADPRMVSIGAGVHLGDFSRIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISV 1686
Cdd:TIGR02353  607 DGTD-LTERDLVTIGDDSTLNEGSVIQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
681-1062 1.47e-20

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: 95.41  E-value: 1.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLfTAMACGGSAILFSPLTFIRNPLMW 759
Cdd:cd17635      8 FTSGTTGEPKAVLLANKTFFaVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTTYKSLFKI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  760 LQTisdYKATHSA-GPNFAFELVirrLEADKAKARNYDLSSMIF---FMIAAEpvrqktlKRFVELtrpFGLSQEVMApg 835
Cdd:cd17635     87 LTT---NAVTTTClVPTLLSKLV---SELKSANATVPSLRLIGYggsRAIAAD-------VRFIEA---TGLTNTAQV-- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  836 YGLAENCVFVSCAYGKkkpilvdwqGRICCGYVDPNDADVDIRIVDADtGLEVDEDGkEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd17635    149 YGLSETGTALCLPTDD---------DSIEINAVGRPYPGVDVYLAATD-GIAGPSAS-FGTIWIKSPANMLGYWNNPERT 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  916 QKTFRNKlqnypgrkYTRTGDLGWVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVESssellrpgccaVIGVPEevls 994
Cdd:cd17635    218 AEVLIDG--------WVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEG-----------VSGVQE---- 274
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728  995 AKGISLPDAsdEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGvtvasvKLIRPRTIS------KTTSGKIKR 1062
Cdd:cd17635    275 CACYEISDE--EFGELVGLAVVASAELDENAIRALKHTIRRELE------PYARPSTIVivtdipRTQSGKVKR 340
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
526-1018 2.41e-20

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: 96.96  E-value: 2.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkienia 602
Cdd:cd12114     14 TYGELAERARRVAGAL---KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVdidQPAARREA------------ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  603 klcnavaILSTVGYHAAVRAGlvknlisftgksvkstGQWPNLPWLHTDSwIKSSKVLPASNIAFQSESQPDDLCFLQFT 682
Cdd:cd12114     79 -------ILADAGARLVLTDG----------------PDAQLDVAVFDVL-ILDLDALAAPAPPPPVDVAPDDLAYVIFT 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  683 SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:cd12114    135 SGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDEAR-RRDPAHWAEL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYKATHSagpNFA---FELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQ---KTLKRFVELTRPFGLSqevmapgy 836
Cdd:cd12114    213 IERHGVTLW---NSVpalLEMLLDVLEAAQA-----LLPSLRLVLLSGDWIPLdlpARLRALAPDARLISLG-------- 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  837 GLAENCVFvSCAYgKKKPILVDWqGRICCGYVDPNDAdvdIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd12114    277 GATEASIW-SIYH-PIDEVPPDW-RSIPYGRPLANQR---YRVLDPR-GRDC-PDWVPGELWIGGRGVALGYLGDPELTA 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  917 KTFrnkLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpGCCAVIGVPEE---- 991
Cdd:cd12114    349 ARF---VTHPDGERLYRTGDLGrYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR-AVVVVLGDPGGkrla 424
                          490       500
                   ....*....|....*....|....*...
gi 1917948728  992 -VLSAKGISLPDASDEVGLVVIAELRDS 1018
Cdd:cd12114    425 aFVVPDNDGTPIAPDALRAFLAQTLPAY 452
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
673-1060 3.34e-20

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: 94.85  E-value: 3.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTF 752
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 iRNPLM----WlQTISDYKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGLS 828
Cdd:cd05944     81 -RNPGLfdnfW-KLVERYRIT-------SLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDAT---GLP 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  829 qevMAPGYGLAENCVFVSCAY--GKKKPilvdwqGRIccGYVDPNdADVDIRIVDADTGLEVDEDGKE-GEIWISSPSAG 905
Cdd:cd05944    149 ---VVEGYGLTEATCLVAVNPpdGPKRP------GSV--GLRLPY-ARVRIKVLDGVGRLLRDCAPDEvGEICVAGPGVF 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 IGYWGKEelsqktfrNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCA 984
Cdd:cd05944    217 GGYLYTE--------GNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV---AFAG 285
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  985 VIGVPEevlsAKGISLPdasdeVGLVVIAelRDSKLVNKDIIKQIESRVAEEHGVTVAsVKLIRPrtISKTTSGKI 1060
Cdd:cd05944    286 AVGQPD----AHAGELP-----VAYVQLK--PGAVVEEEELLAWARDHVPERAAVPKH-IEVLEE--LPVTAVGKV 347
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
666-991 5.87e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 96.38  E-value: 5.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  666 AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACgGSAI 745
Cdd:PRK12583   193 ERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTV-GACL 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  746 LFSPLTFirNPLMWLQTISDYKAT--HSAGPNFAFELvirrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFV-ELT 822
Cdd:PRK12583   272 VYPNEAF--DPLATLQAVEEERCTalYGVPTMFIAEL-------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMdEMH 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  823 RPfglsqEVMApGYGLAENC-VFVSCAYGKKKPILVDWQGRiccgyvdpNDADVDIRIVDADTglEVDEDGKEGEIWISS 901
Cdd:PRK12583   343 MA-----EVQI-AYGMTETSpVSLQTTAADDLERRVETVGR--------TQPHLEVKVVDPDG--ATVPRGEIGELCTRG 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  902 PSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRp 980
Cdd:PRK12583   407 YSVMKGYWNNPEATAESI-------DEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD- 478
                          330
                   ....*....|.
gi 1917948728  981 gcCAVIGVPEE 991
Cdd:PRK12583   479 --VQVFGVPDE 487
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
522-1062 9.90e-20

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: 95.10  E-value: 9.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENI 601
Cdd:cd17651     18 GRRLTYAELDRRANRLAHRL---RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER-------LAFM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILStvgyHAAVRAGLVknlisftgksvkstgqwPNLPWLHTDSWIKSSKVLPASNIAfqsESQPDDLCFLQF 681
Cdd:cd17651     88 LADAGPVLVLT----HPALAGELA-----------------VELVAVTLLDQPGAAAGADAEPDP---ALDADDLAYVIY 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAIL------FSPLTFIRn 755
Cdd:cd17651    144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLppeevrTDPPALAA- 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  756 plmWLQTisdYKATHSAGPNFAFELVIrrLEADKAKARNYDLSSMIffmIAAEPVRQKTLKRfvELTRpfGLSQEVMAPG 835
Cdd:cd17651    222 ---WLDE---QRISRVFLPTVALRALA--EHGRPLGVRLAALRYLL---TGGEQLVLTEDLR--EFCA--GLPGLRLHNH 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  836 YGLAENCVfVSC--------AYGKKKPIlvdwqGRiccgyvdPNDaDVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIG 907
Cdd:cd17651    287 YGPTETHV-VTAlslpgdpaAWPAPPPI-----GR-------PID-NTRVYVLDAA--LRPVPPGVPGELYIGGAGLARG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  908 YWGKEELSQKTFRnKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLRpgccaVI 986
Cdd:cd17651    351 YLNRPELTAERFV-PDPFVPGARMYRTGDLArWLPDGELEFLGRADDQVKIRGFRIELGEIE------AALAR-----HP 418
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728  987 GVPEEVLSAKgislPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVASVKLIR-PRtiskTTSGKIKR 1062
Cdd:cd17651    419 GVREAVVLAR----EDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDAlPL----TPNGKLDR 487
PRK06188 PRK06188
acyl-CoA synthetase; Validated
669-991 1.21e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 95.44  E-value: 1.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  669 SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTA--MACGGSAIL 746
Cdd:PRK06188   163 AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AGGAFFLptLLRGGTVIV 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 ---FSPLTFIRnplmwlqTISDYKAThsagpnFAFeLV---IRRLeADKAKARNYDLSSMIFFMIAAEPVrqkTLKRFVE 820
Cdd:PRK06188   239 lakFDPAEVLR-------AIEEQRIT------ATF-LVptmIYAL-LDHPDLRTRDLSSLETVYYGASPM---SPVRLAE 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  821 LTRPFGlsqEVMAPGYGLAEnCVFVSCAYGKKKPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVDEdGKEGEIWIS 900
Cdd:PRK06188   301 AIERFG---PIFAQYYGQTE-APMVITYLRKRDHDPDDPKRLTSCGRPTPG---LRVALLDED-GREVAQ-GEVGEICVR 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  901 SPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlr 979
Cdd:PRK06188   372 GPLVMDGYWNRPEETAEAFRDG--------WLHTGDVAREDEdGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV-- 441
                          330
                   ....*....|..
gi 1917948728  980 pGCCAVIGVPEE 991
Cdd:PRK06188   442 -AQVAVIGVPDE 452
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
675-1017 1.54e-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: 92.18  E-value: 1.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLI-------HNVKLmrrryRSTSNTVLVSwlPQYHDMGLIGGLFTAMACGgsAILF 747
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaaawaDCADL-----TEDDRYLIIN--PFFHTFGYKAGIVACLLTG--ATVV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 SPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIrrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEltrpfGL 827
Cdd:cd17638     72 PVAVF--DVDAILEAIERERITVLPGPPTLFQSLL-----DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----EL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  828 SQEVMAPGYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDAdtglevdedgkeGEIWISSPSAGIG 907
Cdd:cd17638    140 GFETVLTAYGLTEAGVATMCRPGDDAETVATTCGRAC--------PGFEVRIADD------------GEVLVRGYNVMQG 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  908 YWGKEELSQKTFrnklqnyPGRKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVI 986
Cdd:cd17638    200 YLDDPEATAEAI-------DADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGAL---AEHPGVAQVAVI 269
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1917948728  987 GVPEEVLSAKGISLPDASDEVGLV---VIAELRD 1017
Cdd:cd17638    270 GVPDERMGEVGKAFVVARPGVTLTeedVIAWCRE 303
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
679-1064 1.92e-19

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: 94.29  E-value: 1.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  679 LQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILfspLTFIRNPLM 758
Cdd:cd12118    138 LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGW-CFPWTVAAVGGTNVC---LRKVDAKAI 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 WlQTISDYKATH-SAGPnfafelVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfGLSqevMAPGYG 837
Cdd:cd12118    214 Y-DLIEKHKVTHfCGAP------TVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL----GFD---VTHVYG 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAEncvfvscAYGkkkPILV-DWQ---------------GRICCGYVDPNDADVdiriVDADTGLEVDEDGKE-GEIWIS 900
Cdd:cd12118    280 LTE-------TYG---PATVcAWKpewdelpteerarlkARQGVRYVGLEEVDV----LDPETMKPVPRDGKTiGEIVFR 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  901 SPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGwVIQ--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELL 978
Cdd:cd12118    346 GNIVMKGYLKNPEATAEAFRG--------GWFHSGDLA-VIHpdGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVL 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  979 RpgcCAVIGVPEEVLsakgislpdasdevGLVVIA--ELRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS-- 1053
Cdd:cd12118    417 E---AAVVARPDEKW--------------GEVPCAfvELKEGAKVTeEEIIAFCREHLA----------GFMVPKTVVfg 469
                          410
                   ....*....|....
gi 1917948728 1054 ---KTTSGKIKRFE 1064
Cdd:cd12118    470 elpKTSTGKIQKFV 483
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
674-1081 2.29e-19

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: 95.07  E-value: 2.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 DDLCFLqFTSGSTSDAKGVMITHGGliHNVKL---MRRRYRSTSNTVLvsWLPQyhDMGLIGG----LFTAMACGGSAIL 746
Cdd:cd05967    231 DPLYIL-YTSGTTGKPKGVVRDNGG--HAVALnwsMRNIYGIKPGDVW--WAAS--DVGWVVGhsyiVYGPLLHGATTVL 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 FSPL-TFIRNPLMWLQTISDYKATH--SAgPNfAFElVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKrFVE--L 821
Cdd:cd05967    304 YEGKpVGTPDPGAFWRVIEKYQVNAlfTA-PT-AIR-AIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLE-WAEntL 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  822 TRPfglsqeVM------APGYGLAENCVFVSCaygkkKPILVDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEG 895
Cdd:cd05967    380 GVP------VIdhwwqtETGWPITANPVGLEP-----LPIKAGSPGKPVPGY--------QVQVLDED-GEPV-GPNELG 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  896 EIWIS---SPSAGIGYWGKEELSQKTFrnkLQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTV 971
Cdd:cd05967    439 NIVIKlplPPGCLLTLWKNDERFKKLY---LSKFPG--YYDTGDAGYKDEdGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  972 essseLLRPGC--CAVIGVPEEVlsaKGislpdaSDEVGLVVIAElrDSKLVNKDIIKQIESRVAEEHGvTVASVKL-IR 1048
Cdd:cd05967    514 -----LSHPAVaeCAVVGVRDEL---KG------QVPLGLVVLKE--GVKITAEELEKELVALVREQIG-PVAAFRLvIF 576
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1917948728 1049 PRTISKTTSGKIKRfECLKQFVDGNLNTVPDPI 1081
Cdd:cd05967    577 VKRLPKTRSGKILR-RTLRKIADGEDYTIPSTI 608
PLN02574 PLN02574
4-coumarate--CoA ligase-like
526-1064 2.41e-19

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 94.52  E-value: 2.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltSRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIpipVLPPDPLQRGGQALTKIENIAkLC 605
Cdd:PLN02574    68 SYSELQPLVKSMAAGL--YHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI---VTTMNPSSSLGEIKKRVVDCS-VG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAG--LVKNLISFTGKSVkstgQWPNLPWLhtdsWIKSSKVLPASNIafqsesQPDDLCFLQFTS 683
Cdd:PLN02574   142 LAFTSPENVEKLSPLGVPviGVPENYDFDSKRI----EFPKFYEL----IKEDFDFVPKPVI------KQDDVAAIMYSS 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRR------RYRSTSNTVLVSwLPQYHDMGLigGLF-TAMACGGSAILFSPlTFIRNP 756
Cdd:PLN02574   208 GTTGASKGVVLTHRNLIAMVELFVRfeasqyEYPGSDNVYLAA-LPMFHIYGL--SLFvVGLLSLGSTIVVMR-RFDASD 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  757 LmwLQTISDYKATHsagpnfaFELVIRRLEADKAKARNY---DLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevma 833
Cdd:PLN02574   284 M--VKVIDRFKVTH-------FPVVPPILMALTKKAKGVcgeVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ---- 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  834 pGYGLAENCVFVSCAYGKKKpilvdWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:PLN02574   351 -GYGMTESTAVGTRGFNTEK-----LSKYSSVGLLAPN---MQAKVVDWSTGCLL-PPGNCGELWIQGPGVMKGYLNNPK 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  914 LSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEv 992
Cdd:PLN02574   421 ATQSTIDKD-------GWLRTGDIAYFDEdGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIID---AAVTAVPDK- 489
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728  993 lsakgislpdASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTvasvKLIRPRTISKTTSGKIKRFE 1064
Cdd:PLN02574   490 ----------ECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVR----KVVFVQSIPKSPAGKILRRE 547
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
662-1062 6.24e-19

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 93.12  E-value: 6.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  662 ASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMA 739
Cdd:PLN02330   172 AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLR 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  740 CGGSAILFSPLTfirnplmwLQTISDYKATHSAGPNFAFELVIRRLEADKAkARNYDLSSMIF--FMIAAEPVRQKTLKR 817
Cdd:PLN02330   252 NKGKVVVMSRFE--------LRTFLNALITQEVSFAPIVPPIILNLVKNPI-VEEFDLSKLKLqaIMTAAAPLAPELLTA 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  818 FvELTRPFGLSQEvmapGYGLAE-NCVFVSCAYGKKKpilvdwQG---RICCGYVDPNdadVDIRIVDADTGLEVDEDgK 893
Cdd:PLN02330   323 F-EAKFPGVQVQE----AYGLTEhSCITLTHGDPEKG------HGiakKNSVGFILPN---LEVKFIDPDTGRSLPKN-T 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  894 EGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVe 972
Cdd:PLN02330   388 PGELCVRSQCVMQGYYNNKEETDRTIDED-------GWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAIL- 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  973 ssseLLRPGC--CAVIGVPEEvlsaKGISLPDASdevglVVIAelRDSKLVNKDIIKQIESRVAeeHGVTVASVKLIrpR 1050
Cdd:PLN02330   460 ----LTHPSVedAAVVPLPDE----EAGEIPAAC-----VVIN--PKAKESEEDILNFVAANVA--HYKKVRVVQFV--D 520
                          410
                   ....*....|..
gi 1917948728 1051 TISKTTSGKIKR 1062
Cdd:PLN02330   521 SIPKSLSGKIMR 532
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
522-1063 7.79e-19

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 92.90  E-value: 7.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGGQaltkIENI 601
Cdd:PRK06155    44 GTRWTYAEAARAAAAAAHAL---AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI---NTALRGPQ----LEHI 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILSTVGYHAAVRAGLVKNLisftgkSVKSTGQWPNLPWLHTDSWIKSSKVLPASNIAFQSESQPDDLCFLQF 681
Cdd:PRK06155   114 LRNSGARLLVVEAALLAALEAADPGDL------PLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAILY 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAIL---FSPLTFirnplm 758
Cdd:PRK06155   188 TSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLeprFSASGF------ 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 WlqtisDYKATHSAGPNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPvrqktlKRFVELTRPFGLSqevMAPGYGL 838
Cdd:PRK06155   261 W-----PAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA------ALHAAFRERFGVD---LLDGYGS 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  839 AENCVFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISS--PSA-GIGYWGKEELS 915
Cdd:PRK06155   327 TETNFVIAVTHGSQRP---GSMGRLAPGF--------EARVVDEH-DQEL-PDGEPGELLLRAdePFAfATGYFGMPEKT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  916 QKTFRNkLQNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:PRK06155   394 VEAWRN-LWFHTGDRVVRDAD------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA---AAVFPVPSEL--- 460
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728  996 kgislpdASDEVGLVVIaeLRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKIKRF 1063
Cdd:PRK06155   461 -------GEDEVMAAVV--LRDGTALEpVALVRHCEPRLA----------YFAVPRYVEfvaalpKTENGKVQKF 516
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
690-989 8.97e-19

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: 90.02  E-value: 8.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  690 KGVMITHGGLIH-NVKLMRRrYRSTSNTVLVSWLPQYHdmglIGGLFTAMAC---GGSAILFSPLtfirNPLMWLQTISD 765
Cdd:cd17637     16 RGAVLSHGNLIAaNLQLIHA-MGLTEADVYLNMLPLFH----IAGLNLALATfhaGGANVVMEKF----DPAEALELIEE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATHSagpnFAFELVIRRLEaDKAKARNYDLSSM--IFFMIAAEpvrqkTLKRFVELTRPFGLSqevmapGYGLAENCV 843
Cdd:cd17637     87 EKVTLM----GSFPPILSNLL-DAAEKSGVDLSSLrhVLGLDAPE-----TIQRFEETTGATFWS------LYGQTETSG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  844 FVSCAYGKKKPilvdwqGriCCGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNkl 923
Cdd:cd17637    151 LVTLSPYRERP------G--SAGRPGPL---VRVRIVD-DNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-- 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728  924 qnypgrKYTRTGDLGWV-IQGNLFITGRI--KDLIIVAGRNIYSADVEKTVessseLLRPGCCA--VIGVP 989
Cdd:cd17637    216 ------GWHHTGDLGRFdEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVI-----LEHPAIAEvcVIGVP 275
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
673-1063 1.15e-18

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 92.42  E-value: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltf 752
Cdd:PRK13295   196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---- 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 IRNPLMWLQTISDYKATHSAGPN-FAFELvirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRfveLTRPFGLSqev 831
Cdd:PRK13295   272 IWDPARAAELIRTEGVTFTMASTpFLTDL------TRAVKESGRPVSSLRTFLCAGAPIPGALVER---ARAALGAK--- 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  832 MAPGYGLAENCVFVSCAYGK--KKPILVDwqgriccGYVDPNdadVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYW 909
Cdd:PRK13295   340 IVSAWGMTENGAVTLTKLDDpdERASTTD-------GCPLPG---VEVRVVDAD-GAPLPA-GQIGRLQVRGCSNFGGYL 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  910 GKEELSQKTFRNklqnypgrkYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:PRK13295   408 KRPQLNGTDADG---------WFDTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ---VAIVAY 475
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728  989 PEEVLS--AKGISLPDASDEVGLVVIAELRDSKLVNKDIIKQiesrvaeehgvtvasvKLIRPRTISKTTSGKIKRF 1063
Cdd:PRK13295   476 PDERLGerACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIPE----------------RLVVRDALPRTPSGKIQKF 536
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
524-968 1.57e-18

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: 91.62  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAK 603
Cdd:cd17655     22 TLTYRELNERANQLARTL---REKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER-------IQYILE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 LCNAVAILSTvgyhaavraGLVKNLISFTGKSVKSTGQwpnlpwlhtDSWIKSSKVLPAsniafqsESQPDDLCFLQFTS 683
Cdd:cd17655     92 DSGADILLTQ---------SHLQPPIAFIGLIDLLDED---------TIYHEESENLEP-------VSKSDDLAYVIYTS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILfSPLTFIRNPLMWLQTI 763
Cdd:cd17655    147 GSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDAS-VTEIFASLLSGNTLYI-VRKETVLDGQALTQYI 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  764 SDYKATHSAGPNFAFELVirrleadkAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSQEVMApGYGLAENCv 843
Cdd:cd17655    225 RQNRITIIDLTPAHLKLL--------DAADDSEGLSLKHLIVGGEALSTELAKKIIEL---FGTNPTITN-AYGPTETT- 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  844 fVSCAYGKKKPiLVDWQGRICCGyvdpnDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFrnkL 923
Cdd:cd17655    292 -VDASIYQYEP-ETDQQVSVPIG-----KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKF---V 361
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1917948728  924 QN--YPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17655    362 DDpfVPGERMYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGEIE 409
PLN02246 PLN02246
4-coumarate--CoA ligase
519-1062 2.21e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 91.20  E-value: 2.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  519 GAVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRakvipipvlppdplqRGGQALT-- 596
Cdd:PLN02246    45 GATGRVYTYADVELLSRRVAAGL---HKLGIRQGDVVMLLLPNCPEFVLAFLGASR---------------RGAVTTTan 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  597 ------KIENIAKLCNAVAILSTVGYhaavrAGLVKNLISFTGKSVKSTGQwpnlpwlHTDSWIKSSKVLPASNIAF-QS 669
Cdd:PLN02246   107 pfytpaEIAKQAKASGAKLIITQSCY-----VDKLKGLAEDDGVTVVTIDD-------PPEGCLHFSELTQADENELpEV 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM----RRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMACG---G 742
Cdd:PLN02246   175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGlrvG 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  743 SAILFSPlTFIRNPLMWLqtISDYKAThsAGPnFAFELVIrrleadkAKARN-----YDLSSMIFFMIAAEPVRQktlkr 817
Cdd:PLN02246   251 AAILIMP-KFEIGALLEL--IQRHKVT--IAP-FVPPIVL-------AIAKSpvvekYDLSSIRMVLSGAAPLGK----- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  818 fvELTRPFG--LSQEVMAPGYGLAE-NCVFVSCAYGKKKPILVDwQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKE 894
Cdd:PLN02246   313 --ELEDAFRakLPNAVLGQGYGMTEaGPVLAMCLAFAKEPFPVK-SG--SCGTVVRN---AELKIVDPETGASLPR-NQP 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:PLN02246   384 GEICIRGPQIMKGYLNDPEATANTIDKD-------GWLHTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLIS 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  974 SSELLRpgcCAVIGVPEEVLSakgiSLPdasdeVGLVVIAElrDSKlVNKDIIKQIesrVAEEhgvtVASVKLIRP---- 1049
Cdd:PLN02246   457 HPSIAD---AAVVPMKDEVAG----EVP-----VAFVVRSN--GSE-ITEDEIKQF---VAKQ----VVFYKRIHKvffv 514
                          570
                   ....*....|...
gi 1917948728 1050 RTISKTTSGKIKR 1062
Cdd:PLN02246   515 DSIPKAPSGKILR 527
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
526-1063 5.18e-18

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: 89.46  E-value: 5.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPdpLQRGgqALTKIenIAKLC 605
Cdd:cd05958     12 TYRDLLALANRIANVLVG--ELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPL--LRPK--ELAYI--LDKAR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafQSESQPDDLCFLQFTSGS 685
Cdd:cd05958     84 ITVALCA-------------------------------------------------------HALTASDDICILAFTSGT 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHggliHNVKLMRRRY-----RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTfirnPLMWL 760
Cdd:cd05958    109 TGAPKATMHFH----RDPLASADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT----PDLLL 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAGPNFAFelvirRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGLsqEVMaPGYGLAE 840
Cdd:cd05958    181 SAIARYKPTVLFTAPTAY-----RAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT---GI--PII-DGIGSTE 249
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISSPSagiGYWGKEELSQKTF 919
Cdd:cd05958    250 MFhIFISARPGDARP---GATGKPVPGY--------EAKVVDDE-GNPV-PDGTIGRLAVRGPT---GCRYLADKRQRTY 313
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  920 RNKLQNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPeevlsakg 997
Cdd:cd05958    314 VQGGWNITGDTYSRDPD------GYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVaeCAVVGHP-------- 374
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728  998 islpdasDEVGLVVIAE---LRDSKLVNKDIIKQIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRF 1063
Cdd:cd05958    375 -------DESRGVVVKAfvvLRPGVIPGPVLARELQDHAKAH----IAPYK--YPRAIEfvtelpRTATGKLQRF 436
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
674-1064 7.45e-18

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: 88.93  E-value: 7.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 DDLCFLQFTSGSTSDAKGVMITH---------GGLIHNVKlMRRRYRSTSNTvlvSWLpqyhdMGLIGGLFTAMACGGSA 744
Cdd:cd05972     81 EDPALIYFTSGTTGLPKGVLHTHsyplghiptAAYWLGLR-PDDIHWNIADP---GWA-----KGAWSSFFGPWLLGATV 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  745 ILFSPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkakarNYDLSSMIFFMIAAEPVRQKTLKRFVEltrP 824
Cdd:cd05972    152 FVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS------SYKFSHLRLVVSAGEPLNPEVIEWWRA---A 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  825 FGLSqevMAPGYGLAENCVFVS-CAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVDEdGKEGEIWISSPS 903
Cdd:cd05972    221 TGLP---IRDGYGQTETGLTVGnFPDMPVKP---GSMGRPTPGY--------DVAIIDDD-GRELPP-GEEGDIAIKLPP 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  904 AGI--GYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR- 979
Cdd:cd05972    285 PGLflGYVGDPEKTEASIRG--------DYYLTGDRAYRDEdGYFWFVGRADDIIKSSGYRIGPFEVE------SALLEh 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  980 PGC--CAVIGVPEEVlsaKGiSLPDAsdevgLVVIA--ELRDSKLVnKDIIKQIESRVAEEhgvtvASVKLIR-PRTISK 1054
Cdd:cd05972    351 PAVaeAAVVGSPDPV---RG-EVVKA-----FVVLTsgYEPSEELA-EELQGHVKKVLAPY-----KYPREIEfVEELPK 415
                          410
                   ....*....|
gi 1917948728 1055 TTSGKIKRFE 1064
Cdd:cd05972    416 TISGKIRRVE 425
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
660-1068 1.53e-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: 87.40  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  660 LPASNIAFQ---SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFT 736
Cdd:cd05912     60 LTPNELAFQlkdSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLSI 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  737 AMAcggSAILFSPLTFIR--NPLMWLQTISDYKATH-SAGPNfafelVIRRLEADKAKARNYDLSSMiffMIAAEPVRQK 813
Cdd:cd05912    136 LMR---SVIYGMTVYLVDkfDAEQVLHLINSGKVTIiSVVPT-----MLQRLLEILGEGYPNNLRCI---LLGGGPAPKP 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  814 TLKRFVELTRPFGLSqevmapgYGLAENC---VFVSCAYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDe 890
Cdd:cd05912    205 LLEQCKEKGIPVYQS-------YGMTETCsqiVTLSPEDALNKI-----------GSAGKPLFPVELKIEDDGQPPYEV- 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  891 dgkeGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEK 969
Cdd:cd05912    266 ----GEILLKGPNVTKGYLNRPDATEESFENG--------WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  970 TVESssellRPGC--CAVIGVPEevlsakgislpdasDEVGLVVIAELRDSKLVNKD-IIKQIESRVAeehgvtvasvKL 1046
Cdd:cd05912    334 VLLS-----HPAIkeAGVVGIPD--------------DKWGQVPVAFVVSERPISEEeLIAYCSEKLA----------KY 384
                          410       420
                   ....*....|....*....|....*...
gi 1917948728 1047 IRPRTI------SKTTSGKIKRFEcLKQ 1068
Cdd:cd05912    385 KVPKKIyfvdelPRTASGKLLRHE-LKQ 411
PRK08315 PRK08315
AMP-binding domain protein; Validated
666-992 1.58e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 88.71  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  666 AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGlftAMAC--GGS 743
Cdd:PRK08315   191 ARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLG---NLACvtHGA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  744 AILFSPLTFirNPLMWLQTISDYKATHSAG-----------PNFAfelvirrleadkakarNYDLSSMIFFMIAAEPVRQ 812
Cdd:PRK08315   268 TMVYPGEGF--DPLATLAAVEEERCTALYGvptmfiaeldhPDFA----------------RFDLSSLRTGIMAGSPCPI 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  813 KTLKRFVELtrpFGLSQEVMApgYGLAEnCVFVSCAYGKKKPIL--VDWQGRiccgyVDPNdadVDIRIVDADTGLEVdE 890
Cdd:PRK08315   330 EVMKRVIDK---MHMSEVTIA--YGMTE-TSPVSTQTRTDDPLEkrVTTVGR-----ALPH---LEVKIVDPETGETV-P 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  891 DGKEGEIWISSPSAGIGYWGKEElsqKTfrnklqnypgRK------YTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNI 962
Cdd:PRK08315   395 RGEQGELCTRGYSVMKGYWNDPE---KT----------AEaidadgWMHTGDLA-VMdeEGYVNIVGRIKDMIIRGGENI 460
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1917948728  963 YSADVEktvesssELLR--PGC--CAVIGVP-----EEV 992
Cdd:PRK08315   461 YPREIE-------EFLYthPKIqdVQVVGVPdekygEEV 492
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
670-1062 3.14e-17

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: 87.03  E-value: 3.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGSAILFSP 749
Cdd:cd17640     84 ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYTSI 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  750 LTFirnplmwLQTISDYKATHSAGpnfafelVIRRLEAdkakarnydLSSMIFFMIAAEP-VRQKTLKRFVELTR-PFGL 827
Cdd:cd17640    163 RTL-------KDDLKRVKPHYIVS-------VPRLWES---------LYSGIQKQVSKSSpIKQFLFLFFLSGGIfKFGI 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  828 SQE-VMAP---------------GYGLAENCVFVSCayGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGlEVDED 891
Cdd:cd17640    220 SGGgALPPhvdtffeaigievlnGYGLTETSPVVSA--RRLKCNVRGSVGRPL--------PGTEIKIVDPEGN-VVLPP 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  892 GKEGEIWISSPSAGIGYWGKEE-----LSQKTFRNklqnypgrkytrTGDLGW-VIQGNLFITGRIKDLIIVA-GRNIYS 964
Cdd:cd17640    289 GEKGIVWVRGPQVMKGYYKNPEatskvLDSDGWFN------------TGDLGWlTCGGELVLTGRAKDTIVLSnGENVEP 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  965 ADVEKTVEsSSELLRPgcCAVIG----------VP-----EEVLSAKGISLPdaSDEVGLvvIAELRDSKLVNKDIIKQI 1029
Cdd:cd17640    357 QPIEEALM-RSPFIEQ--IMVVGqdqkrlgaliVPnfeelEKWAKESGVKLA--NDRSQL--LASKKVLKLYKNEIKDEI 429
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1917948728 1030 ESRVAEEHGVTVASVKLIRPRTISK---TTSGKIKR 1062
Cdd:cd17640    430 SNRPGFKSFEQIAPFALLEEPFIENgemTQTMKIKR 465
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
526-1035 3.68e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 87.22  E-value: 3.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLtsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPL--QRGGQALTKIEN 600
Cdd:PRK06839    29 TYKQLHEYVSKVAAYLI--YELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLnirLTENELifQLKDSGTTVLFV 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 IAKLCNAVAILSTVGYhaavraglVKNLISFTGksvkstgqwpnlpwlhtdswIKSSKVLPASNIAFQSESQPDDLCFlq 680
Cdd:PRK06839   107 EKTFQNMALSMQKVSY--------VQRVISITS--------------------LKEIEDRKIDNFVEKNESASFIICY-- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 fTSGSTSDAKGVMITHGGL----IHNVKLMRRryrsTSNTVLVSWLPQYHDMGLigGLFT--AMACGGSAILfsPLTFir 754
Cdd:PRK06839   157 -TSGTTGKPKGAVLTQENMfwnaLNNTFAIDL----TMHDRSIVLLPLFHIGGI--GLFAfpTLFAGGVIIV--PRKF-- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGlsqevmaP 834
Cdd:PRK06839   226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETT-----NLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------Q 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENC--VF-VSCAYGKKKPILVDWQGRICcgyvdpndadvDIRIVDADTGlEVdEDGKEGEIWISSPSAGIGYWGK 911
Cdd:PRK06839   294 GFGMTETSptVFmLSEEDARRKVGSIGKPVLFC-----------DYELIDENKN-KV-EVGEVGELLIRGPNVMKEYWNR 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  912 EELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPE 990
Cdd:PRK06839   361 PDATEETIQD--------GWLCTGDLARVDEdGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE---VAVVGRQH 429
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1917948728  991 EVLSakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAE 1035
Cdd:PRK06839   430 VKWG-----------EIPIAFIVKKSSSVLIEKDVIEHCRLFLAK 463
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
501-1034 3.71e-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: 87.30  E-value: 3.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  501 AAQEITqnkalyTWINEGGAVgcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFG--CLRAKVI 578
Cdd:cd12119     10 GDREIV------SRTHEGEVH--RYTYAEVAERARRLANAL---RRLGVKPGDRVATLAWNTHRHLELYYAvpGMGAVLH 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  579 PI-PVLPPdplqrggqaltkiENIAKLCNavailstvgyHAAVRAGLVKnlISFTGKSVKSTGQWPNLP-WLHTDSWIKS 656
Cdd:cd12119     79 TInPRLFP-------------EQIAYIIN----------HAEDRVVFVD--RDFLPLLEAIAPRLPTVEhVVVMTDDAAM 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  657 SKVLPASNIAFQS--ESQPDDL----------CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRR--RYRSTSNTVLVSw 721
Cdd:cd12119    134 PEPAGVGVLAYEEllAAESPEYdwpdfdentaAAICYTSGTTGNPKGVVYSHRSLVlHAMAALLTdgLGLSESDVVLPV- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  722 LPQYHDMGLigGL-FTAMACGGSAILFSPLTfirNPLMWLQTISDYKATHSAG-PnfafelVIRRLEADKAKARNYDLSS 799
Cdd:cd12119    213 VPMFHVNAW--GLpYAAAMVGAKLVLPGPYL---DPASLAELIEREGVTFAAGvP------TVWQGLLDHLEANGRDLSS 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  800 MIFFMIAAEPVRQKTLKRFVELtrpfGLsqEVMApGYGLAENCVFVSCAYGKKK----PILVDW-----QGRICCGyvdp 870
Cdd:cd12119    282 LRRVVIGGSAVPRSLIEAFEER----GV--RVIH-AWGMTETSPLGTVARPPSEhsnlSEDEQLalrakQGRPVPG---- 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  871 ndadVDIRIVDADTGlEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNklqnypGrkYTRTGDLGwVI--QGNLFI 947
Cdd:cd12119    351 ----VELRIVDDDGR-ELPWDGKAvGELQVRGPWVTKSYYKNDEESEALTED------G--WLRTGDVA-TIdeDGYLTI 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsaKGISLPdasdeVGLVVIAElrDSKLVNKDIIK 1027
Cdd:cd12119    417 TDRSKDVIKSGGEWISSVELENAIMAHPAVAE---AAVIGVPHP----KWGERP-----LAVVVLKE--GATVTAEELLE 482

                   ....*..
gi 1917948728 1028 QIESRVA 1034
Cdd:cd12119    483 FLADKVA 489
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
526-968 6.29e-17

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: 86.21  E-value: 6.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17643     14 TYGELDARANRLARTL---RAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER-------IAFILADS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd17643     84 GPSLLLT-----------------------------------------------------------DPDDLAYVIYTSGS 104
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlvsWLpQYHDMGL---IGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:cd17643    105 TGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFdfsVWEIWGALLHGGRLVVVPYEV-ARSPEDFARL 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYKAT-HSAGPNfAFElviRRLEADKAKARNYDLSSMIFFmiAAEPVRQKTLKRFVEltrPFGLSQEVMAPGYGLAEN 841
Cdd:cd17643    180 LRDEGVTvLNQTPS-AFY---QLVEAADRDGRDPLALRYVIF--GGEALEAAMLRPWAG---RFGLDRPQLVNMYGITET 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  842 CVFVSCaygkkKPILVDwqgriccgYVDPNDA--------DVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:cd17643    251 TVHVTF-----RPLDAA--------DLPAAAAspigrplpGLRVYVLDAD-GRPV-PPGVVGELYVSGAGVARGYLGRPE 315
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  914 LSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17643    316 LTAERFVANPFGGPGSRMYRTGDLArRLPDGELEYLGRADEQVKIRGFRIELGEIE 371
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
526-1060 6.64e-17

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: 86.86  E-value: 6.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVPGL-DFIDAFFGCLRAKVIPIPVLppdplqrGGQALTKIENIAKL 604
Cdd:cd17634     86 SYRELHREVCRFAGTL---LDLGVKKGDRVA-IYMPMIpEAAVAMLACARIGAVHSVIF-------GGFAPEAVAGRIID 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGYhaaVRAGLVKNLISFTGKS-------------VKSTG---QWPNLPWLHTDSWIKsskvlpASNIAFQ 668
Cdd:cd17634    155 SSSRLLITADGG---VRAGRSVPLKKNVDDAlnpnvtsvehvivLKRTGsdiDWQEGRDLWWRDLIA------KASPEHQ 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  669 SES-QPDDLCFLQFTSGSTSDAKGVMITHGGliHNVKL---MRRRYRSTSNTVlVSWlpqYHDMGLIGG----LFTAMAC 740
Cdd:cd17634    226 PEAmNAEDPLFILYTSGTTGKPKGVLHTTGG--YLVYAattMKYVFDYGPGDI-YWC---TADVGWVTGhsylLYGPLAC 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  741 GGSAILFSPLTFIRNPLMWLQTISDYKATHSagpnFAFELVIRRL--EADKAKARnYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd17634    300 GATTLLYEGVPNWPTPARMWQVVDKHGVNIL----YTAPTAIRALmaAGDDAIEG-TDRSSLRILGSVGEPINPEAYEWY 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  819 velTRPFGLSQEVMAPGYGLAENCVFVScaygkkkPILvdwQGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKEGEIW 898
Cdd:cd17634    375 ---WKKIGKEKCPVVDTWWQTETGGFMI-------TPL---PGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLV 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  899 ISSPSAG--IGYWGKEELSQKTFRNKLQNYpgrkYTrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:cd17634    442 ITDPWPGqtRTLFGDHERFEQTYFSTFKGM----YF-SGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  976 ELLRpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKT 1055
Cdd:cd17634    517 KVAE---AAVVGIPHAI---KGQAP------YAYVV---LNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKT 581

                   ....*
gi 1917948728 1056 TSGKI 1060
Cdd:cd17634    582 RSGKI 586
PRK06164 PRK06164
acyl-CoA synthetase; Validated
515-988 8.95e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 86.34  E-value: 8.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  515 INEGGAVgcqrTYAELDSNASCVAHKLLtsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP-------PDP 587
Cdd:PRK06164    30 IDEDRPL----SRAELRALVDRLAAWLA---AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTryrshevAHI 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  588 LQRGGQALTKIENIAKLCNAVAILSTVGYhaAVRAGLvKNLISFTGKSVKSTGQWP----NLPWLHtdswiksskvLPAS 663
Cdd:PRK06164   103 LGRGRARWLVVWPGFKGIDFAAILAAVPP--DALPPL-RAIAVVDDAADATPAPAPgarvQLFALP----------DPAP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  664 NIAFQSESQPDDLCFLQFT-SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMAcGG 742
Cdd:PRK06164   170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALA-GG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  743 SAILFSPlTFIRNPLmwLQTISDYKATHSAGPNFAFELVIRRL--EADKAKARNYDLSSmifFMIAAEPVRQKTLKRFVE 820
Cdd:PRK06164   248 APLVCEP-VFDAART--ARALRRHRVTHTFGNDEMLRRILDTAgeRADFPSARLFGFAS---FAPALGELAALARARGVP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  821 LTRPFGlSQEVMApgyglaencvFVSCaygkkKPILVDWQGRICCGYVdPNDADVDIRIVDADTGlEVDEDGKEGEIWIS 900
Cdd:PRK06164   322 LTGLYG-SSEVQA----------LVAL-----QPATDPVSVRIEGGGR-PASPEARVRARDPQDG-ALLPDGESGEIEIR 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  901 SPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGNLFI-TGRIKDLIIVAGRNIYSADVEKTVESssellR 979
Cdd:PRK06164   384 APSLMRGYLDNPDATARALTDD-------GYFRTGDLGYTRGDGQFVyQTRMGDSLRLGGFLVNPAEIEHALEA-----L 451
                          490
                   ....*....|.
gi 1917948728  980 PGC--CAVIGV 988
Cdd:PRK06164   452 PGVaaAQVVGA 462
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
674-990 1.21e-16

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 85.86  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVkLMRRRYR---STSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPL 750
Cdd:PRK06710   206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLyncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKF 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFirnpLMWLQTISDYKATHSAG-PNFAFELVIRRLeadkakARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfglsQ 829
Cdd:PRK06710   285 DM----KMVFEAIKKHKVTLFPGaPTIYIALLNSPL------LKEYDISSIRACISGSAPLPVEVQEKFETVT------G 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  830 EVMAPGYGLAENCVFVSCAYgkkkpilvDWQGRIcCGYVDPNDADVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:PRK06710   349 GKLVEGYGLTESSPVTHSNF--------LWEKRV-PGSIGVPWPDTEAMIMSLETG-EALPPGEIGEIVVKGPQIMKGYW 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  910 GKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:PRK06710   419 NKPEETAAVLQD--------GWLHTGDVGYMDEdGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE---VVTIGV 487

                   ..
gi 1917948728  989 PE 990
Cdd:PRK06710   488 PD 489
PRK07470 PRK07470
acyl-CoA synthetase; Validated
526-1034 1.46e-16

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 85.48  E-value: 1.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPV----LPPDplqrggqaltkIEN 600
Cdd:PRK07470    34 TWREIDARVDALAAALAAR---GVRKGDRIL-VHSRnCNQMFESMFAAFRLGAVWVPTnfrqTPDE-----------VAY 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 IAKLCNAVAILSTVGYHAAVRAglvknlisftgksVKSTGqwpnlPWLHTDSWIKSSKV------LPASNIAFQSESQP- 673
Cdd:PRK07470    99 LAEASGARAMICHADFPEHAAA-------------VRAAS-----PDLTHVVAIGGARAgldyeaLVARHLGARVANAAv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 --DDLCFLQFTSGSTSDAKGVMITHGGLI-----HNVKLMRRryrSTSNTVLVSWLPQYHDMGlIGGLfTAMACGGSAIL 746
Cdd:PRK07470   161 dhDDPCWFFFTSGTTGRPKAAVLTHGQMAfvitnHLADLMPG---TTEQDASLVVAPLSHGAG-IHQL-CQVARGAATVL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 -----FSPLTFirnplmWlQTISDYKATHSagpnFAFELVIRRLEADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVEL 821
Cdd:PRK07470   236 lpserFDPAEV------W-ALVERHRVTNL----FTVPTILKMLVEHPAVDR-YDHSSLRYVIYAGAPMYRADQKRALAK 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  822 TRPfglsqeVMAPGYGLAEncvfVSCAYGKKKPILVDW----QGRI-CCGYvdpndadvdirivdADTGLEV---DEDGK 893
Cdd:PRK07470   304 LGK------VLVQYFGLGE----VTGNITVLPPALHDAedgpDARIgTCGF--------------ERTGMEVqiqDDEGR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  894 E------GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:PRK07470   360 ElppgetGEICVIGPAVFAGYYNNPEANAKAFRDG--------WFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPRE 431
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728  967 VEKTVessseLLRPGC--CAVIGVPEEVLSakgislpdasdEVGLVVIAeLRDSKLVNKD-IIKQIESRVA 1034
Cdd:PRK07470   432 IEEKL-----LTHPAVseVAVLGVPDPVWG-----------EVGVAVCV-ARDGAPVDEAeLLAWLDGKVA 485
PRK07529 PRK07529
AMP-binding domain protein; Validated
673-989 2.24e-16

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 85.39  E-value: 2.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTF 752
Cdd:PRK07529   212 PDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 iRNP-LM---WlQTISDYKATH-SAGPNFAFELVIRRLEAdkakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGL 827
Cdd:PRK07529   292 -RGPgVIanfW-KIVERYRINFlSGVPTVYAALLQVPVDG-------HDISSLRYALCGAAPLPVEVFRRFEAAT---GV 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  828 SqevMAPGYGLAENCVFVSCAY--GKKKP----ILVDWQgriccgyvdpndaDVDIRIVDADTGLEVD-EDGKEGEIWIS 900
Cdd:PRK07529   360 R---IVEGYGLTEATCVSSVNPpdGERRIgsvgLRLPYQ-------------RVRVVILDDAGRYLRDcAVDEVGVLCIA 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  901 SPSAGIGYWGKEelsqktfrnklQN---YPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessse 976
Cdd:PRK07529   424 GPNVFSGYLEAA-----------HNkglWLEDGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEA------ 486
                          330
                   ....*....|....*.
gi 1917948728  977 LLR-P--GCCAVIGVP 989
Cdd:PRK07529   487 LLRhPavALAAAVGRP 502
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
658-1031 4.01e-16

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 85.36  E-value: 4.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  658 KVLPASNI--AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 735
Cdd:PRK08633   764 RLLPARLLkrLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLW 843
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  736 TAMACGGSAILFSpltfirNPLMWL---QTISDYKATHSAG-PNFaFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVR 811
Cdd:PRK08633   844 LPLLEGIKVVYHP------DPTDALgiaKLVAKHRATILLGtPTF-LRLYLRNKKLHPL-----MFASLRLVVAGAEKLK 911
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  812 QKTLKRFVEltrPFGLsqEVMApGYGLAEncvfvsCAygkkkPIlvdwqgrICCGYVDPNDAD----------------- 874
Cdd:PRK08633   912 PEVADAFEE---KFGI--RILE-GYGATE------TS-----PV-------ASVNLPDVLAADfkrqtgskegsvgmplp 967
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  875 -VDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTfrnkLQNYPGRKYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK08633   968 gVAVRIVDPETFEEL-PPGEDGLILIGGPQVMKGYLGDPEKTAEV----IKDIDGIGWYVTGDKGHLdEDGFLTITDRYS 1042
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  953 DLIIVAGRNIYSADVEktvESSSELL--RPGCCAVIGVPEEvlsAKGISL-----PDASDEVGLV-VIAELRDSKLVNKD 1024
Cdd:PRK08633  1043 RFAKIGGEMVPLGAVE---EELAKALggEEVVFAVTAVPDE---KKGEKLvvlhtCGAEDVEELKrAIKESGLPNLWKPS 1116

                   ....*..
gi 1917948728 1025 IIKQIES 1031
Cdd:PRK08633  1117 RYFKVEA 1123
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 2.16e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.56  E-value: 2.16e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
526-1070 2.60e-15

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: 81.43  E-value: 2.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRkptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd05918     26 TYAELDRLSSRLAHHLRSLG---VGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQR-------LQEILQDT 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd05918     96 GAKVVLT----------------------------------------------------------SSPSDAAYVIFTSGS 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VL--------VSwlpqyhdmglIGGLFTAMACGGSaiLFSPLTFIR-N 755
Cdd:cd05918    118 TGKPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVS----------ILEIFTTLAAGGC--LCIPSEEDRlN 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  756 PLmwLQTISDYKATHsagpnfAFeL---VIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqeVM 832
Cdd:cd05918    186 DL--AGFINRLRVTW------AF-LtpsVARLLDPE-------DVPSLRTLVLGGEALTQSDVDTWADRVR-------LI 242
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  833 ApGYGLAENCVFVSCaygkkKPILVDWQGRI------CCGY-VDPNDADvdiRIVDAdtglevdedGKEGEIWISSPSAG 905
Cdd:cd05918    243 N-AYGPAECTIAATV-----SPVVPSTDPRNigrplgATCWvVDPDNHD---RLVPI---------GAVGELLIEGPILA 304
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 IGYWGKEELSQKTF-------RNKLQNYPGRKYtRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:cd05918    305 RGYLNDPEKTAAAFiedpawlKQEGSGRGRRLY-RTGDL--VRYnpdGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSL 381
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  976 ELLRPgCCAVIGVPeevlsakgislPDASDEVGLVVIAELRDSKLVNKDiikqIESRVAEEHGVTVASVKLIRPR----- 1050
Cdd:cd05918    382 PGAKE-VVVEVVKP-----------KDGSSSPQLVAFVVLDGSSSGSGD----GDSLFLEPSDEFRALVAELRSKlrqrl 445
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1917948728 1051 -------------TISKTTSGKIKRfECLKQFV 1070
Cdd:cd05918    446 psymvpsvflplsHLPLTASGKIDR-RALRELA 477
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
660-968 4.23e-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: 80.20  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  660 LPASNIAFQSE--------SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhDMGLI 731
Cdd:cd17650     71 YPAERLQYMLEdsgaklllTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASF-SFDVF 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  732 GGLFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKAThsagpnfAFELV---IRRLEADKAKaRNYDLSSMIFFMIAAE 808
Cdd:cd17650    150 AGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRIT-------LMESTpalIRPVMAYVYR-NGLDLSAMRLLIVGSD 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  809 PVrqkTLKRFVELTRPFGLSQEVMApGYGLAENCVFVSCAYGKKKPILVdwQGRICCGYVDPNDAdvdIRIVDADtgLEV 888
Cdd:cd17650    222 GC---KAQDFKTLAARFGQGMRIIN-SYGVTEATIDSTYYEEGRDPLGD--SANVPIGRPLPNTA---MYVLDER--LQP 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  889 DEDGKEGEIWISSPSAGIGYWGKEELSQKTF-RNKLQnyPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:cd17650    291 QPVGVAGELYIGGAGVARGYLNRPELTAERFvENPFA--PGERMYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGE 368

                   ..
gi 1917948728  967 VE 968
Cdd:cd17650    369 IE 370
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
504-1064 5.10e-15

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: 80.62  E-value: 5.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  504 EITQNKALYTWINEGGaVGCQRTYAELdSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPvl 583
Cdd:cd05970     28 KEYPDKLALVWCDDAG-EERIFTFAEL-ADYSDKTANFFKAMG--IGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP-- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  584 ppdplqrgGQALTKIENIAKLCNAVAILSTVgyhaAVRAGLVKNLISftgKSVKSTGQWPNLPWLH---TDSWIKSSKVL 660
Cdd:cd05970    102 --------ATHQLTAKDIVYRIESADIKMIV----AIAEDNIPEEIE---KAAPECPSKPKLVWVGdpvPEGWIDFRKLI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  661 PASNIAFQ-----SESQPDDLCFLQFTSGSTSDAKgvMITH------GGLI-----HNVKLMRRRYrSTSNTvlvSWlpq 724
Cdd:cd05970    167 KNASPDFErptanSYPCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVtakywQNVREGGLHL-TVADT---GW--- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  725 yhDMGLIGGLFTAMACGGSAILFSPLTFIrnPLMWLQTISDYKATHSAGPNFAFELVIRrleadkAKARNYDLSSMIFFM 804
Cdd:cd05970    238 --GKAVWGKIYGQWIAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIR------EDLSRYDLSSLRYCT 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  805 IAAEPVRQKTLKRFVELTrpfGLSqevMAPGYGLAENCVFVSCAYG-KKKPILVdwqGRICCGYvdpndadvDIRIVDAD 883
Cdd:cd05970    308 TAGEALNPEVFNTFKEKT---GIK---LMEGFGQTETTLTIATFPWmEPKPGSM---GKPAPGY--------EIDLIDRE 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  884 tGLEVdEDGKEGEIWISSpSAGI------GYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLII 956
Cdd:cd05970    371 -GRSC-EAGEEGEIVIRT-SKGKpvglfgGYYKDAEKTAEVWHD--------GYYHTGDAAWMDEdGYLWFVGRTDDLIK 439
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  957 VAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLsakgislpdasdevGLVVIAELrdskLVNKD------IIKQIE 1030
Cdd:cd05970    440 SSGYRIGPFEVESALIQHPAVLE---CAVTGVPDPIR--------------GQVVKATI----VLAKGyepseeLKKELQ 498
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 1917948728 1031 SRVAEehgVTvASVKLirPRTIS------KTTSGKIKRFE 1064
Cdd:cd05970    499 DHVKK---VT-APYKY--PRIVEfvdelpKTISGKIRRVE 532
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
677-992 5.72e-15

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: 78.50  E-value: 5.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  677 CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRyRSTSNTVLVSWLPQYHdmglIGGLFTAMA---CGGSAIlfspltF 752
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQ-AIDEGTVFLNSGPLFH----IGTLMFTLAtfhAGGTNV------F 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 IR--NPLMWLQTISDYKATHS--AGPNFAfelVIRRLEADkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLS 828
Cdd:cd17636     72 VRrvDAEEVLELIEAERCTHAflLPPTID---QIVELNAD----GLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGGYG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  829 Q-EVMapgyGLAencvfVSCAYGKKkpilvdwqGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIG 907
Cdd:cd17636    145 QtEVM----GLA-----TFAALGGG--------AIGGAGRPSPL---VQVRILDED-GREV-PDGEVGEIVARGPTVMAG 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  908 YWGKEELSQKTFRNklqnypgrKYTRTGDLGW-VIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellRPGC--CA 984
Cdd:cd17636    203 YWNRPEVNARRTRG--------GWHHTNDLGRrEPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-----HPAVadAA 269

                   ....*...
gi 1917948728  985 VIGVPEEV 992
Cdd:cd17636    270 VIGVPDPR 277
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
525-1017 9.04e-15

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 79.56  E-value: 9.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDplqrggqaltKIENI 601
Cdd:PRK08276    12 VTYGELEARSNRLAHGL---RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhLTAA----------EIAYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILSTVGYhAAVRAGLVKNLISftGKSVKSTGQWPNLPWLHTDSWIKSSkvlPASNIAFQSESQPddlcfLQF 681
Cdd:PRK08276    79 VDDSGAKVLIVSAAL-ADTAAELAAELPA--GVPLLLVVAGPVPGFRSYEEALAAQ---PDTPIADETAGAD-----MLY 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVM-------ITHGGLIHNVKLMRRRYRSTSNTVLVSwLPQYHDMGLIGGLfTAMACGGSAIL---FSPLT 751
Cdd:PRK08276   148 SSGTTGRPKGIKrplpgldPDEAPGMMLALLGFGMYGGPDSVYLSP-APLYHTAPLRFGM-SALALGGTVVVmekFDAEE 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  752 FirnplmwLQTISDYKATHSagpnfafELV----IRRLE-ADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfg 826
Cdd:PRK08276   226 A-------LALIERYRVTHS-------QLVptmfVRMLKlPEEVRAR-YDVSSLRVAIHAAAPCPVEVKRAMIDWWGP-- 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  827 lsqeVMAPGYGLAENC--VFVSCAYGKKKPILVD--WQGRIccgyvdpndadvdiRIVDADtGLEVDEdGKEGEIWISSP 902
Cdd:PRK08276   289 ----IIHEYYASSEGGgvTVITSEDWLAHPGSVGkaVLGEV--------------RILDED-GNELPP-GEIGTVYFEMD 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  903 SAGIGYWGKEElsqKTfrnkLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-P 980
Cdd:PRK08276   349 GYPFEYHNDPE---KT----AAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIE------NLLVThP 415
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1917948728  981 GC--CAVIGVP-----EEVlsaKGISLP----DASDEVGLVVIAELRD 1017
Cdd:PRK08276   416 KVadVAVFGVPdeemgERV---KAVVQPadgaDAGDALAAELIAWLRG 460
PRK06145 PRK06145
acyl-CoA synthetase; Validated
661-990 1.19e-14

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 79.16  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLihnvklmrrRYRSTSNTVLVSwLPQYHDMGLIGGLFTAMAC 740
Cdd:PRK06145   136 GGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL---------HWKSIDHVIALG-LTASERLLVVGPLYHVGAF 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  741 G--GSAILF--SPLTFIRN--PLMWLQTISDYKAThsaGPNFAFELVIRRL---EADKakarnYDLSSMIFFMIAAEPVR 811
Cdd:PRK06145   206 DlpGIAVLWvgGTLRIHREfdPEAVLAAIERHRLT---CAWMAPVMLSRVLtvpDRDR-----FDLDSLAWCIGGGEKTP 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  812 QKTLKRFVELTRpfglsQEVMAPGYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLEvdED 891
Cdd:PRK06145   278 ESRIRDFTRVFT-----RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRAL--------AHVEIRIADGAGRWL--PP 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  892 GKEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK06145   343 NMKGEICMRGPKVTKGYWKDPEKTAEAFYG--------DWFRSGDVGYLDeEGFLYLTDRKKDMIISGGENIASSEVERV 414
                          330       340
                   ....*....|....*....|
gi 1917948728  971 VESSSELLRpgcCAVIGVPE 990
Cdd:PRK06145   415 IYELPEVAE---AAVIGVHD 431
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
497-1062 1.36e-14

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: 79.46  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  497 LKHWAAQEITQnkALYTWINEGGAVGcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:cd05968     67 LDKWLADTRTR--PALRWEGEDGTSR-TLTYGELLYEVKRLANGL---RALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  577 VIPIPVLP---PDPlqrggqALTKIENiaklCNAVAILSTVGYhaaVRAGLVKNLISFTGKSVKST-----------GQW 642
Cdd:cd05968    141 GIVVPIFSgfgKEA------AATRLQD----AEAKALITADGF---TRRGREVNLKEEADKACAQCptvekvvvvrhLGN 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  643 PNLPWLHTDSWIKSSKvlpASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWL 722
Cdd:cd05968    208 DFTPAKGRDLSYDEEK---ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWF 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  723 PqyhDMGLIGG---LFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKATH-SAGPNfafelVIRRLEA-DKAKARNYDL 797
Cdd:cd05968    285 T---DLGWMMGpwlIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHlGLSPT-----LIRALKPrGDAPVNAHDL 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  798 SSMIFFMIAAEPVRQKTLKRFVELTrpfglsqevmapgygLAENCVFVSCAYGkkkpilVDWQGRICCGYV----DPNDA 873
Cdd:cd05968    357 SSLRVLGSTGEPWNPEPWNWLFETV---------------GKGRNPIINYSGG------TEISGGILGNVLikpiKPSSF 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  874 DVDIRIVDADTgleVDEDGK-----EGEIWISSPSAGI--GYWGKEELSQKTFRNKLQNypgrKYTRtGDLGWV-IQGNL 945
Cdd:cd05968    416 NGPVPGMKADV---LDESGKparpeVGELVLLAPWPGMtrGFWRDEDRYLETYWSRFDN----VWVH-GDFAYYdEEGYF 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  946 FITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsaKGislpdaSDEVGLVViaeLRDSKLVNKDI 1025
Cdd:cd05968    488 YILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE---SAAIGVPHPV---KG------EAIVCFVV---LKPGVTPTEAL 552
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1917948728 1026 IKQIESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1062
Cdd:cd05968    553 AEELMERVADELG------KPLSPERIlfvkdlPKTRNAKVMR 589
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
524-988 1.49e-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: 78.66  E-value: 1.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIEniak 603
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAY---GIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 lcnavailstvgyhaavraglvknlisftgksvkstgqwPNlpwlhtdswiksskvlpasniAFQSESQPDDLCFLQFTS 683
Cdd:cd05910     75 ---------------------------------------PD---------------------AFIGIPKADEPAAILFTS 94
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhdmgligGLFTAmACGGSAIL--FSPLTFIR-NPLMWL 760
Cdd:cd05910     95 GSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGP-ALGLTSVIpdMDPTRPARaDPQKLV 166
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAGPNFAFELVIRRLEADKAKarnydLSSMIFFMIAAEPVRQKTLKRFVELTRPfglSQEVMAPgYGLAE 840
Cdd:cd05910    167 GAIRQYGVSIVFGSPALLERVARYCAQHGIT-----LPSLRRVLSAGAPVPIALAARLRKMLSD---EAEILTP-YGATE 237
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 N---CVFVSCAYGKKKPILVDWQGRICCGY-VDPNDADV----DIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKE 912
Cdd:cd05910    238 AlpvSSIGSRELLATTTAATSGGAGTCVGRpIPGVRVRIieidDEPIAEWDDTLELP-RGEIGEITVTGPTVTPTYVNRP 316
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728  913 elsQKTFRNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:cd05910    317 ---VATALAKIDDNSEGFWHRMGDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR---SALVGV 387
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
675-1062 2.39e-14

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: 76.60  E-value: 2.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMACggsAILFSPLTFIR 754
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH----VGGLAILVRS---LLAGAELVLLE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLMWLQTISDYKATHSAgpnfafeLV---IRRLEADKAKARNYDLSSMIFfmIAAEPVRQKTLKRFVELTRPfglsqev 831
Cdd:cd17630     74 RNQALAEDLAPPGVTHVS-------LVptqLQRLLDSGQGPAALKSLRAVL--LGGAPIPPELLERAADRGIP------- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  832 MAPGYGLAEncvFVSCAYGKKkpilvdwQGRICCGYVDPNDADVDIRIVDadtglevdedgkEGEIWISSPSAGIGYWGK 911
Cdd:cd17630    138 LYTTYGMTE---TASQVATKR-------PDGFGRGGVGVLLPGRELRIVE------------DGEIWVGGASLAMGYLRG 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  912 EELSQktfrnklqnYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPE 990
Cdd:cd17630    196 QLVPE---------FNEDGWFTTKDLGeLHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD---AFVVGVPD 263
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728  991 EVLSAKgislpdasdevgLVVIAELRDSKLVnkdiiKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKR 1062
Cdd:cd17630    264 EELGQR------------PVAVIVGRGPADP-----AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDR 318
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
526-1002 4.49e-14

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: 77.21  E-value: 4.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17645     25 TYKQLNEKANQLARHL---RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER-------IAYMLADS 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd17645     95 SAKILLT-----------------------------------------------------------NPDDLAYVIYTSGS 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHnvklmrrryrstsntvLVSWlpqYHDMgligglFTAMACGGSAIlFSPLTFIRNPLMWLQTISD 765
Cdd:cd17645    116 TGLPKGVMIEHHNLVN----------------LCEW---HRPY------FGVTPADKSLV-YASFSFDASAWEIFPHLTA 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATHSAGPNfafelviRRLEADKAKARNYDLSSMIFFMI--AAEPVRQ-------------KTLKRFVEltRPFGLSQe 830
Cdd:cd17645    170 GAALHVVPSE-------RRLDLDALNDYFNQEGITISFLPtgAAEQFMQldnqslrvlltggDKLKKIER--KGYKLVN- 239
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  831 vmapGYGLAENCVFVSCAYgkkkpilvdwqgriccgyVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWISSPS 903
Cdd:cd17645    240 ----NYGPTENTVVATSFE------------------IDKPYANIPIgkpidntRVYILDEALQLQPIGVAGELCIAGEG 297
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  904 AGIGYWGKEELSQKTFRNKLQnYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELL---- 978
Cdd:cd17645    298 LARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIElaav 376
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1917948728  979 --------RPGCCAVIGVPEEVLSAK-----GISLPD 1002
Cdd:cd17645    377 lakedadgRKYLVAYVTAPEEIPHEElrewlKNDLPD 413
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
19-264 4.85e-14

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 76.88  E-value: 4.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   97 LEEM-DLHKLALIDsFTGEYHDIN-VAEDYMSLVSLTLEIQDKAKDSnhIGIHAVSDIASDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231     83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAA--LDPWAHPAAELDRESlaEWLRRNGASPSARR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMSLWKKISKSLLIKVCCNTEVQAVRRDGSDVNV 245
Cdd:COG1231    160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234
                          250
                   ....*....|....*....
gi 1917948728  246 DITNssGETEHkeFDKIII 264
Cdd:COG1231    235 TTDD--GGTVR--ADAVIV 249
PRK09088 PRK09088
acyl-CoA synthetase; Validated
520-1062 4.85e-14

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 77.15  E-value: 4.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  520 AVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPdplqrggqalT 596
Cdd:PRK09088    18 ALGRRWTYAELDALVGRLAAVL---RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSA----------S 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  597 KIENIAKLCNAVAILSTvgyhAAVRAGlvknlisftgksvkstgqwpNLPWLHTDSWIKSSKvlpASNIAFQSESQPDDL 676
Cdd:PRK09088    85 ELDALLQDAEPRLLLGD----DAVAAG--------------------RTDVEDLAAFIASAD---ALEPADTPSIPPERV 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  677 CFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSaILFSPLTFIRNP 756
Cdd:PRK09088   138 SLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS-ILVSNGFEPKRT 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  757 LMWLQTiSDYKATHSAG-PNFAFELvirRLEADKAKARnydLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqevMAPG 835
Cdd:PRK09088   217 LGRLGD-PALGITHYFCvPQMAQAF---RAQPGFDAAA---LRHLTALFTGGAPHAAEDILGWLDDGIP-------MVDG 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  836 YGLAE-NCVF---VSCAYGKKKpilvdwqgricCGYVDPNDADVDIRIVDADtglevDED---GKEGEIWISSPSAGIGY 908
Cdd:PRK09088   283 FGMSEaGTVFgmsVDCDVIRAK-----------AGAAGIPTPTVQTRVVDDQ-----GNDcpaGVPGELLLRGPNLSPGY 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  909 WGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIG 987
Cdd:PRK09088   347 WRRPQATARAF-------TGDGWFRTGDIARRdADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRE---CAVVG 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  988 VpeevlsakgislPDAS-DEVGLVVIAELRDSKLVNKDIIKQIESRVAE----EHGVTVASVklirPRtiskTTSGKIKR 1062
Cdd:PRK09088   417 M------------ADAQwGEVGYLAIVPADGAPLDLERIRSHLSTRLAKykvpKHLRLVDAL----PR----TASGKLQK 476
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
526-968 7.49e-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: 7.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd12116     14 SYAELDERANRLAARL---RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR-------LRYILEDA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTvgyhAAVRAGLVKNLisftgksvkstgqwpnlpwlhtDSWIKSSKVLPASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:cd12116     84 EPALVLTD----DALPDRLPAGL----------------------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGS 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMACGGSAILFSPLTfIRNPLMWLQTISD 765
Cdd:cd12116    138 TGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAPRET-QRDPEALARLIEA 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKATHsagpnfafelvirrLEADKAKARnydlssmifFMIAAEPVRQKTLKRFV---ELtrPFGLSQEVMAPG------Y 836
Cdd:cd12116    216 HSITV--------------MQATPATWR---------MLLDAGWQGRAGLTALCggeAL--PPDLAARLLSRVgslwnlY 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  837 GLAENCVfvscaygkkkpilvdWQgriCCGYVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:cd12116    271 GPTETTI---------------WS---TAARVTAAAGPIPIgrplantQVYVLDAALRPVPPGVPGELYIGGDGVAQGYL 332
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  910 GKEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd12116    333 GRPALTAERFVPDPFAGPGSRLYRTGDLVrRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
22-94 9.47e-14

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: 76.02  E-value: 9.47e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
675-1062 1.26e-13

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: 74.36  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLIH----NVKLMrrrYRSTSNTVLVSWlPQYHDMGLIGGLFtAMACGGSAILFSPL 750
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIEsfvcNEDLF---NISGEDAILAPG-PLSHSLFLYGAIS-ALYLGGTFIGQRKF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 tfirNPLMWLQTISDYKAThsagpnfAFELVIRRLEAdKAKARNYDLSSMIFFMIAA--EPVRQKTLKRfveltrpfGLS 828
Cdd:cd17633     76 ----NPKSWIRKINQYNAT-------VIYLVPTMLQA-LARTLEPESKIKSIFSSGQklFESTKKKLKN--------IFP 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  829 QEVMAPGYGLAE-NCVFVSCAYGKKKPILVdwqGRICcgyvdPNdadVDIRIVDADtglevdeDGKEGEIWISSPSAGIG 907
Cdd:cd17633    136 KANLIEFYGTSElSFITYNFNQESRPPNSV---GRPF-----PN---VEIEIRNAD-------GGEIGKIFVKSEMVFSG 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  908 YWgKEELSQKTfrnklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGccaVI 986
Cdd:cd17633    198 YV-RGGFSNPD-----------GWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI---VV 262
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  987 GVPEEVLSAKGislpdasdeVGLVVIAELRDSKLvnKDIIKQIESRvaEEhgvtVASvKLIRPRTISKTTSGKIKR 1062
Cdd:cd17633    263 GIPDARFGEIA---------VALYSGDKLTYKQL--KRFLKQKLSR--YE----IPK-KIIFVDSLPYTSSGKIAR 320
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
522-968 1.41e-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: 75.48  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkieni 601
Cdd:cd17649     10 DQSLSYAELDARANRLAHRL---RALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER----------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 aklcnavailstvgyhaavraglvknlisftgksvkstgqwpnLPWLHTDSWIKSskVLPAsniafqsesQPDDLCFLQF 681
Cdd:cd17649     76 -------------------------------------------LRYMLEDSGAGL--LLTH---------HPRQLAYVIY 101
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAILfspltfiRNPLMWLQ 761
Cdd:cd17649    102 TSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVL-------RPDELWAS 173
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  762 TISDYKATHSAG-------PNFAFELVirrLEADKAKARNYdlSSMIFFMIAAEPVRQKTLKRF----VELTRPFGLSQE 830
Cdd:cd17649    174 ADELAEMVRELGvtvldlpPAYLQQLA---EEADRTGDGRP--PSLRLYIFGGEALSPELLRRWlkapVRLFNAYGPTEA 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  831 VMAPgygLAENCVFVSCAYGKKKPIlvdwqGRICCGYVdpndadvdIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWG 910
Cdd:cd17649    249 TVTP---LVWKCEAGAARAGASMPI-----GRPLGGRS--------AYILDADLNPV--PVGVTGELYIGGEGLARGYLG 310
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728  911 KEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17649    311 RPELTAERFVPDPFGAPGSRLYRTGDLArWRDDGVIEYLGRVDHQVKIRGFRIELGEIE 369
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
526-968 2.08e-13

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: 75.39  E-value: 2.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHkLLTSRkpTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKL 604
Cdd:cd17646     25 TYRELDERANRLAH-LLRAR--GVGPEDRVA-VLLPrSADLVVALLAVLKAGAAYLPLDPGYPADR-------LAYMLAD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 CNAVAILSTVGYHAAVRAGLVKNLISFTG-KSVKSTGQWPnlpwlhtdswiksskvlpasniafqsESQPDDLCFLQFTS 683
Cdd:cd17646     94 AGPAVVLTTADLAARLPAGGDVALLGDEAlAAPPATPPLV--------------------------PPRPDNLAYVIYTS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTI 763
Cdd:cd17646    148 GSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPGGH-RDPAYLAALI 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  764 SDYKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevmAP---GYGLAE 840
Cdd:cd17646    226 REHGVT-------TCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG---------AElhnLYGPTE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NCVFVScaYGKKKPilVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd17646    290 AAIDVT--HWPVRG--PAETPSVPIGRPVPN---TRLYVLDDA--LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFV 360
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1917948728  921 NKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17646    361 PDPFGPGSRMY-RTGDLArWRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
669-1011 9.06e-13

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 73.31  E-value: 9.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  669 SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGL-IGGLFTAMAcgGSAILF 747
Cdd:PRK06334   178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLS--GVPVVF 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 S--PLtfirNPLMWLQTISDYKATHSAGPNFAFELVIRrleadKAKARNYDLSSMIFFMIAAE----PVRQKTLKRFVEL 821
Cdd:PRK06334   256 AynPL----YPKKIVEMIDEAKVTFLGSTPVFFDYILK-----TAKKQESCLPSLRFVVIGGDafkdSLYQEALKTFPHI 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  822 TrpfgLSQevmapGYGLAEnCVFVSCAYGKKKPilvdwQGRICCGYvdPNDAdVDIRIVDADTGLEVdEDGKEGEIWISS 901
Cdd:PRK06334   327 Q----LRQ-----GYGTTE-CSPVITINTVNSP-----KHESCVGM--PIRG-MDVLIVSEETKVPV-SSGETGLVLTRG 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  902 PSAGIGYWGKEelsqktFRNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIysadvekTVESSSELLRP 980
Cdd:PRK06334   388 TSLFSGYLGED------FGQGFVELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMV-------SLEALESILME 454
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1917948728  981 GCcavigvpeevlsakgiSLPDASDEVGLVV 1011
Cdd:PRK06334   455 GF----------------GQNAADHAGPLVV 469
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
526-1018 1.94e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 72.42  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTKIENIAKLC 605
Cdd:PRK13391    26 TYRELDERSNRLAHLF---RSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV---------NSHLTPAEAAYIVD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVA-ILSTVGYHAAVRAGLVKNLISFTGKSV-KSTGQWPnlPWLHTDSWIKSskvLPASNIAFQSESQPddlcfLQFTS 683
Cdd:PRK13391    94 DSGArALITSAAKLDVARALLKQCPGVRHRLVlDGDGELE--GFVGYAEAVAG---LPATPIADESLGTD-----MLYSS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVM--ITHGGLIHNVKL---MRRRYRSTSNTVLVSWLPQYHDmgliGGLFTAM---ACGGSAIL---FSPLTF 752
Cdd:PRK13391   164 GTTGRPKGIKrpLPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHS----APQRAVMlviRLGGTVIVmehFDAEQY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 irnplmwLQTISDYKATHSagpNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVM 832
Cdd:PRK13391   240 -------LALIEEYGVTHT---QLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP------II 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  833 APGYGLAENCVFVSCAYGK--KKPILVdwqGRICCGyvdpndadvDIRIVDaDTGLEVDEdGKEGEIWIsspsagigywg 910
Cdd:PRK13391   304 HEYYAATEGLGFTACDSEEwlAHPGTV---GRAMFG---------DLHILD-DDGAELPP-GEPGTIWF----------- 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  911 KEELSQKTF----RNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAV 985
Cdd:PRK13391   359 EGGRPFEYLndpaKTAEARHPDGTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAD---AAV 435
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1917948728  986 IGVPEEVL--SAKGISLP----DASDEVGLVVIAELRDS 1018
Cdd:PRK13391   436 FGVPNEDLgeEVKAVVQPvdgvDPGPALAAELIAFCRQR 474
PRK07867 PRK07867
acyl-CoA synthetase; Validated
640-992 2.34e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 72.02  E-value: 2.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  640 GQWPNLPWLHTDSWIKSSKVLPASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGGL-IHNVKLMRRRYRSTSNTV 717
Cdd:PRK07867   117 GLDPGVRVINVDSPAWADELAAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRFGLGPDDVC 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  718 LVSwLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmwLQTISDYKATHSagpnfafelvirrleadkakarN 794
Cdd:PRK07867   197 YVS-MPLFHSNAVMAGWAVALAAGASIALrrkFSASGF-------LPDVRRYGATYA----------------------N 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  795 Y---DLSsmifFMIAAEPV---RQKTLK-------------RFVeltRPFGLsqeVMAPGYGLAENCVFVSCAYGKKKPI 855
Cdd:PRK07867   247 YvgkPLS----YVLATPERpddADNPLRivygnegapgdiaRFA---RRFGC---VVVDGFGSTEGGVAITRTPDTPPGA 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  856 LvdwqGRiccgyvdpndADVDIRIVDADTGLEV-----DEDGKE------GEIW-ISSPSAGIGYWGKEELSQKTFRNkl 923
Cdd:PRK07867   317 L----GP----------LPPGVAIVDPDTGTECppaedADGRLLnadeaiGELVnTAGPGGFEGYYNDPEADAERMRG-- 380
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728  924 qnypGRKYtrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PGC--CAVIGVPEEV 992
Cdd:PRK07867   381 ----GVYW--SGDLAYRdADGYAYFAGRLGDWMRVDGENLGTAPIERI------LLRyPDAteVAVYAVPDPV 441
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
526-951 3.52e-12

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 71.46  E-value: 3.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRKPTIKPgdrvLLVHvPGLDF--IDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAK 603
Cdd:PRK04813    29 TYGQLKEDSDALAAFIDSLKLPDKSP----IIVF-GHMSPemLATFLGAVKAGHAYIPVDVSSPAER----IEMIIEVAK 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 lcnAVAILSTVGyhaavraglvknlISFTGKSVKstgqwpnlpwLHTDSWIKSSKVLPASnIAFQSESQPDDLCFLQFTS 683
Cdd:PRK04813   100 ---PSLIIATEE-------------LPLEILGIP----------VITLDELKDIFATGNP-YDFDHAVKGDDNYYIIFTS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGgLFTAMACGGSaiLFS-PLTFIRNPLMWLQT 762
Cdd:PRK04813   153 GTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMD-LYPTLASGGT--LVAlPKDMTANFKQLFET 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYK-ATHSAGPNFA-FELVIRRLEADKakarnydLSSMIFFMIAAE--PVR--QKTLKRFveltrPfglsQEVMAPGY 836
Cdd:PRK04813   230 LPQLPiNVWVSTPSFAdMCLLDPSFNEEH-------LPNLTHFLFCGEelPHKtaKKLLERF-----P----SATIYNTY 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  837 GLAENCVFVS--------CAYGKKKPIlvdwqgriccGYVDPndaDVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGY 908
Cdd:PRK04813   294 GPTEATVAVTsieitdemLDQYKRLPI----------GYAKP---DSPLLIIDEE--GTKLPDGEQGEIVISGPSVSKGY 358
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1917948728  909 WGKEELSQKTF--RNKLQNYpgrkytRTGDLGWVIQGNLFITGRI 951
Cdd:PRK04813   359 LNNPEKTAEAFftFDGQPAY------HTGDAGYLEDGLLFYQGRI 397
y4iL_like cd08152
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ...
1757-1993 3.87e-12

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: 69.60  E-value: 3.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1757 KGYLKLYDDiqgLPEH---DIFGPGKRYTVIVRHSNSLSADDDARL-DARGAALRIL---------SDDSPLLDLTLKTG 1823
Cdd:cd08152     16 KAEFTVLDD---LPPElaqGLFAEPGTYPAVIRFSNAPGDILDDSVpDPRGMAIKVLgvpgekllpEEDATTQDFVLVNH 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1824 KAFYARTISDFA--TWLVCGLAAREEHVKRVPH----VRDAVWTSLRQADSFADLH-----------YYSNTCrlFRFKD 1886
Cdd:cd08152     93 PVFFARDAKDYLalLKLLARTTSLPDGAKAALSaplrGALRVLEAAGGESPTLKLGghppahplgetYWSQAP--YRFGD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1887 RqemYVKFKLRPSDENIEEdigkvepsgiLPPETGAIPRDANDTRPLL--FLAEDfhnrvkspsGVRYIFQLQVRpipQD 1964
Cdd:cd08152    171 Y---VAKYSVVPASPALPA----------LTGKELDLTDDPDALREALadFLAEN---------DAEFEFRIQLC---TD 225
                          250       260
                   ....*....|....*....|....*....
gi 1917948728 1965 EAARDIAlDCTKPWDESQFPYIDVGEVII 1993
Cdd:cd08152    226 LEKMPIE-DASVEWPEALSPFVPVATITI 253
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
670-993 4.60e-12

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: 70.87  E-value: 4.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLcflQFTSGSTSDAKGVMITH-GGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDMGLIGgLFTAMACGGSAIL 746
Cdd:cd05929    124 EAAGWKM---LYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVL 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 ---FSPLTFirnplmwLQTISDYKATHSagpNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEP----VRQKTLKrfv 819
Cdd:cd05929    200 mekFDPEEF-------LRLIERYRVTFA---QFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppwVKEQWID--- 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  820 eltrpfgLSQEVMAPGYGLAEnCVFVSCAYGKkkpilvDWQ------GRICCGyvdpndadvDIRIVDADtGLEVdEDGK 893
Cdd:cd05929    267 -------WGGPIIWEYYGGTE-GQGLTIINGE------EWLthpgsvGRAVLG---------KVHILDED-GNEV-PPGE 321
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  894 EGEIWISsPSAGIGY-----WGKEELSQKTFRNklqnypgrkytrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADV 967
Cdd:cd05929    322 IGEVYFA-NGPGFEYtndpeKTAAARNEGGWST------------LGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEI 388
                          330       340
                   ....*....|....*....|....*.
gi 1917948728  968 EKTVESSSELLRpgcCAVIGVPEEVL 993
Cdd:cd05929    389 ENALIAHPKVLD---AAVVGVPDEEL 411
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
874-1068 5.31e-12

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 70.76  E-value: 5.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  874 DVDIRIVDadtGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK03640   315 PCELKIEK---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG--------WFKTGDIGYLdEEGFLYVLDRRS 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  953 DLIIVAGRNIYSADVEKTVESSSELLRPGccaVIGVPEEVLsakgislpdasdevGLVVIAELRDSKLVNKDIIKQIesr 1032
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAG---VVGVPDDKW--------------GQVPVAFVVKSGEVTEEELRHF--- 443
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1917948728 1033 vAEEHgvtVASVKliRPRTI------SKTTSGKIKRFEcLKQ 1068
Cdd:PRK03640   444 -CEEK---LAKYK--VPKRFyfveelPRNASGKLLRHE-LKQ 478
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
670-955 5.94e-12

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: 70.71  E-value: 5.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDMGLIgGLFTAMACGGsAILF 747
Cdd:cd17639     84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllGPDDRYLAYLPLAHIFELA-AENVCLYRGG-TIGY 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 -SPLTFI----RNPlmwLQTISDYKATHSAGPNFAFELVIRRLEAD------------------KAKARNYDLSSMIFFM 804
Cdd:cd17639    162 gSPRTLTdkskRGC---KGDLTEFKPTLMVGVPAIWDTIRKGVLAKlnpmgglkrtlfwtayqsKLKALKEGPGTPLLDE 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  805 IAAEPVRQKT-----------------LKRFVE-LTRPfglsqevMAPGYGLAEncvfvSCAYGkkkPILVDWQGRICCg 866
Cdd:cd17639    239 LVFKKVRAALggrlrymlsggaplsadTQEFLNiVLCP-------VIQGYGLTE-----TCAGG---TVQDPGDLETGR- 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  867 yVDPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnklqnypGRKYTRTGDLG-WVIQGN 944
Cdd:cd17639    303 -VGPPLPCCEIKLVDwEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFD-------GDGWFHTGDIGeFHPDGT 374
                          330
                   ....*....|.
gi 1917948728  945 LFITGRIKDLI 955
Cdd:cd17639    375 LKIIDRKKDLV 385
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
681-991 8.73e-12

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 70.11  E-value: 8.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGVM---ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMAcGGSAIL---FSPLTFir 754
Cdd:PRK12406   159 YTSGTTGHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL-GGVLVLqprFDPEEL-- 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 nplmwLQTISDYKATHSAGPNFAFelvIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAP 834
Cdd:PRK12406   236 -----LQLIERHRITHMHMVPTMF---IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYE 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 GYGLAENCVFVSCAYGK--KKPILVdwqGRICCGyvdpndadVDIRIVDADtGLEVdEDGKEGEIWISSPS-AGIGYWGK 911
Cdd:PRK12406   302 YYGSTESGAVTFATSEDalSHPGTV---GKAAPG--------AELRFVDED-GRPL-PQGEIGEIYSRIAGnPDFTYHNK 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  912 EELSQKTFRNKLqnypgrkyTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIG 987
Cdd:PRK12406   369 PEKRAEIDRGGF--------ITSGDVGYLDAdGYLFLCDRKRDMVISGGVNIYPAEIE------AVLHAvPGVhdCAVFG 434

                   ....
gi 1917948728  988 VPEE 991
Cdd:PRK12406   435 IPDA 438
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
673-1062 9.81e-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: 70.19  E-value: 9.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYH-------DMG-LIGGLFTAMAcgGSA 744
Cdd:cd05932    136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHvtervfvEGGsLYGGVLVAFA--ESL 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  745 ILF-------SPLTFIRNPLMWLQTisdYKATHSAGPNFAFEL-----VIRRLEADKAkARNYDLSSMIFFMIAAEPVRQ 812
Cdd:cd05932    214 DTFvedvqraRPTLFFSVPRLWTKF---QQGVQDKIPQQKLNLllkipVVNSLVKRKV-LKGLGLDQCRLAGCGSAPVPP 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  813 KTLkrfvELTRPFGLSqevMAPGYGLAENCvfvscAYGkkkpiLVDWQGRICCGYVDPNDADVDIRIVDadtglevdedg 892
Cdd:cd05932    290 ALL----EWYRSLGLN---ILEAYGMTENF-----AYS-----HLNYPGRDKIGTVGNAGPGVEVRISE----------- 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  893 kEGEIWISSPSAGIGYWGKEELSQKTFrnklqNYPGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVA-GRNIYSADVEKT 970
Cdd:cd05932    342 -DGEILVRSPALMMGYYKDPEATAEAF-----TADG--FLRTGDKGELdADGNLTITGRVKDIFKTSkGKYVAPAPIENK 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  971 VESSSellRPGCCAVIG------VPEEVLSAKGISLPDASDEvglvviAELRDSKlvnKDIIKQIESRVaEEHGVTVASV 1044
Cdd:cd05932    414 LAEHD---RVEMVCVIGsglpapLALVVLSEEARLRADAFAR------AELEASL---RAHLARVNSTL-DSHEQLAGIV 480
                          410       420
                   ....*....|....*....|.
gi 1917948728 1045 KLIRPRTISK---TTSGKIKR 1062
Cdd:cd05932    481 VVKDPWSIDNgilTPTLKIKR 501
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
673-1064 1.56e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 69.44  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHN--VKLMRRRYrsTSNTVLVSWLPQYHdmglIGGLFTAMA---CGGSAILF 747
Cdd:PLN02860   171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslAKIAIVGY--GEDDVYLHTAPLCH----IGGLSSALAmlmVGACHVLL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 spltfirnplmwlqtisdykathsagPNFAFELVIRRLEadkakarNYDLSSMIFF--MIA--AEPVRQK-TLKRFVELT 822
Cdd:PLN02860   245 --------------------------PKFDAKAALQAIK-------QHNVTSMITVpaMMAdlISLTRKSmTWKVFPSVR 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  823 RPF----GLSQEVMA------------PGYGLAENC---VFVS-------------CAYGKKKPILVDWQGRICCGYVDP 870
Cdd:PLN02860   292 KILngggSLSSRLLPdakklfpnaklfSAYGMTEACsslTFMTlhdptlespkqtlQTVNQTKSSSVHQPQGVCVGKPAP 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  871 NdadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIGYWG--KEELSQKTFRNKLQnypgrkytrTGDLGWVIQ-GNLFI 947
Cdd:PLN02860   372 H---VELKI-------GLDESSRVGRILTRGPHVMLGYWGqnSETASVLSNDGWLD---------TGDIGWIDKaGNLWL 432
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  948 TGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPEEVLSAKgislpdasdevglvVIAELR--------D 1017
Cdd:PLN02860   433 IGRSNDRIKTGGENVYPEEVEAVL-----SQHPGVasVVVVGVPDSRLTEM--------------VVACVRlrdgwiwsD 493
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1018 SKLVNKDIIKQIESRVAEEH-------GVTVASVKLIRPRTISKTTSGKIKRFE 1064
Cdd:PLN02860   494 NEKENAKKNLTLSSETLRHHcreknlsRFKIPKLFVQWRKPFPLTTTGKIRRDE 547
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
1569-2302 1.88e-11

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: 69.39  E-value: 1.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1569 THIKTWFGHQLAIACHVRFaklLSGTEAFCMYLRLLGAKVGRYCSIRAINP-IADprMVSIGAGVHLGDFSrIITGFYSQ 1647
Cdd:TIGR02353   79 TYLRFWTVKRLVDAAPTVL---LSGSPLYSLYLRALGAKIGKGVDIGSLPPvCTD--LLTIGAGTIVRKEV-MLLGYRAE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1648 SGYIQ-GNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGSQSpvmvkNTIHALDDRIEEMDPky 1726
Cdd:TIGR02353  153 RGRLHtGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPA-----QKTGADYRKVQPARP-- 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1727 kkivgnlaanlaattlkVKSRYFHRIGVSGKGYLKLYDDIQGLPEHDIFgpgkryTVIVRHSNSLsadddarldarGAAL 1806
Cdd:TIGR02353  226 -----------------YTVRRRLYVAGALFVVFVLLPPLAFLFAIPVA------ITFDEIDWTL-----------GPDM 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1807 RILSDdspLLDLTLKTGKAFYARTI-SDFATWLVCGLAAREEHVKRVPHVRDAVWT-SLRQADSFADLHYYSNTcrlfrf 1884
Cdd:TIGR02353  272 VGFIL---ALVLTFVALAGFIAYTVlLLAAVRLLLNLVLKPGRYYVHSGFYYQAWTvQQLMDNSRVLLFPLYAS------ 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1885 kdrqeMYVKFKLRpsdeNIEEDIGKVEPSGilpPETGAIPrDANDTRPLLFLAED--FHNRVKSPSGVRyIFQLQVRP-- 1960
Cdd:TIGR02353  343 -----SYIPHWYR----ALGAKIGKVAEIS---SAQHEVP-DLTDIGEETFIADGllMGNARLSGGWFR-LGRTRIGRrs 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1961 -------IPQDEAARDIALDCTKpwdeSQFPyIDvGEViiNENLTKEGSEKLEVNpflRCHEVDviratsssqsasiDHG 2033
Cdd:TIGR02353  409 flgnsgyYPPGAKTGDNVLLGVL----SMTP-KD-GKV--REGVGWLGSPPFELP---RRVNRD-------------DEL 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2034 RSLIYEicqhlrngdplPEAWRVFLeqsdvkvdlsgcpmaaaleRKDTEKVTLSRPWYLTTWAVFAQPL---LQTIVPYF 2110
Cdd:TIGR02353  465 EALTFE-----------PDPRRRLA-------------------RKNVENLRIILPFLLVQWAMLFALVvldLQALDDYT 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2111 LLGLIIyFPLNLLLhcknarnmpvhwtfpffwVSTGILAALTCAAAKYILVGKKKEDETVhIWSRGVFM-DTIWQAIRTV 2189
Cdd:TIGR02353  515 EWGAVA-LLAALIL------------------MAVGVGAFLILVERKWLVFGRLKPQEHP-LWSPFVWLhELHWKLYESV 574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2190 FGDYFVEMTSGSALFLMWMKLMGssVELDKGTYVDSmgaALNPE--MVEVEGGGSVEREALLFGHVYdgEGGAVKFGKIV 2267
Cdd:TIGR02353  575 AVPNFLRPFRGTPFLPAILRLLG--VKIGRGVYIDG---TDLTErdLVTIGDDSTLNEGSVIQTHLF--EDRVMKSDTVT 647
                          730       740       750
                   ....*....|....*....|....*....|....*..
gi 1917948728 2268 VGEGGFVGSRAVAMPGVESGGS--LSALSLAMKGEAI 2302
Cdd:TIGR02353  648 IGDGATLGPGAIVLYGVVMGEGsvLGPDSLVMKGEEV 684
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
497-1068 2.98e-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: 68.65  E-value: 2.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  497 LKHWAAQEIT----QNKALYtWINEGGAvGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLLV--HVPGLDFIDAff 570
Cdd:cd05928     12 LDQWADKEKAgkrpPNPALW-WVNGKGD-EVKWSFRELGSLSRKAANVL--SGACGLQRGDRVAVIlpRVPEWWLVNV-- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  571 GCLRAKVIPIP----VLPPDPLQR----GGQALTKIENIAKLCNAVAILSTvgyhaavraglvknliSFTGKSVKSTGQW 642
Cdd:cd05928     86 ACIRTGLVFIPgtiqLTAKDILYRlqasKAKCIVTSDELAPEVDSVASECP----------------SLKTKLLVSEKSR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  643 PNlpWLHTDSWIKSSKvlpASNIAFQSESQpdDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlVSWl 722
Cdd:cd05928    150 DG--WLNFKELLNEAS---TEHHCVETGSQ--EPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASD-IMW- 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  723 pQYHDMG----LIGGLFTAMACGGSAILFSPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIRRleadkakarnyDLS 798
Cdd:cd05928    221 -NTSDTGwiksAWSSLFEPWIQGACVFVHHLPRF--DPLVILKTLSSYPITTFCGAPTVYRMLVQQ-----------DLS 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  799 SMIF-----FMIAAEPVRQKTLKRFVELTrpfGLSqevMAPGYGLAEncVFVSCAYGKKKPILVDWQGRICCGYvdpnda 873
Cdd:cd05928    287 SYKFpslqhCVTGGEPLNPEVLEKWKAQT---GLD---IYEGYGQTE--TGLICANFKGMKIKPGSMGKASPPY------ 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  874 dvDIRIVDaDTGlEVDEDGKEGEIWIS-SPSAGIG----YWGKEELSQKTFRNKLQNypgrkytrTGDLGWVIQ-GNLFI 947
Cdd:cd05928    353 --DVQIID-DNG-NVLPPGTEGDIGIRvKPIRPFGlfsgYVDNPEKTAATIRGDFYL--------TGDRGIMDEdGYFWF 420
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  948 TGRIKDLIIVAGRNIYSADVEKtvesssellrpgccAVIGVPEEVLSAKgISLPDA-SDEV--GLVVIAElrDSKLVNKD 1024
Cdd:cd05928    421 MGRADDVINSSGYRIGPFEVES--------------ALIEHPAVVESAV-VSSPDPiRGEVvkAFVVLAP--QFLSHDPE 483
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1025 -IIKQIESRVAEehgvTVASVKLirPRTIS------KTTSGKIKRFECLKQ 1068
Cdd:cd05928    484 qLTKELQQHVKS----VTAPYKY--PRKVEfvqelpKTVTGKIQRNELRDK 528
PRK12316 PRK12316
peptide synthase; Provisional
526-937 6.33e-11

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 68.45  E-value: 6.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiaklc 605
Cdd:PRK12316  4578 TYAELNRRANRLAHALIAR---GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER---LAYMMED----- 4646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGyHAAVRAGLVKNLISFtgkSVKSTGQWPNLPwlHTDswiksskvlPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:PRK12316  4647 SGAALLLTQS-HLLQRLPIPDGLASL---ALDRDEDWEGFP--AHD---------PAVRLH------PDNLAYVIYTSGS 4705
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAIlfspltfIRNPLMWL----- 760
Cdd:PRK12316  4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVV-------IRDDSLWDperly 4777
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QTISDYKATHSAGPNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAE 840
Cdd:PRK12316  4778 AEIHEHRVTVLVFPPVYLQQLAEHAERDG------EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFN-----GYGPTE 4846
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NCVFVSCaygkkkpilvdwqgRICCGYVDPNDADVDIRIVDADTGLEVDED-------GKEGEIWISSPSAGIGYWGKEE 913
Cdd:PRK12316  4847 TTVTVLL--------------WKARDGDACGAAYMPIGTPLGNRSGYVLDGqlnplpvGVAGELYLGGEGVARGYLERPA 4912
                          410       420
                   ....*....|....*....|....
gi 1917948728  914 LSQKTFRNKLQNYPGRKYTRTGDL 937
Cdd:PRK12316  4913 LTAERFVPDPFGAPGGRLYRTGDL 4936
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
651-1062 6.84e-11

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: 67.55  E-value: 6.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  651 DSWIKSSKVLPASNIAFQSES--QPDDLCFLQFTSGSTSDAKGVMITHGGLIhnVKLMRRRYRSTSN-----TVLVSWLP 723
Cdd:cd17642    159 YTFITQNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNqiipdTAILTVIP 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  724 QYHDMGLIGGLFTAMaCGGSAIL---FSPLTFirnplmwLQTISDYKATHS--AGPNFAF----ELVirrleaDKakarn 794
Cdd:cd17642    237 FHHGFGMFTTLGYLI-CGFRVVLmykFEEELF-------LRSLQDYKVQSAllVPTLFAFfaksTLV------DK----- 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  795 YDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAENcvfvscaygkKKPILVDWQGRI---CCGYVDPN 871
Cdd:cd17642    298 YDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ-----GYGLTET----------TSAILITPEGDDkpgAVGKVVPF 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  872 dadVDIRIVDADTG--LEVDEdgkEGEIWISSPSAGIGYWGKEElSQKTFRNKlqnypgRKYTRTGDLG-WVIQGNLFIT 948
Cdd:cd17642    363 ---FYAKVVDLDTGktLGPNE---RGELCVKGPMIMKGYVNNPE-ATKALIDK------DGWLHSGDIAyYDEDGHFFIV 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  949 GRIKDLIIVAGRNIYSADVEKTVESSSELLRPGccaVIGVPEevlsakgislPDASDEVGLVVIAElRDSKLVNKDIIKQ 1028
Cdd:cd17642    430 DRLKSLIKYKGYQVPPAELESILLQHPKIFDAG---VAGIPD----------EDAGELPAAVVVLE-AGKTMTEKEVMDY 495
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1917948728 1029 IESRVAEEHGVTvASVKLIrpRTISKTTSGKIKR 1062
Cdd:cd17642    496 VASQVSTAKRLR-GGVKFV--DEVPKGLTGKIDR 526
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
672-971 7.53e-11

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: 67.38  E-value: 7.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  672 QPDDLCFLQFTSGSTSDAKGVMITHGGL----IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGsAILF 747
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYF 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 S-----------------PLTFIRNPLMW-----------------------------LQTISDYKATHSagPNFAFELV 781
Cdd:cd05933    227 AqpdalkgtlvktlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGES--PSPLFYRL 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  782 IRRLEADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGlsqevmaPGYGLAEN--CVFVSCAYGkkkpilvdw 859
Cdd:cd05933    305 AKKLVFKKVRKA-LGLDRCQKFFTGAAPISRETLEFFLSLNIPIM-------ELYGMSETsgPHTISNPQA--------- 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  860 QGRICCGYVDPNdadVDIRIVdadtglEVDEDGkEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGW 939
Cdd:cd05933    368 YRLLSCGKALPG---CKTKIH------NPDADG-IGEICFWGRHVFMGYLNMEDKTEEAIDED-------GWLHSGDLGK 430
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1917948728  940 V-IQGNLFITGRIKDLIIVA-GRNIYSADVEKTV 971
Cdd:cd05933    431 LdEDGFLYITGRIKELIITAgGENVPPVPIEDAV 464
PRK05857 PRK05857
fatty acid--CoA ligase;
527-1062 1.18e-10

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 66.57  E-value: 1.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  527 YAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkienIAK 603
Cdd:PRK05857    44 YRELVAEVGGLAADL---RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAdgnLPIAAIER----------FCQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 LCNAVAILSTVGYHAAvRAGLVKNLISFTGKSVKSTGQwpnlpwlHTDSWIKSSKVLPASNIafqsESQPDDLCFLQFTS 683
Cdd:PRK05857   111 ITDPAAALVAPGSKMA-SSAVPEALHSIPVIAVDIAAV-------TRESEHSLDAASLAGNA----DQGSEDPLAMIFTS 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMR----RRYRSTSNTVLVSWLPQYHdmglIGGLFTAMAC---GGSAIlfsplTFIRNP 756
Cdd:PRK05857   179 GTTGEPKAVLLANRTFFAVPDILQkeglNWVTWVVGETTYSPLPATH----IGGLWWILTClmhGGLCV-----TGGENT 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  757 LMWLQTISDYK-ATHSAGPNFAFELVirrleaDKAKARNYDLSSMIFF------MIAAEpvrqktlKRFVELTrpfGLSQ 829
Cdd:PRK05857   250 TSLLEILTTNAvATTCLVPTLLSKLV------SELKSANATVPSLRLVgyggsrAIAAD-------VRFIEAT---GVRT 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  830 evmAPGYGLAENCVFVSCAYGKKKPIlvdwqGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKE----GEIWISSPSAG 905
Cdd:PRK05857   314 ---AQVYGLSETGCTALCLPTDDGSI-----VKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfGTLWIKSPANM 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 IGYWGKEElsqktfrnklqnypgrkytRTGDL---GWVIQGNL---------FITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:PRK05857   386 LGYWNNPE-------------------RTAEVlidGWVNTGDLlerredgffYIKGRSSEMIICGGVNIAPDEVDRIAEG 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  974 ssellrpgccaVIGVPEevlsAKGISLPDA--SDEVGLVVIAelrdSKLVNKDIIKQIESRVAEEHGVTVASVKliRPRT 1051
Cdd:PRK05857   447 -----------VSGVRE----AACYEIPDEefGALVGLAVVA----SAELDESAARALKHTIAARFRRESEPMA--RPST 505
                          570
                   ....*....|....*..
gi 1917948728 1052 ------ISKTTSGKIKR 1062
Cdd:PRK05857   506 ivivtdIPRTQSGKVMR 522
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
526-991 1.70e-10

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: 65.99  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLtSRKPtiKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGGQALTKIENiAKLC 605
Cdd:cd05923     30 TYSELRARIEAVAARLH-ARGL--RPGQRVAVVLPNSVEAVIALLALHRLGAVPALI---NPRLKAAELAELIER-GEMT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAilstvgyhaAVRAGLVKNLISFTGKsVKSTGQWPNLPWLHTDSwikssKVLPASniafqsESQPDDLCFLQFTSGS 685
Cdd:cd05923    103 AAVI---------AVDAQVMDAIFQSGVR-VLALSDLVGLGEPESAG-----PLIEDP------PREPEQPAFVFYTSGT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRR--YRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPltfiRNPLMWL 760
Cdd:cd05923    162 TGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVveeFDP----ADALKLI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  761 QT--ISDYKAThsagPNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRF-----VELTRPFGlSQEVM- 832
Cdd:cd05923    238 EQerVTSLFAT----PTHLDALAAAAEFAGL------KLSSLRHVTFAGATMPDAVLERVnqhlpGEKVNIYG-TTEAMn 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  833 -------APGYGLaencvfvscaygkkKPilvdwqgriccGYVDpndadvDIRIVDADTG-LEVDEDGKEGEIWI--SSP 902
Cdd:cd05923    307 slymrdaRTGTEM--------------RP-----------GFFS------EVRIVRIGGSpDEALANGEEGELIVaaAAD 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  903 SAGIGYWGKEELSQKTFRNklqnypgRKYtRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVEssselLRPG 981
Cdd:cd05923    356 AAFTGYLNQPEATAKKLQD-------GWY-RTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLS-----RHPG 422
                          490
                   ....*....|..
gi 1917948728  982 C--CAVIGVPEE 991
Cdd:cd05923    423 VteVVVIGVADE 434
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
682-1064 2.00e-10

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 65.56  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRS---TSNTVLVSWLPqyhdMGL-IGGLFTAMAC---GGSAILFSPLtfir 754
Cdd:COG1541     91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAagvRPGDRVQNAFG----YGLfTGGLGLHYGAerlGATVIPAGGG---- 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLMWLQTISDYKATHSAG-PNFAFELvIRRLEADKAKARNYDLSSMIFfmiAAEPVRQKTLKRFVELtrpFGLsqEVMA 833
Cdd:COG1541    163 NTERQLRLMQDFGPTVLVGtPSYLLYL-AEVAEEEGIDPRDLSLKKGIF---GGEPWSEEMRKEIEER---WGI--KAYD 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  834 pGYGLAE--NCVFVSCAYgkkKPILVDWQGRIccgYVDpndadvdirIVDADTGlEVDEDGKEGEIWISS------Psag 905
Cdd:COG1541    234 -IYGLTEvgPGVAYECEA---QDGLHIWEDHF---LVE---------IIDPETG-EPVPEGEEGELVVTTltkeamP--- 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 igywgkeelsqktfrnkLQNYpgrkytRTGDLGWVIQGN----------LFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:COG1541    294 -----------------LIRY------RTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  976 ELlrpGCCAVIGVPEEvlsakgislpDASDEvgLVVIAELRDsKLVNKDIIKQIESRVAEEHGVTVAsVKLIRPRTISKT 1055
Cdd:COG1541    351 EV---GPEYQIVVDRE----------GGLDE--LTVRVELAP-GASLEALAEAIAAALKAVLGLRAE-VELVEPGSLPRS 413

                   ....*....
gi 1917948728 1056 TsGKIKRFE 1064
Cdd:COG1541    414 E-GKAKRVI 421
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
526-973 2.42e-10

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: 65.30  E-value: 2.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd12117     24 TYAELNERANRLARRL---RAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER-------LAFMLADA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAGLVknlisftgksvkstgqwpnlPWLHTDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:cd12117     94 GAKVLLTDRSLAGRAGGLEV--------------------AVVIDEALDAGPAGNPAVPVS------PDDLAYVMYTSGS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKlmRRRYRS-TSNTVLVSWLPQYHDMGLIGgLFTAMACGGSAILFSPLTFIRnplmwLQTIS 764
Cdd:cd12117    148 TGRPKGVAVTHRGVVRLVK--NTNYVTlGPDDRVLQTSPLAFDASTFE-IWGALLNGARLVLAPKGTLLD-----PDALG 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  765 DYKATHsaGPNFAFelvirrleadkakarnydLSSMIFFMIAAE-PVRQKTLKRFVeltrpFGlsQEVMAP--------- 834
Cdd:cd12117    220 ALIAEE--GVTVLW------------------LTAALFNQLADEdPECFAGLRELL-----TG--GEVVSPphvrrvlaa 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  835 --------GYGLAENCVFvSCAYGKKKPilvdwqgriccgyvDPNDADVDI-RIVDADTGLEVDEDGK------EGEIWI 899
Cdd:cd12117    273 cpglrlvnGYGPTENTTF-TTSHVVTEL--------------DEVAGSIPIgRPIANTRVYVLDEDGRpvppgvPGELYV 337
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  900 SSPSAGIGYWGKEELSQKTF-RNKLQnyPGRKYTRTGDL-GWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:cd12117    338 GGDGLALGYLNRPALTAERFvADPFG--PGERLYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
srpA_like cd08153
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ...
1778-1994 3.08e-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: 63.79  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1778 GKRYTVIVRHSNS--LSADDDARLDARGAALRILSDDSPLLDLTLKTGKAFYARTISDFATWLVCGL---------AARE 1846
Cdd:cd08153     45 GGSVPVTGRFSLGggNPKAPDDAANPRGMALKFRLPDGEQWRMVMNSFPVFPVRTPEEFLALLKAIApdatgkpdpAKLK 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1847 EHVKRVPHVRDAVwTSLRQA---DSFADLHYYS-NTcrlFRFKDRQ--EMYVKFKLRPSDenieedigkvEPSGILPPET 1920
Cdd:cd08153    125 AFLAAHPEAAAFL-AWIKTApppASFANTTYYGvNA---FYFTNANgkRQPVRWRFVPED----------GVKYLSDEEA 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 1921 GAIPRDandtrpllFLAEDFHNRVKS-PsgVRYIFQLQVrPIPQDEAArdialDCTKPWDESQfPYIDVGEVIIN 1994
Cdd:cd08153    191 AKLGPD--------FLFDELAQRLAQgP--VRWDLVLQL-AEPGDPTD-----DPTKPWPADR-KEVDAGTLTIT 248
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
32-264 5.06e-10

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: 64.43  E-value: 5.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   32 SGLSAAYALAKLGyRDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLaANSAPVIFHLAKESGTELEE--MDLHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGLEDRLvlPDPAPFYTVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  110 SFTGEYHDINVAEDYMSLVSL-----TLEIQDKAK---DSNHIGIHAVSDIASDLTPAYLEAHGIKSVPKSVQYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRlglAALASDALDEFDLDDFSLAESLLFLGRRGPGDVEVWDRLIDP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRMKGGYMSLWKKISKSLL---IKVccNTEVQAVRRDGSD 242
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRL--NTRVRSIDREGDG 236
                          250       260
                   ....*....|....*....|..
gi 1917948728  243 VNVDITNSsgetEHKEFDKIII 264
Cdd:pfam01593  237 VTVTLTDG----EVIEADAVIV 254
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1124-1185 7.23e-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: 7.23e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1124 EFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1185
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK07788 PRK07788
acyl-CoA synthetase; Validated
524-991 8.88e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 63.79  E-value: 8.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLR--AKVIpipvlppdpLQRGGQALTKIENI 601
Cdd:PRK07788    74 TLTYAELDEQSNALARGLLAL---GVRAGDGVAVLARNHRGFVLALYAAGKvgARII---------LLNTGFSGPQLAEV 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  602 AKLCNAVAILSTVGYHAAVRA-----GLVKNLISFTGKSVKSTGQWPNLpwlhtDSWI--KSSKVLPASniafqseSQPD 674
Cdd:PRK07788   142 AAREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETL-----DDLIagSSTAPLPKP-------PKPG 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLqfTSGSTSDAKGVMITH-------GGLIHNVKLmrrryRSTSNTVLVSwlPQYHDMGLiGGLFTAMACGGSAIL- 746
Cdd:PRK07788   210 GIVIL--TSGTTGTPKGAPRPEpsplaplAGLLSRVPF-----RAGETTLLPA--PMFHATGW-AHLTLAMALGSTVVLr 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 --FSPLTFIRNplmwlqtISDYKAThsagpnfafELVI------RRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:PRK07788   280 rrFDPEATLED-------IAKHKAT---------ALVVvpvmlsRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRA 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  819 VELtrpFGlsqEVMAPGYGLAEnCVFVSCAYGK---KKPILVdwqGRICCGyvdpndadVDIRIVDADtGLEVDEdGKEG 895
Cdd:PRK07788   344 LEA---FG---PVLYNLYGSTE-VAFATIATPEdlaEAPGTV---GRPPKG--------VTVKILDEN-GNEVPR-GVVG 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  896 EIWISSPSAGIGYWGKeelsqktfRNKlQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvess 974
Cdd:PRK07788   404 RIFVGNGFPFEGYTDG--------RDK-QIIDG--LLSSGDVGYFDEdGLLFVDGRDDDMIVSGGENVFPAEVE------ 466
                          490       500
                   ....*....|....*....|.
gi 1917948728  975 sELL--RPGC--CAVIGVPEE 991
Cdd:PRK07788   467 -DLLagHPDVveAAVIGVDDE 486
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
673-990 1.63e-09

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 62.78  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLihnvkLMRRRYRS-----TSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL- 746
Cdd:PRK08008   172 TDDTAEILFTSGTTSRPKGVVITHYNL-----RFAGYYSAwqcalRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLl 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 --FSPLTFirnplmWLQtISDYKATHSAgpnfAFELVIRRLEADKAKA--RNYDLSSMIFFMIAAEPVRQKTLKRF-VEL 821
Cdd:PRK08008   247 ekYSARAF------WGQ-VCKYRATITE----CIPMMIRTLMVQPPSAndRQHCLREVMFYLNLSDQEKDAFEERFgVRL 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  822 TRPFGLSQEVMA-----PGyglaencvfvscayGKKKpilvdWQ--GRICCGYvdpndadvDIRIVDADtGLEVDEdGKE 894
Cdd:PRK08008   316 LTSYGMTETIVGiigdrPG--------------DKRR-----WPsiGRPGFCY--------EAEIRDDH-NRPLPA-GEI 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 GEIWISS-PSAGI--GYWGKEELSQKTFRnklqnypGRKYTRTGDLGWVIQGNLF-ITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK08008   367 GEICIKGvPGKTIfkEYYLDPKATAKVLE-------ADGWLHTGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENI 439
                          330       340
                   ....*....|....*....|
gi 1917948728  971 VESSSELLRpgcCAVIGVPE 990
Cdd:PRK08008   440 IATHPKIQD---IVVVGIKD 456
PRK12467 PRK12467
peptide synthase; Provisional
526-970 1.64e-09

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 64.03  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGgQALTKIENIAKLC 605
Cdd:PRK12467   539 SYAELNRQANRLAHVLIAA---GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL-AYMLDDSGVRLLL 614
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVGYHAAVRAgLVKNLISftgksvkstgqwpnlpwlhtDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:PRK12467   615 TQSHLLAQLPVPAGLRS-LCLDEPA--------------------DLLCGYSGHNPEVALD------PDNLAYVIYTSGS 667
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQTISD 765
Cdd:PRK12467   668 TGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPPDC-ARDAEAFAALMAD 745
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  766 YKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEL---TRPFGLsqevmapgYGLAENC 842
Cdd:PRK12467   746 QGVT-------VLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALgpgARLINH--------YGPTETT 810
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  843 VFVScaygkkkpilvdwQGRICCGYVDPND-------ADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:PRK12467   811 VGVS-------------TYELSDEERDFGNvpigqplANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRRPALT 875
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  916 QKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK12467   876 AERFVPDPFGADGGRLYRTGDLArYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
524-968 1.88e-09

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: 62.27  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAK 603
Cdd:cd17652     12 TLTYAELNARANRLARLLAAR---GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER-------IAYMLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 LCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTS 683
Cdd:cd17652     82 DARPALLLT-----------------------------------------------------------TPDNLAYVIYTS 102
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLvswlpQYHDMGLIGG---LFTAMACGGSAILFSPLTFIR-NPLm 758
Cdd:cd17652    103 GSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVL-----QFASPSFDASvweLLMALLAGATLVLAPAEELLPgEPL- 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  759 wLQTISDYKATHSAGPNFAfelvIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevMAPGYGL 838
Cdd:cd17652    177 -ADLLREHRITHVTLPPAA----LAALPPD-------DLPDLRTLVVAGEACPAELVDRWAPGRR--------MINAYGP 236
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  839 AENCVFVSCAY----GKKKPILVDWQGriccgyvdpndadVDIRIVDAdtGLEVDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd17652    237 TETTVCATMAGplpgGGVPPIGRPVPG-------------TRVYVLDA--RLRPVPPGVPGELYIAGAGLARGYLNRPGL 301
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728  915 SQKTFrnkLQN---YPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17652    302 TAERF---VADpfgAPGSRMYRTGDLArWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
PRK12316 PRK12316
peptide synthase; Provisional
526-968 1.90e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 63.82  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALtkieniaklc 605
Cdd:PRK12316  2030 SYAELDSRANRLAHRL---RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML---------- 2096
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navailstvgyhAAVRAGLvknLISFTGKSVK--STGQWPNLPWLHTDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTS 683
Cdd:PRK12316  2097 ------------EDSGAAL---LLTQRHLLERlpLPAGVARLPLDRDAEWADYPDTAPAVQLA------GENLAYVIYTS 2155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYR-STSNTVLvSWLPQYHDmGLIGGLFTAMaCGGSAILFSPLTfIRNPLMWLQT 762
Cdd:PRK12316  2156 GSTGLPKGVAVSHGALVAHCQAAGERYElSPADCEL-QFMSFSFD-GAHEQWFHPL-LNGARVLIRDDE-LWDPEQLYDE 2231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  763 ISDYKATHSAGPNFAFELVIRRLEAD--KAKARNYDLSsmiffmiaAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAE 840
Cdd:PRK12316  2232 MERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFG--------GEAVPAASLRLAWEALRPVYLFN-----GYGPTE 2298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  841 NCVFVSCaygkkkpilvdWQgricCGYVDPNDA----------DVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWG 910
Cdd:PRK12316  2299 AVVTPLL-----------WK----CRPQDPCGAayvpigralgNRRAYILDAD--LNLLAPGMAGELYLGGEGLARGYLN 2361
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728  911 KEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12316  2362 RPGLTAERFVPDPFSASGERLYRTGDLArYRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
PRK07798 PRK07798
acyl-CoA synthetase; Validated
524-991 2.06e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 62.60  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkien 600
Cdd:PRK07798    28 RLTYAELEERANRLAHYLIAQ---GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVEDELRY---------- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  601 IAKLCNAVAILstvgYHAAVrAGLVKNLIsftgksvkstgqwPNLPWLHTdsWIK----SSKVLPASNIAFQS------- 669
Cdd:PRK07798    95 LLDDSDAVALV----YEREF-APRVAEVL-------------PRLPKLRT--LVVvedgSGNDLLPGAVDYEDalaagsp 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 -----ESQPDDLCFLqFTSGSTSDAKGVMITH--------GGL-------IHNVKLMRRRYRSTSNTVLVSWLPQYHDMG 729
Cdd:PRK07798   155 erdfgERSPDDLYLL-YTGGTTGMPKGVMWRQedifrvllGGRdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  730 LIGGlFTAMACGGSAILFSPLTFirNPLMWLQTISDYKATHSA--GPNFAfelviRRLEADKAKARNYDLSSMifFMIA- 806
Cdd:PRK07798   234 QWAA-FAALFSGQTVVLLPDVRF--DADEVWRTIEREKVNVITivGDAMA-----RPLLDALEARGPYDLSSL--FAIAs 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  807 -AEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAE--NCVFVSCAYGKKKpilvDWQGRIccgyvdpnDADVDIRIVDAD 883
Cdd:PRK07798   304 gGALFSPSVKEALLEL-----LPNVVLTDSIGSSEtgFGGSGTVAKGAVH----TGGPRF--------TIGPRTVVLDED 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  884 TGLEVDEDGKEGeiWIS-SPSAGIGYWGKEELSQKTFRnklqNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRN 961
Cdd:PRK07798   367 GNPVEPGSGEIG--WIArRGHIPLGYYKDPEKTAETFP----TIDGVRYAIPGDRArVEADGTITLLGRGSVCINTGGEK 440
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1917948728  962 IYSADVEktvesssELLR--PGC--CAVIGVPEE 991
Cdd:PRK07798   441 VFPEEVE-------EALKahPDVadALVVGVPDE 467
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
653-750 3.64e-09

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 62.03  E-value: 3.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  653 WIKSSKVLPASNIAFQsesQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG 732
Cdd:PRK08043   347 WIFAHLLMPRLAQVKQ---QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTV 423
                           90
                   ....*....|....*....
gi 1917948728  733 GLFTAMACGGSAILF-SPL 750
Cdd:PRK08043   424 GLFTPLLTGAEVFLYpSPL 442
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
23-60 3.87e-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: 61.30  E-value: 3.87e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:COG0493    123 KVAVVGSGPAGLAAAYQLARAGH-EVTVFEALDKPGGL 159
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
875-1062 4.43e-09

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: 61.81  E-value: 4.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  875 VDIRIVDADTGlEVDEDGkEGEIWISSPSAGI--GYWGKEELSQKTFrnkLQNYPGrkYTRTGDlGWVI--QGNLFITGR 950
Cdd:cd05966    419 IEPAILDEEGN-EVEGEV-EGYLVIKRPWPGMarTIYGDHERYEDTY---FSKFPG--YYFTGD-GARRdeDGYYWITGR 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  951 IKDLIIVAGRNIYSADVEktvesSSELLRPGC--CAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQ 1028
Cdd:cd05966    491 VDDVINVSGHRLGTAEVE-----SALVAHPAVaeAAVVGRPHDI---KGEAI------YAFVT---LKDGEEPSDELRKE 553
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1917948728 1029 IESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1062
Cdd:cd05966    554 LRKHVRKEIG------PIATPDKIqfvpglPKTRSGKIMR 587
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
497-919 4.62e-09

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: 61.68  E-value: 4.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  497 LKHWAAQEITQnkalyTWINEGGAVGCQR--TYAELDSNASCVAHKLLtSRKptIKPGDRVLLVHVPGLDFIDAFFGCLR 574
Cdd:cd05921      1 LAHWARQAPDR-----TWLAEREGNGGWRrvTYAEALRQVRAIAQGLL-DLG--LSAERPLLILSGNSIEHALMALAAMY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  575 AKVIPIPVLPPDPLQrgGQALTKIENIAKLCN--AVAILSTVGYHAAVRAGL---VKNLISFTGKSVKSTGQWPNLpwLH 649
Cdd:cd05921     73 AGVPAAPVSPAYSLM--SQDLAKLKHLFELLKpgLVFAQDAAPFARALAAIFplgTPLVVSRNAVAGRGAISFAEL--AA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  650 TDSWIKSSKVLPASniafqsesQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMR--RRYRSTSNTVLVSWLPQYHD 727
Cdd:cd05921    149 TPPTAAVDAAFAAV--------GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqtYPFFGEEPPVLVDWLPWNHT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  728 MGLIGGLFTAMACGGSAILF----SPLTF---IRNplmwLQTIS-DYKATHSAGpnfaFELVIRRLEADKAKARNYdLSS 799
Cdd:cd05921    221 FGGNHNFNLVLYNGGTLYIDdgkpMPGGFeetLRN----LREISpTVYFNVPAG----WEMLVAALEKDEALRRRF-FKR 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  800 MIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKkkpilvdwQGRIccGYVDPNDADVDIRI 879
Cdd:cd05921    292 LKLMFYAGAGLSQDVWDRLQALAVATVGERIPMMAGLGATETAPTATFTHWP--------TERS--GLIGLPAPGTELKL 361
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1917948728  880 VDADTGLEVDEDGkegeiwissPSAGIGYWGKEELSQKTF 919
Cdd:cd05921    362 VPSGGKYEVRVKG---------PNVTPGYWRQPELTAQAF 392
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
673-954 4.72e-09

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: 61.46  E-value: 4.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNV----KLMRRRYRSTSNTVLVSWLPQYHdmgliggLF-----TAMACGGS 743
Cdd:cd05927    113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAH-------IFervveALFLYHGA 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  744 AILF---------------SPLTFIRNPLMwLQTISD-YKATHSAGP-------NFAFELVIRRLEA------------- 787
Cdd:cd05927    186 KIGFysgdirlllddikalKPTVFPGVPRV-LNRIYDkIFNKVQAKGplkrklfNFALNYKLAELRSgvvraspfwdklv 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  788 -DKAKARnydLSSMIFFMI-AAEPVRQKTLKRfveLTRPFGLsqEVMApGYGLAENCVFVSCAygkkkpilvdWQGRICC 865
Cdd:cd05927    265 fNKIKQA---LGGNVRLMLtGSAPLSPEVLEF---LRVALGC--PVLE-GYGQTECTAGATLT----------LPGDTSV 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  866 GYVDPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypGrkYTRTGDLG-WVIQG 943
Cdd:cd05927    326 GHVGGPLPCAEVKLVDvPEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED-----G--WLHTGDIGeWLPNG 398
                          330
                   ....*....|.
gi 1917948728  944 NLFITGRIKDL 954
Cdd:cd05927    399 TLKIIDRKKNI 409
PRK07233 PRK07233
hypothetical protein; Provisional
23-68 6.59e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 60.67  E-value: 6.59e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEG 68
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGG 45
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
670-954 1.11e-08

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: 60.51  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVlVSWLPQYHDMGLIGGLFTAMACGgSAILF- 747
Cdd:cd17641    154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLgHCAAYLAADPLGPGDEY-VSVLPLPWIGEQMYSVGQALVCG-FIVNFp 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 -SPLTFIRNplmwLQTIsdykathsaGPNFAFeLVIRRLEADKAKARNYdlssmiffMIAAEPVRQKTLKRFVELTR--- 823
Cdd:cd17641    232 eEPETMMED----LREI---------GPTFVL-LPPRVWEGIAADVRAR--------MMDATPFKRFMFELGMKLGLral 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  824 PFGLSQEVMAPG----YGLAENCVF-----------VSCAYGKKKPILVD----------------WQGRICCGYVDPND 872
Cdd:cd17641    290 DRGKRGRPVSLWlrlaSWLADALLFrplrdrlgfsrLRSAATGGAALGPDtfrffhaigvplkqlyGQTELAGAYTVHRD 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  873 ADVDIRIVD---ADTGLEVDEdgkEGEIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWVIQ-GNLFIT 948
Cdd:cd17641    370 GDVDPDTVGvpfPGTEVRIDE---VGEILVRSPGVFVGYYKNPEATAEDF-------DEDGWLHTGDAGYFKEnGHLVVI 439

                   ....*.
gi 1917948728  949 GRIKDL 954
Cdd:cd17641    440 DRAKDV 445
PRK12467 PRK12467
peptide synthase; Provisional
524-968 1.16e-08

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 60.95  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiak 603
Cdd:PRK12467  1599 ELTYGELNRRANRLAHRLIAL---GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER---LAYMIED--- 1669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  604 lcNAVAILSTvgyHAAVRAGLVknlisfTGKSVKSTGQWPNLPWLHTDSwikssKVLPASNIAfqsesqPDDLCFLQFTS 683
Cdd:PRK12467  1670 --SGIELLLT---QSHLQARLP------LPDGLRSLVLDQEDDWLEGYS-----DSNPAVNLA------PQNLAYVIYTS 1727
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTI 763
Cdd:PRK12467  1728 GSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS-VWELFWPLINGARLVIAPPGAH-RDPEQLIQLI 1805
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  764 SDYKATHSAGPNFAFELVirrLEADKAKARNYDLSSMIFfmiAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAENCV 843
Cdd:PRK12467  1806 ERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVC---GGEALEVEALRPWLERLPDTGLFN-----LYGPTETAV 1874
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  844 FVScaygKKKPILVDWQGRICCGYVDPNdADVDIRIVDAdtGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKL 923
Cdd:PRK12467  1875 DVT----HWTCRRKDLEGRDSVPIGQPI-ANLSTYILDA--SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADP 1947
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1917948728  924 QNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12467  1948 FGTVGSRLYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
PLN03102 PLN03102
acyl-activating enzyme; Provisional
660-989 2.20e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 59.26  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  660 LPASNIAFQSESQPDDLcflQFTSGSTSDAKGVMITHGGlihnvklmrrRYRSTSNTVlVSW-----------LPQYHDM 728
Cdd:PLN03102   175 LVARMFRIQDEHDPISL---NYTSGTTADPKGVVISHRG----------AYLSTLSAI-IGWemgtcpvylwtLPMFHCN 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  729 GLIGGLFTAmACGGSAILFSPLTfirNPLMWlQTISDYKATHSAGPNFAFELVIRRLEADKAKArnydlSSMIFFMIAAE 808
Cdd:PLN03102   241 GWTFTWGTA-ARGGTSVCMRHVT---APEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPR-----SGPVHVLTGGS 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  809 PVRQKTLKRFVELtrpfGLsqEVMApGYGLAEncvfvscAYGkkkPIL-VDWQG-------------RICCGYVDPNDAD 874
Cdd:PLN03102   311 PPPAALVKKVQRL----GF--QVMH-AYGLTE-------ATG---PVLfCEWQDewnrlpenqqmelKARQGVSILGLAD 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  875 VDIRivDADTGLEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNKLQNypgrkytrTGDLGwVIQ--GNLFITGRI 951
Cdd:PLN03102   374 VDVK--NKETQESVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLN--------TGDVG-VIHpdGHVEIKDRS 442
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1917948728  952 KDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVP 989
Cdd:PLN03102   443 KDIIISGGENISSVEVENVLYKYPKVLE---TAVVAMP 477
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
873-1080 2.21e-08

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 59.41  E-value: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  873 ADVDIRIVDADTGLEvDEDGKEGEIWISSPSAGIGYW----GKEELSQKTFRNKLQNYPGRKYT-----RTGDLGWVIQ- 942
Cdd:PRK05620   365 ASLEYRIVNDGQVME-STDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFTadgwlRTGDVGSVTRd 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  943 GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE---------VLSAKGISLPDASDEvglvvia 1013
Cdd:PRK05620   444 GFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE---CAVIGYPDDkwgerplavTVLAPGIEPTRETAE------- 513
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1014 ELRDSklvnkdIIKQIESRVAEEHGVTVASvklirprtISKTTSGKIKRFECLKQFVDGNLN--TVPDP 1080
Cdd:PRK05620   514 RLRDQ------LRDRLPNWMLPEYWTFVDE--------IDKTSVGKFDKKDLRQHLADGDFEiiKLKGP 568
PRK13382 PRK13382
bile acid CoA ligase;
642-991 2.36e-08

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 59.39  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  642 WPNLPWLHTdswiksSKVLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVK--LMRRRYRSTSNTVLV 719
Cdd:PRK13382   170 WTDEDHDLT------VEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKaiLDRTPWRAEEPTVIV 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  720 SwlPQYHDMGLIGGLFTA-MACggsailfsPLTFIR--NPLMWLQTISDYKATHSAGPNFAFElviRRLEADKAKARNYD 796
Cdd:PRK13382   244 A--PMFHAWGFSQLVLAAsLAC--------TIVTRRrfDPEATLDLIDRHRATGLAVVPVMFD---RIMDLPAEVRNRYS 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  797 LSSMIFFMIAAEPVRQKTLKRFVEltrPFGlsqEVMAPGYGLAEnCVFVSCAYGKKKPILVDWQGRiccgyvdPNDAdVD 876
Cdd:PRK13382   311 GRSLRFAAASGSRMRPDVVIAFMD---QFG---DVIYNNYNATE-AGMIATATPADLRAAPDTAGR-------PAEG-TE 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  877 IRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKeelSQKTFRNKlqnypgrkYTRTGDLG-WVIQGNLFITGRIKDLI 955
Cdd:PRK13382   376 IRILDQD-FREV-PTGEVGTIFVRNDTQFDGYTSG---STKDFHDG--------FMASGDVGyLDENGRLFVVGRDDEMI 442
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1917948728  956 IVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK13382   443 VSGGENVYPIEVEKTLATHPDVAE---AAVIGVDDE 475
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
13-60 3.47e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 58.73  E-value: 3.47e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1917948728   13 KLHPCLPlDT--RIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGM 60
Cdd:PRK12771   128 KFPAPAP-DTgkRVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGM 175
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
674-1063 4.69e-08

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: 57.91  E-value: 4.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLvsWlpQYHDMGLIGGLFTA----MACGGSAIL--- 746
Cdd:cd05973     88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--W--NAADPGWAYGLYYAitgpLALGHPTILleg 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  747 -FSPltfirnPLMWlQTISDYKATHSAGPNFAFelviRRLEADKAKARNYDLSSMIFFMIAAEPVRQktlkrfvELTRPF 825
Cdd:cd05973    164 gFSV------ESTW-RVIERLGVTNLAGSPTAY----RLLMAAGAEVPARPKGRLRRVSSAGEPLTP-------EVIRWF 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  826 GLSQEV-MAPGYGLAENCVFVSCAYGKKKPILVDWQGRICCGYvdpndadvdiRI-VDADTGLEVDEdGKEGEIWI---S 900
Cdd:cd05973    226 DAALGVpIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGW----------RVaVLDDDGDELGP-GEPGRLAIdiaN 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  901 SPSAGI-GYWGKEelsQKTFrnklqnyPGRKYtRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesSSELL 978
Cdd:cd05973    295 SPLMWFrGYQLPD---TPAI-------DGGYY-LTGDTVEFdPDGSFSFIGRADDVITMSGYRIGPFDVE-----SALIE 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  979 RPGC--CAVIGVPE----EVLSAkgislpdasdevgLVVIAE-LRDSKLVNKDIIKQIESRVAeEHGvtvasvkliRPRT 1051
Cdd:cd05973    359 HPAVaeAAVIGVPDpertEVVKA-------------FVVLRGgHEGTPALADELQLHVKKRLS-AHA---------YPRT 415
                          410
                   ....*....|....*...
gi 1917948728 1052 IS------KTTSGKIKRF 1063
Cdd:cd05973    416 IHfvdelpKTPSGKIQRF 433
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
526-973 6.46e-08

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: 57.71  E-value: 6.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGqaltkieniaklc 605
Cdd:cd12115     26 TYAELNRRANRLAARL---RAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLR------------- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 navAILSTvgyhAAVRAGLVknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd12115     90 ---FILED----AQARLVLT----------------------------------------------DPDDLAYVIYTSGS 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLihnVKLMRRRYRSTSNTVLVSWL---PQYHDMGlIGGLFTAMACGGSAILF-SPLTFIRNP----L 757
Cdd:cd12115    117 TGRPKGVAIEHRNA---AAFLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVVLAdNVLALPDLPaaaeV 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  758 MWLQTIsdykathsagPNFAFELVirRLEADKAKARNYDLssmiffmiAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYG 837
Cdd:cd12115    193 TLINTV----------PSAAAELL--RHDALPASVRVVNL--------AGEPLPRDLVQRLYAR-----LQVERVVNLYG 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  838 LAEncvfvSCAYGKKKPILVDWQGRICCGYVDPND-ADVdirivdADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd12115    248 PSE-----DTTYSTVAPVPPGASGEVSIGRPLANTqAYV------LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTA 316
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728  917 KTFRNKlQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:cd12115    317 ERFLPD-PFGPGARLYRTGDLVrWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRS 373
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
671-970 7.64e-08

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: 57.44  E-value: 7.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  671 SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILfSPL 750
Cdd:cd17644    103 TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVL-RPE 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAKArnydLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQE 830
Cdd:cd17644    181 EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDL----PSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLIN 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  831 VmapgYGLAENCVFVSCAYGKKkpILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWG 910
Cdd:cd17644    257 V----YGPTEATIAATVCRLTQ--LTERNITSVPIGRPIAN---TQVYILDEN--LQPVPVGVPGELHIGGVGLARGYLN 325
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728  911 KEELSQKTF-RNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:cd17644    326 RPELTAEKFiSHPFNSSESERLYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
833-1005 8.35e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 57.31  E-value: 8.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  833 APGYGLAENCVFVSCAygkkKPilvD--WQGRICCGYVDPNdADVDIRivdadtglevdeDGKEGEIWISSPSAGIGYWG 910
Cdd:PRK07445   258 APTYGMTETASQIATL----KP---DdfLAGNNSSGQVLPH-AQITIP------------ANQTGNITIQAQSLALGYYP 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  911 KEELSQKTFRnklqnypgrkytrTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEkTVESSSELLRPGCcaVIGVP 989
Cdd:PRK07445   318 QILDSQGIFE-------------TDDLGyLDAQGYLHILGRNSQKIITGGENVYPAEVE-AAILATGLVQDVC--VLGLP 381
                          170       180
                   ....*....|....*....|
gi 1917948728  990 E----EVLSAkgISLPDASD 1005
Cdd:PRK07445   382 DphwgEVVTA--IYVPKDPS 399
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1605-1686 8.84e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 53.34  E-value: 8.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRAINPIADPRMVSIGAGVHLGDFSRIITGFY-----SQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDV 1679
Cdd:COG0110     27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGA 106

                   ....*..
gi 1917948728 1680 ILGAISV 1686
Cdd:COG0110    107 VVGAGSV 113
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1118-1194 1.08e-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: 51.01  E-value: 1.08e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 1118 SNRNIVEFLKQLISEQTGISIQNISATESLVS-YGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLL 1194
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PRK07208 PRK07208
hypothetical protein; Provisional
26-75 1.42e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 56.44  E-value: 1.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEIEGKVYDLGG 75
Cdd:PRK07208     9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
678-1081 1.67e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 56.67  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  678 FLQFTSGSTSDAKGVMITHGGlihNVKLMRRRYRSTSNTVLVSWLPQYHDMGLI---GGLFTAMACGGSAILFSPlTFIR 754
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSLSLGNTFVMFEG-GIIK 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  755 NPLM----WlQTISDYKATHSagpnFAFELVIRRL-----EADKAKArNYDLSSMIFFMIAAEPVRQkTLKRFVELTRPF 825
Cdd:PTZ00237   334 NKHIeddlW-NTIEKHKVTHT----LTLPKTIRYLiktdpEATIIRS-KYDLSNLKEIWCGGEVIEE-SIPEYIENKLKI 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  826 GLSQevmapGYGLAE-NCVFVSCAYGKKKPILVdwqgricCG----YVDPndadvdirivdadtgLEVDEDGKE------ 894
Cdd:PTZ00237   407 KSSR-----GYGQTEiGITYLYCYGHINIPYNA-------TGvpsiFIKP---------------SILSEDGKElnvnei 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  895 GEIWIS---SPSAGIGYWGKEELSQKTFrNKlqnYPGrkYTRTGDLGWVIQGNLF-ITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PTZ00237   460 GEVAFKlpmPPSFATTFYKNDEKFKQLF-SK---FPG--YYNSGDLGFKDENGYYtIVSRSDDQIKISGNKVQLNTIETS 533
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  971 VESSSELLRpgCCAVigvpeevlsakGISLPD-ASDEVGLVVIAELRDS------KLVNK--DIIKQ-IESrvaeehgVT 1040
Cdd:PTZ00237   534 ILKHPLVLE--CCSI-----------GIYDPDcYNVPIGLLVLKQDQSNqsidlnKLKNEinNIITQdIES-------LA 593
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1917948728 1041 VASVKLIRPRtISKTTSGKIKRfECLKQFVDGNLNTVPDPI 1081
Cdd:PTZ00237   594 VLRKIIIVNQ-LPKTKTGKIPR-QIISKFLNDSNYQLPDNV 632
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
521-1020 2.03e-07

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 56.32  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  521 VGCQRTYAELDSNASCVAHKLltSRKpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPdplqrggqalTK 597
Cdd:PRK07786    39 LGNTTTWRELDDRVAALAGAL--SRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVnfrLTP----------PE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  598 IENIAKLCNAVAIL---STVGYHAAVRAglvknlISFTGKSVKSTGQWPNlpwlhtDSWIKSSKVLPASNIAFQSESQPD 674
Cdd:PRK07786   106 IAFLVSDCGAHVVVteaALAPVATAVRD------IVPLLSTVVVAGGSSD------DSVLGYEDLLAEAGPAHAPVDIPN 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DL-CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFSPLTF 752
Cdd:PRK07786   174 DSpALIMYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGI-GSMLPGLLLGAPTVIYPLGAF 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  753 irNPLMWLQTISDYKATHsagpnfAFeLVIRRLEA--DKAKARNYDLSsMIFFMIAAEPVRQKTLKRFVElTRP------ 824
Cdd:PRK07786   253 --DPGQLLDVLEAEKVTG------IF-LVPAQWQAvcAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAA-TFPeaqila 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  825 -FGlsQEVMAPgyglaencvfVSCAYGKKKPIlvdwQGRICCGYVDPNdadVDIRIVDADTGlEVDEdGKEGEIWISSPS 903
Cdd:PRK07786   322 aFG--QTEMSP----------VTCMLLGEDAI----RKLGSVGKVIPT---VAARVVDENMN-DVPV-GEVGEIVYRAPT 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  904 AGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRp 980
Cdd:PRK07786   381 LMSGYWNNPEATAEAFAGG--------WFHSGDL--VRQdeeGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVE- 449
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1917948728  981 gcCAVIGVPE----EVLSAKgISLPDASDEVGLVVIAELRDSKL 1020
Cdd:PRK07786   450 --VAVIGRADekwgEVPVAV-AAVRNDDAALTLEDLAEFLTDRL 490
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
23-59 2.15e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 55.96  E-value: 2.15e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK11749   142 KVAVIGAGPAGLTAAHRLARKGY-DVTIFEARDKAGG 177
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1341-1432 2.92e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 51.80  E-value: 2.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHWfemlGARIGSSVLLDT-VDITDPSLVSIGDGAVIAEGALL--QSHEVRN---SILRLQPIRIGRNCSV 1414
Cdd:COG0110     15 VVIGPGVRIYGG----NITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWI 90
                           90
                   ....*....|....*...
gi 1917948728 1415 GPYAVVQKGSVLREGAEV 1432
Cdd:COG0110     91 GAGATILPGVTIGDGAVV 108
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
21-74 4.29e-07

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 55.24  E-value: 4.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLG 74
Cdd:COG1233      3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTFERPGFRFDVG 55
PRK12316 PRK12316
peptide synthase; Provisional
526-968 4.98e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 55.73  E-value: 4.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKiENIAKLC 605
Cdd:PRK12316   538 DYAELNRRANRLAHAL---IERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLED-SGVQLLL 613
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  606 NAVAILSTVgyhaAVRAGLvkNLISFTGKSVKSTGQWPNLPWLHTDswiksskvlpasniafqsesqPDDLCFLQFTSGS 685
Cdd:PRK12316   614 SQSHLGRKL----PLAAGV--QVLDLDRPAAWLEGYSEENPGTELN---------------------PENLAYVIYTSGS 666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  686 TSDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSwLPQYHDMGlIGGLFTAMACGGSAILFSPlTFIRNPLMWLQTIs 764
Cdd:PRK12316   667 TGKPKGAGNRHRALSNRLCWMQQAYgLGVGDTVLQK-TPFSFDVS-VWEFFWPLMSGARLVVAAP-GDHRDPAKLVELI- 742
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  765 dykATHSAGpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAENCVF 844
Cdd:PRK12316   743 ---NREGVD---TLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAK-----LPQAGLYNLYGPTEAAID 811
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  845 VSC-----AYGKKKPIlvdwqGRICcgyvdpndADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTF 919
Cdd:PRK12316   812 VTHwtcveEGGDSVPI-----GRPI--------ANLACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1917948728  920 RNKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12316   877 VPSPFVAGERMY-RTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIE 925
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
526-769 1.25e-06

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 54.28  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAKl 604
Cdd:PRK10252   485 SYREMREQVVALANLL---RERGVKPGDSVA-VALPrSVFLTLALHAIVEAGAAWLPLDTGYPDDR----LKMMLEDAR- 555
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  605 cnAVAILSTvgyhAAVRAglvknliSFTGKsvkstgqwPNLPWLHTDSWiksskvLPASNIAFQSESQPDDLCFLQFTSG 684
Cdd:PRK10252   556 --PSLLITT----ADQLP-------RFADV--------PDLTSLCYNAP------LAPQGAAPLQLSQPHHTAYIIFTSG 608
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTIS 764
Cdd:PRK10252   609 STGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFIAGAKLVMAEPEAH-RDPLAMQQFFA 686

                   ....*
gi 1917948728  765 DYKAT 769
Cdd:PRK10252   687 EYGVT 691
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
1605-1702 1.29e-06

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: 50.10  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRA-INPIadprmvSIGAGVHLGDFSrIITGFYSQSGYIQGNV-----------DIKDNSVTGSQSLILPG 1672
Cdd:cd04645     23 GSSVWFGAVLRGdVNPI------RIGERTNIQDGS-VLHVDPGYPTIIGDNVtvghgavlhgcTIGDNCLIGMGAIILDG 95
                           90       100       110
                   ....*....|....*....|....*....|
gi 1917948728 1673 SVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:cd04645     96 AVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
681-991 1.55e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 53.46  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  681 FTSGSTSDAKGV----MITHGGLIHNVKLMRRRYRSTSNTVLVswLPQYHDMGLiGGLFTAMACGGSAILFSPLtfirnp 756
Cdd:PRK13383   181 LTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGSRISVA--MPMFHGLGL-GMLMLTIALGGTVLTHRHF------ 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  757 lmwlqtisDYKAT------HSAGPNFAFELVIRRLE--ADKAKARNyDLSSMIFFMIAAEPVRQKTLKRFVEltrPFGls 828
Cdd:PRK13383   252 --------DAEAAlaqaslHRADAFTAVPVVLARILelPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMD---TYG-- 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  829 qEVMAPGYGLAEncvfVSCAYGKKKPILVDWQ---GRICCGyvdpndadVDIRIVDAD---TGLEVdedgkEGEIWISSP 902
Cdd:PRK13383   318 -DILYNGYGSTE----VGIGALATPADLRDAPetvGKPVAG--------CPVRILDRNnrpVGPRV-----TGRIFVGGE 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  903 SAGIGYWGKeelSQKTFRNKLqnypgrkyTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPg 981
Cdd:PRK13383   380 LAGTRYTDG---GGKAVVDGM--------TSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN- 447
                          330
                   ....*....|
gi 1917948728  982 ccAVIGVPEE 991
Cdd:PRK13383   448 --AVIGVPDE 455
PRK12316 PRK12316
peptide synthase; Provisional
429-1003 2.58e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 53.42  E-value: 2.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  429 FAFELTERNSSYAMALICKHFASANSLPTFPYVKSLFTLQLDQEETGLKTLSETSGvvfpNLPTLDCYLKHWAAQEITQN 508
Cdd:PRK12316  2996 YATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAA----EYPLERGVHRLFEEQVERTP 3071
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  509 KALYTWINEGgavgcQRTYAELDSNASCVAHKLltsRKPTIKPgDRVLLVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDP 587
Cdd:PRK12316  3072 DAVALAFGEQ-----RLSYAELNRRANRLAHRL---IERGVGP-DVLVGVAVErSLEMVVGLLAILKAGGAYVPLDPEYP 3142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  588 LQRGGQALTKieniaklcNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLpwlhtdswiksskvlpasniaf 667
Cdd:PRK12316  3143 EERLAYMLED--------SGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIR---------------------- 3192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  668 qseSQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAILf 747
Cdd:PRK12316  3193 ---TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVL- 3267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 spltfiRNPLMWLQTISDYKATHSAGPNF--AFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPF 825
Cdd:PRK12316  3268 ------AGPEDWRDPALLVELINSEGVDVlhAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLY 3341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  826 GLSQEVMAPgygLAENCVFVSCAYgkkKPIlvdwqgriccGYVDPNDAdvdirIVDADTGLEVDEDGKEGEIWISSPSAG 905
Cdd:PRK12316  3342 GPTEATITV---THWQCVEEGKDA---VPI----------GRPIANRA-----CYILDGSLEPVPVGALGELYLGGEGLA 3400
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  906 IGYWGKEELSQKTFRNKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCA 984
Cdd:PRK12316  3401 RGYHNRPGLTAERFVPDPFVPGERLY-RTGDLArYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA 3479
                          570       580
                   ....*....|....*....|..
gi 1917948728  985 VIG---VPEEVLSAKGISLPDA 1003
Cdd:PRK12316  3480 VDGrqlVAYVVPEDEAGDLREA 3501
PLN02736 PLN02736
long-chain acyl-CoA synthetase
487-995 2.78e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 52.79  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  487 FPNLPTLDCYLKHwAAQEITQNKALYTWINEGGAVGCQR--TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLD 564
Cdd:PLN02736    40 HPEIGTLHDNFVY-AVETFRDYKYLGTRIRVDGTVGEYKwmTYGEAGTARTAIGSGLVQH---GIPKGACVGLYFINRPE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  565 FIDAFFGCLRAKVIPIPV---LPPDplqrggqALTKIENIAKL----CNAV---AILSTVGYHAAVRaglvknLISFTGK 634
Cdd:PLN02736   116 WLIVDHACSAYSYVSVPLydtLGPD-------AVKFIVNHAEVaaifCVPQtlnTLLSCLSEIPSVR------LIVVVGG 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  635 SvksTGQWPNLPWLHTDSWIKSSKVLPASNIAFQS--ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS 712
Cdd:PLN02736   183 A---DEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPfrPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  713 TSNTVLVSWLPQ---YHDMGLIGGLFtamacGGSAILF---------------SPLTFIRNPLMWlQTISD--YKATHSA 772
Cdd:PLN02736   260 YPSDVHISYLPLahiYERVNQIVMLH-----YGVAVGFyqgdnlklmddlaalRPTIFCSVPRLY-NRIYDgiTNAVKES 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  773 GP------NFAFELVIRRLEADKAKARNYDlsSMIFFMIAAepvRQKTLKRFVeLTRPFGLSQEVM-----------APG 835
Cdd:PLN02736   334 GGlkerlfNAAYNAKKQALENGKNPSPMWD--RLVFNKIKA---KLGGRVRFM-SSGASPLSPDVMeflricfggrvLEG 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  836 YGLAE-NCVFVSCAygkkkpilvdwQGRICCGYVDPNDADVDIRIVDADTGLEVDEDG--KEGEIWISSPSAGIGYWGKE 912
Cdd:PLN02736   408 YGMTEtSCVISGMD-----------EGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpyPRGEICVRGPIIFKGYYKDE 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  913 ELSQKTFRNKlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---------SELLRPG 981
Cdd:PLN02736   477 VQTREVIDED-------GWLHTGDIGlWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCkfvaqcfvyGDSLNSS 549
                          570
                   ....*....|....
gi 1917948728  982 CCAVIGVPEEVLSA 995
Cdd:PLN02736   550 LVAVVVVDPEVLKA 563
PRK05691 PRK05691
peptide synthase; Validated
497-968 5.02e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 52.48  E-value: 5.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  497 LKHWAAQEiTQNKALyTWinEGGAVGcqrtYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:PRK05691  1137 LNEQARQT-PERIAL-VW--DGGSLD----YAELHAQANRLAHYL---RDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  577 VIPIPVLPPDPLQRGGQALTKieniaklCNAVAILStvgyhaavRAGLVKNLISFTGKSVKSTGQwpnlpwLHTDSWIKS 656
Cdd:PRK05691  1206 GAYVPLDPDYPAERLAYMLAD-------SGVELLLT--------QSHLLERLPQAEGVSAIALDS------LHLDSWPSQ 1264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  657 SKVLPASNiafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFT 736
Cdd:PRK05691  1265 APGLHLHG---------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVS-VWECFW 1334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  737 AMACGGSAILFSPLTFiRNPLMWLQTISDYKAT--HSAGPnfafelvIRRLEADKAKARNYDLSSMIFFMIAAEP--VRQ 812
Cdd:PRK05691  1335 PLITGCRLVLAGPGEH-RDPQRIAELVQQYGVTtlHFVPP-------LLQLFIDEPLAAACTSLRRLFSGGEALPaeLRN 1406
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  813 KTLKRfveltrpfgLSQEVMAPGYGLAENCVFVS---C--AYGKKKPIlvdwqGR----ICCgyvdpndadvdiRIVDAD 883
Cdd:PRK05691  1407 RVLQR---------LPQVQLHNRYGPTETAINVThwqCqaEDGERSPI-----GRplgnVLC------------RVLDAE 1460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  884 tgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNI 962
Cdd:PRK05691  1461 --LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRArWNADGALEYLGRLDQQVKLRGFRV 1538

                   ....*.
gi 1917948728  963 YSADVE 968
Cdd:PRK05691  1539 EPEEIQ 1544
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
491-729 5.08e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 51.97  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  491 PTLDCYLKHWAAQEITQnkalyTWINEGGAVGCQ---RTYAELDSNASCVAHKLLTSRKPtikPGDRVLLVHVPGLDFID 567
Cdd:PRK12582    49 RSIPHLLAKWAAEAPDR-----PWLAQREPGHGQwrkVTYGEAKRAVDALAQALLDLGLD---PGRPVMILSGNSIEHAL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  568 AFFGCLRAKVIPIPVLPPDPLQRGGQAltKIENIAKLCNAVAILSTVG--YHAAVRAglvknlISFTGKSVKS-TGQWPN 644
Cdd:PRK12582   121 MTLAAMQAGVPAAPVSPAYSLMSHDHA--KLKHLFDLVKPRVVFAQSGapFARALAA------LDLLDVTVVHvTGPGEG 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  645 LPWLHTDSWIkSSKVLPASNIAFQSESqPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM---RRRYRSTSNTVLVSW 721
Cdd:PRK12582   193 IASIAFADLA-ATPPTAAVAAAIAAIT-PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQeqlRPREPDPPPPVSLDW 270

                   ....*...
gi 1917948728  722 LPQYHDMG 729
Cdd:PRK12582   271 MPWNHTMG 278
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
22-96 5.91e-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: 51.38  E-value: 5.91e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYR---DITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLGLE 79
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
21-103 7.45e-06

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: 50.32  E-value: 7.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGG-------MCESVEIegkVYDLG-GQVLAANSAPV---IFHL 89
Cdd:COG0654      3 RTDVLIVGGGPAGLALALALARAGIR-VTVVERAPPPRPdgrgialSPRSLEL---LRRLGlWDRLLARGAPIrgiRVRD 78
                           90
                   ....*....|....
gi 1917948728   90 AkESGTELEEMDLH 103
Cdd:COG0654     79 G-SDGRVLARFDAA 91
PRK13984 PRK13984
putative oxidoreductase; Provisional
16-60 1.15e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 50.54  E-value: 1.15e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1917948728   16 PCLPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK13984   278 EPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGV 321
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1087-1187 1.61e-05

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 49.36  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1087 LTRSFTTGTCREGKTPRSHLAKSSLAPSPKLSNRNIVEFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSD 1166
Cdd:COG3433    185 LLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRK 264
                           90       100
                   ....*....|....*....|.
gi 1917948728 1167 fLGVPVGAVDIFTATCIADLA 1187
Cdd:COG3433    265 -AGLDVSFADLAEHPTLAAWW 284
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
673-751 1.70e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 50.12  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVK-LMRRRYRSTSNTVLVSWLPQYHDMGLIGGlfTAMACGGSAILF-SPL 750
Cdd:PLN02387   249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgVMTVVPKLGKNDVYLAYLPLAHILELAAE--SVMAAVGAAIGYgSPL 326

                   .
gi 1917948728  751 T 751
Cdd:PLN02387   327 T 327
PRK08162 PRK08162
acyl-CoA synthetase; Validated
679-1064 1.82e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 49.95  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  679 LQFTSGSTSDAKGVMITHGGLIHNvklmrrryrSTSNTVlvSW-----------LPQYHdmgLIGGLF--TAMACGGSAI 745
Cdd:PRK08162   187 LNYTSGTTGNPKGVVYHHRGAYLN---------ALSNIL--AWgmpkhpvylwtLPMFH---CNGWCFpwTVAARAGTNV 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  746 lfspltFIR--NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAKarnydLSSMIFFMIAAEP----VRQKTLKRFV 819
Cdd:PRK08162   253 ------CLRkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG-----IDHPVHAMVAGAAppaaVIAKMEEIGF 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  820 ELTRPFGLSqEVmapgYGLAencvfVSCAygkKKPilvDW-----------QGRICCGYVdpndADVDIRIVDADTGLEV 888
Cdd:PRK08162   322 DLTHVYGLT-ET----YGPA-----TVCA---WQP---EWdalplderaqlKARQGVRYP----LQEGVTVLDPDTMQPV 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  889 DEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:PRK08162   382 PADGETiGEIMFRGNIVMKGYLKNPKATEEAFAGG--------WFHTGDLAvLHPDGYIKIKDRSKDIIISGGENISSIE 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  967 VEKTvessseLLR-PGccavigvpeeVLSAKGISLPDAS-DEVGLVVIaELRDSKLVNK-DIIKQIESRVAeehGVTVAs 1043
Cdd:PRK08162   454 VEDV------LYRhPA----------VLVAAVVAKPDPKwGEVPCAFV-ELKDGASATEeEIIAHCREHLA---GFKVP- 512
                          410       420
                   ....*....|....*....|.
gi 1917948728 1044 vKLIRPRTISKTTSGKIKRFE 1064
Cdd:PRK08162   513 -KAVVFGELPKTSTGKIQKFV 532
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
853-1061 2.25e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 49.62  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  853 KPILVDWQGRICCGYVDPNDADvDIRIVDADTGLE---------------VDEDGKEgeiwisSPSAGIG--YWGKEELS 915
Cdd:PRK13390   287 KHAMIDWLGPIVYEYYSSTEAH-GMTFIDSPDWLAhpgsvgrsvlgdlhiCDDDGNE------LPAGRIGtvYFERDRLP 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  916 -------QKTFRNKLQNYPgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVEssselLRPGC--CAV 985
Cdd:PRK13390   360 frylndpEKTAAAQHPAHP--FWTTVGDLGSVDEdGYLYLADRKSFMIISGGVNIYPQETENALT-----MHPAVhdVAV 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  986 IGVPEevlsakgislPDASDEVGLVV--IAELRDSKLVNKDIIKQIESRVAeeHGVTVASVKLIR--PRT-ISKTTSGKI 1060
Cdd:PRK13390   433 IGVPD----------PEMGEQVKAVIqlVEGIRGSDELARELIDYTRSRIA--HYKAPRSVEFVDelPRTpTGKLVKGLL 500

                   .
gi 1917948728 1061 K 1061
Cdd:PRK13390   501 R 501
PLN03000 PLN03000
amine oxidase
5-97 2.57e-05

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 49.63  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728    5 KSVEDQFsklhPCLPLDTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIE----GKVYDLGGQVLAA 80
Cdd:PLN03000   172 QAIKDKF----PAQSSKSSVVIVGAGLSGLAAARQLMRFGFK-VTVLEGRKRPGGRVYTKKMEanrvGAAADLGGSVLTG 246
                           90
                   ....*....|....*..
gi 1917948728   81 NSAPVIFHLAKESGTEL 97
Cdd:PLN03000   247 TLGNPLGIIARQLGSSL 263
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
22-96 2.74e-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: 49.08  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEgkvyDLG-----GQ--VLAANSApvIFHLAKESG 94
Cdd:COG3349      4 PRVVVVGGGLAGLAAAVELAEAGFR-VTLLEARPRLGGRARSFPDP----DTGlpidnGQhvLLGCYRN--TLDLLRRIG 76

                   ..
gi 1917948728   95 TE 96
Cdd:COG3349     77 AA 78
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
21-59 3.23e-05

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: 48.71  E-value: 3.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVMEKHKSVGG 59
Cdd:COG2072      6 HVDVVVIGAGQAGLAAAYHLRRAG-IDFVVLEKADDVGG 43
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
674-954 3.35e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 49.20  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS-----TSNTVLVSWLPQYHDMGLigGLFTAMACGGSAILF- 747
Cdd:PTZ00216   264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligppEEDETYCSYLPLAHIMEF--GVTNIFLARGALIGFg 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  748 SPLT----FIR--------NPLMWL------QTISdyKATHSAGP----------NFAFELVIRRLEADK---------- 789
Cdd:PTZ00216   342 SPRTltdtFARphgdltefRPVFLIgvprifDTIK--KAVEAKLPpvgslkrrvfDHAYQSRLRALKEGKdtpywnekvf 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  790 AKARNYDLSSMIFFMIAAEPVRQKTlKRFVELTrpFGLsqevMAPGYGLAENCvfvsCAYGKKKPilvdwqGRICCGYVD 869
Cdd:PTZ00216   420 SAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNVV--FGM----VIQGWGLTETV----CCGGIQRT------GDLEPNAVG 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  870 PNDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFIT 948
Cdd:PTZ00216   483 QLLKGVEMKLLDTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDED-------GWFHTGDVGSIaANGTLRII 555

                   ....*.
gi 1917948728  949 GRIKDL 954
Cdd:PTZ00216   556 GRVKAL 561
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
23-110 3.44e-05

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 48.69  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYR-DITVMEKHKSVGGMCESVEIEGKVYDLGgqvlaansaPVIFHLAKESGTELeemd 101
Cdd:PRK11883     2 KVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFPIELG---------PESFLARKPSAPAL---- 68

                   ....*....
gi 1917948728  102 LHKLALIDS 110
Cdd:PRK11883    69 VKELGLEDE 77
PLN02576 PLN02576
protoporphyrinogen oxidase
21-94 3.57e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 48.86  E-value: 3.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGYRDITVMEKHKSVGGMCESVEIEGKVYDLGgqvlaANS---APVIFHLAKESG 94
Cdd:PLN02576    12 SKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEG-----PNSfqpSDPELTSAVDSG 83
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
1352-1434 4.18e-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: 44.52  E-value: 4.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1352 WFEMLGAR--IGSSVLLDTVDitdpsLVSIGDGAVIAEGALL--QSHEVRNSILRL--QPIRIGRNCSVGPYAVVQKGSV 1425
Cdd:cd05825      2 WNLTIGDNswIGEGVWIYNLA-----PVTIGSDACISQGAYLctGSHDYRSPAFPLitAPIVIGDGAWVAAEAFVGPGVT 76

                   ....*....
gi 1917948728 1426 LREGAEVPA 1434
Cdd:cd05825     77 IGEGAVVGA 85
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1354-1432 4.69e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.57  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1354 EMLGARIGSSVLLDTVDITDPSLVSIGDGAV------------------IAEGALLQSH-EVRNSIL----------RLQ 1404
Cdd:PRK14356   241 ELLRARIVEKHLESGVLIHAPESVRIGPRATiepgaeiygpceiygasrIARGAVIHSHcWLRDAVVssgatihsfsHLE 320
                           90       100
                   ....*....|....*....|....*...
gi 1917948728 1405 PIRIGRNCSVGPYAVVQKGSVLREGAEV 1432
Cdd:PRK14356   321 GAEVGDGCSVGPYARLRPGAVLEEGARV 348
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
661-770 5.32e-05

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 48.33  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITH----------GGLIhnvklmrrryRSTSNTVLVSWLPQYHDMGL 730
Cdd:PRK08279   186 PTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLL----------RLTPDDVLYCCLPLYHNTGG 255
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1917948728  731 IGGLFTAMACGGSAIL---FSPLTFirnplmWLQtISDYKATH 770
Cdd:PRK08279   256 TVAWSSVLAAGATLALrrkFSASRF------WDD-VRRYRATA 291
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
23-60 6.40e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 48.19  E-value: 6.40e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK12814   195 KVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGM 231
PRK07638 PRK07638
acyl-CoA synthetase; Validated
874-1068 7.43e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 47.85  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  874 DVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTfrnklqnyPGRKYTRTGDLGWVIQ-GNLFITGRIK 952
Cdd:PRK07638   315 NVQVRICNEA-GEEV-QKGEIGTVYVKSPQFFMGYIIGGVLAREL--------NADGWMTVRDVGYEDEeGFIYIVGREK 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  953 DLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLSAKGISLPDASDEVglvviaelrdsklvnkdiiKQIESR 1032
Cdd:PRK07638   385 NMILFGGINIFPEEIESVLHEHPAVDE---IVVIGVPDSYWGEKPVAIIKGSATK-------------------QQLKSF 442
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1917948728 1033 VAEEhgvtVASVKliRPR------TISKTTSGKIKRFECLKQ 1068
Cdd:PRK07638   443 CLQR----LSSFK--IPKewhfvdEIPYTNSGKIARMEAKSW 478
PRK12467 PRK12467
peptide synthase; Provisional
473-746 8.68e-05

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 48.23  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  473 ETGLKTLSETSGVVFPNLPTLDCYLKHWAAQEITQNKALYT-------WIN-------EGGAVGC---QRTYAELDSNAS 535
Cdd:PRK12467  3052 DRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPserlvhqLIEaqvartpEAPALVFgdqQLSYAELNRRAN 3131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  536 CVAHKLLTsrkptIKPGDRVLL-VHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiaklcNAVAILST 613
Cdd:PRK12467  3132 RLAHRLIA-----IGVGPDVLVgVAVErSVEMIVALLAVLKAGGAYVPLDPEYPRER---LAYMIED-----SGVKLLLT 3198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  614 VGyHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDswiksskvlpasniafqsesqPDDLCFLQFTSGSTSDAKGVM 693
Cdd:PRK12467  3199 QA-HLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVM---------------------GENLAYVIYTSGSTGKPKGVG 3256
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1917948728  694 ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAIL 746
Cdd:PRK12467  3257 VRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLVV 3308
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
672-840 9.08e-05

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 48.04  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILF-SPL 750
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYpSPL 870
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  751 TFIRNPLMwlqtISDYKATHSAGPNFaFelvirrLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEltrPFGLSqe 830
Cdd:PRK06814   871 HYRIIPEL----IYDTNATILFGTDT-F------LNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWME---KFGIR-- 934
                          170
                   ....*....|
gi 1917948728  831 vMAPGYGLAE 840
Cdd:PRK06814   935 -ILEGYGVTE 943
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
1607-1686 1.48e-04

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: 43.21  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1607 KVGRYCSIRAINPIADPRMVSIGAGVHLGDFSRIITGFYS--------QSGYIQGNVDIKDNSVTGSQSLILPGSVVEKD 1678
Cdd:cd04647      3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                   ....*...
gi 1917948728 1679 VILGAISV 1686
Cdd:cd04647     83 AVVGAGSV 90
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1341-1432 1.71e-04

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: 46.56  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIaegalLQSHeVRNSIlrlqpirIGRNCSVGPYAV 1419
Cdd:COG1207    279 VILEGKTVIGE-----GVVIGPnCTLKDST---------IGDGVVI-----KYSV-IEDAV-------VGAGATVGPFAR 331
                           90
                   ....*....|...
gi 1917948728 1420 VQKGSVLREGAEV 1432
Cdd:COG1207    332 LRPGTVLGEGVKI 344
PRK06753 PRK06753
hypothetical protein; Provisional
23-178 2.12e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 46.22  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKH---KSVG---GMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKESGTE 96
Cdd:PRK06753     2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNesvKEVGagiGIGDNVIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   97 LEEM---------DLHKLALIDSFTGEYHDinvaedymSLVSLTLEIQDKAKDSNHIGIHaVSDIASDLTPAYLEAHGIK 167
Cdd:PRK06753    81 LNKVklksntlnvTLHRQTLIDIIKSYVKE--------DAIFTGKEVTKIENETDKVTIH-FADGESEAFDLCIGADGIH 151
                          170
                   ....*....|....*....
gi 1917948728  168 SV------PKS-VQY-GYT 178
Cdd:PRK06753   152 SKvrqsvnADSkVRYqGYT 170
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
18-60 2.20e-04

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.39  E-value: 2.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1917948728   18 LPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:COG1148    137 VPVNKRALVIGGGIAGMTAALELAEQGY-EVYLVEKEPELGGR 178
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
23-264 2.22e-04

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 46.26  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKlgYRDITVMEKHKSVGGMCESVEIegkvyDLGGQVLAANSA---------PVIFHLAKES 93
Cdd:COG2907      5 RIAVIGSGISGLTAAWLLSR--RHDVTLFEANDRLGGHTHTVDV-----DLDGRTVPVDTGfivfnertyPNLTALFAEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728   94 GTELEEMDLhklalidSF------TG-EY--HDINvaedymslvslTLEIQdkakDSN-----HIGI---------HAVS 150
Cdd:COG2907     78 GVPTQPSDM-------SFsvsldgGGlEYagSNLN-----------GLFAQ----RRNllrprFWRMlrdilrfnrEAPA 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  151 DIASDLTP-----AYLEAHGIksvPKSVQYGY-----TA---SGYGFVQDMPYAYIHEFTRT----SMAGKI--RRMKGG 211
Cdd:COG2907    136 LLEAGSDDdltlgEFLDRNGY---SEAFRDHYllpmgAAiwsCPPDDMLDFPARFFVRFFHNhgllSVTDRPqwRTVKGG 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728  212 ---YMslwKKISKSLLIKVCCNTEVQAVRRDGSdvNVDITNSSGETEHkeFDKIII 264
Cdd:COG2907    213 sreYV---RRLTAGLKDRIRLNTPVRSVRRDAD--GVEVRTADGEEER--FDHVVF 261
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
21-60 2.57e-04

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 46.10  E-value: 2.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGYR--DITVMEKHKSVG-GM 60
Cdd:COG4529      5 RKRIAIIGGGASGTALAIHLLRRAPEplRITLFEPRPELGrGV 47
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
2103-2302 3.00e-04

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: 46.28  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2103 LQTIVPYFLLGLIIY---FPLNLLLHCknarnMPVhwtfpFFWVSTGILAalTCAAAKYILVGKKKEdETVHIWsrGVFM 2179
Cdd:TIGR02353   16 LQWLAPLLGYNWLYEaldDVSWLYLRA-----VAL-----VFAVPVGRLG--FAIAAKWLLVGRWKP-GTYPIW--GSTY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2180 DTIWQAIRTV--FGDYFVemtSGSALFLMWMKLMGssVELDKGTYVDSMGAALNpEMVEVEGGGSVEREALLFGhvYDGE 2257
Cdd:TIGR02353   81 LRFWTVKRLVdaAPTVLL---SGSPLYSLYLRALG--AKIGKGVDIGSLPPVCT-DLLTIGAGTIVRKEVMLLG--YRAE 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1917948728 2258 GGAVKFGKIVVGEGGFVGSRAVAMPG--VESGGSLSALSLAMKGEAI 2302
Cdd:TIGR02353  153 RGRLHTGPVTLGRDAFIGTRSTLDIDtsIGDGAQLGHGSALQGGQSI 199
gltD PRK12810
glutamate synthase subunit beta; Reviewed
23-59 3.65e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 45.54  E-value: 3.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK12810   145 KVAVVGSGPAGLAAADQLARAGH-KVTVFERADRIGG 180
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
526-744 4.69e-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: 45.52  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  526 TYAELDSNASCVAHKLLTSRkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIE------ 599
Cdd:cd17632     69 TYAELWERVGAVAAAHDPEQ--PVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprllav 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  600 NIAKLCNAVAILSTVG---------YHAAV---RAGLVKNLISFTGKSVKSTgqwpnlpwLHTDSWIKSSKVLPASniAF 667
Cdd:cd17632    147 SAEHLDLAVEAVLEGGtpprlvvfdHRPEVdahRAALESARERLAAVGIPVT--------TLTLIAVRGRDLPPAP--LF 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  668 QSESQPDDLCFLQFTSGSTSDAKGVMITHggliHNVKLMRRRYRST-----SNTVLVSWLPQYHDMGLIgGLFTAMACGG 742
Cdd:cd17632    217 RPEPDDDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIqdirpPASITLNFMPMSHIAGRI-SLYGTLARGG 291

                   ..
gi 1917948728  743 SA 744
Cdd:cd17632    292 TA 293
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
22-55 4.95e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 45.01  E-value: 4.95e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHK 55
Cdd:PRK12409     2 SHIAVIGAGITGVTTAYALAQRGYQ-VTVFDRHR 34
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
1371-1432 5.56e-04

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: 41.67  E-value: 5.56e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1371 ITDPSLVSIGDGAVIAEGALLQSH--------EVRNSILRLQPIRIGRNCSVGPYAVVQKGSVLREGAEV 1432
Cdd:cd04647     16 ISAGGGITIGDNVLIGPNVTIYDHnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1356-1420 5.73e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 42.17  E-value: 5.73e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 1356 LGARIGSSVLLDTVDITDPSLVSIGDGAVIAEGAllqshevrnSILRLQPIRIGRNCSVGPYAVV 1420
Cdd:COG0110      7 FGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGV---------TIDDPGGITIGDNVLIGPGVTI 62
PLN02654 PLN02654
acetate-CoA ligase
888-1082 5.74e-04

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 45.27  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  888 VDEDGKE--GE------IWISSPSAGIGYWGKEELSQKTFRNKLQNY--PGRKYTRTGDlgwviqGNLFITGRIKDLIIV 957
Cdd:PLN02654   468 VDEKGKEieGEcsgylcVKKSWPGAFRTLYGDHERYETTYFKPFAGYyfSGDGCSRDKD------GYYWLTGRVDDVINV 541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  958 AGRNIYSADVEktvesSSELLRPGC--CAVIGVPEEVlsaKGislpdasdeVGLVVIAELRDSKLVNKDIIKQIESRVAE 1035
Cdd:PLN02654   542 SGHRIGTAEVE-----SALVSHPQCaeAAVVGIEHEV---KG---------QGIYAFVTLVEGVPYSEELRKSLILTVRN 604
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 1036 EHGVTVASVKLIRPRTISKTTSGKIKRfECLKQFVD------GNLNTVPDPIV 1082
Cdd:PLN02654   605 QIGAFAAPDKIHWAPGLPKTRSGKIMR-RILRKIASrqldelGDTSTLADPGV 656
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
673-729 8.58e-04

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 44.48  E-value: 8.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728  673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYHDMG 729
Cdd:PRK08180   208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFG 266
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
23-59 1.10e-03

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: 43.54  E-value: 1.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:pfam01266    1 DVVVIGGGIVGLSTAYELARRGL-SVTLLERGDDPGS 36
PRK06185 PRK06185
FAD-dependent oxidoreductase;
20-55 1.26e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 43.69  E-value: 1.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1917948728   20 LDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHK 55
Cdd:PRK06185     5 ETTDCCIVGGGPAGMMLGLLLARAGV-DVTVLEKHA 39
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
879-1062 1.33e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 43.98  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  879 IVDaDTGLEVdEDGKEGEIWISSPSAGI--GYWGKEELSQKTFRNKlqnYPGRKYTrtGDlgWVIQ---GNLFITGRIKD 953
Cdd:PRK00174   437 VVD-EEGNPL-EGGEGGNLVIKDPWPGMmrTIYGDHERFVKTYFST---FKGMYFT--GD--GARRdedGYYWITGRVDD 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  954 LIIVAGRNIYSADVEKTV---ESSSEllrpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQIE 1030
Cdd:PRK00174   508 VLNVSGHRLGTAEIESALvahPKVAE------AAVVGRPDDI---KGQGI------YAFVT---LKGGEEPSDELRKELR 569
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1917948728 1031 SRVAEEHGvTVASVKLIR-----PrtisKTTSGKIKR 1062
Cdd:PRK00174   570 NWVRKEIG-PIAKPDVIQfapglP----KTRSGKIMR 601
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
24-59 1.59e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 42.46  E-value: 1.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1917948728   24 IGIVGGGPSGLSAAYALAKLGYRDITVMEKHKSVGG 59
Cdd:pfam01946   20 VVIVGAGSSGLTAAYYLAKNRGLKVAIIERSVSPGG 55
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
21-54 1.74e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 42.97  E-value: 1.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVMEKH 54
Cdd:COG0665      2 TADVVVIGGGIAGLSTAYHLARRG-LDVTVLERG 34
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
675-752 1.75e-03

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: 43.50  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728  675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLT 751
Cdd:cd05940     82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASN 161

                   .
gi 1917948728  752 F 752
Cdd:cd05940    162 F 162
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
23-60 2.16e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 42.67  E-value: 2.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK12770    20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGL 56
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
26-61 2.33e-03

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 42.84  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMC 61
Cdd:PRK05249    10 VIGSGPAGEGAAMQAAKLGKR-VAVIERYRNVGGGC 44
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
1341-1432 2.62e-03

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: 41.25  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIAEGallqSHeVRNSIlrlqpirIGRNCSVGPYAV 1419
Cdd:cd03353     28 VILEGKTVIGE-----DCVIGPnCVIKDST---------IGDGVVIKAS----SV-IEGAV-------IGNGATVGPFAH 81
                           90
                   ....*....|...
gi 1917948728 1420 VQKGSVLREGAEV 1432
Cdd:cd03353     82 LRPGTVLGEGVHI 94
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
1606-1698 3.35e-03

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: 41.24  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1606 AKVGRYCSIRAinpiadprMVSIGAGVHLGDFSRiitgfysqsgyIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAis 1685
Cdd:cd03352      2 AKIGENVSIGP--------NAVIGEGVVIGDGVV-----------IGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGD-- 60
                           90
                   ....*....|...
gi 1917948728 1686 vapvNSVLQSGGV 1698
Cdd:cd03352     61 ----RVIIHSGAV 69
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
23-59 4.11e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.42  E-value: 4.11e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK12778   433 KVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
26-58 4.24e-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: 41.54  E-value: 4.24e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1917948728   26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVG 58
Cdd:TIGR02032    5 VVGAGPAGASAAYRLADKGLR-VLLLEKKSFPR 36
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
29-58 4.83e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 41.49  E-value: 4.83e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1917948728   29 GGPSGLSAAYALAKLGYrDITVMEKHKSVG 58
Cdd:COG0644      1 AGPAGSAAARRLARAGL-SVLLLEKGSFPG 29
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
25-60 5.57e-03

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 39.57  E-value: 5.57e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1917948728   25 GIVGGGPSGLSAAYALAKLGYR---DITVMEKHKSVGGM 60
Cdd:pfam13454    1 AIVGGGPSGLALLERLLARAPKrplEITLFDPSPPGAGG 39
PRK08401 PRK08401
L-aspartate oxidase; Provisional
21-51 7.09e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 41.33  E-value: 7.09e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1917948728   21 DTRIGIVGGGPSGLSAAYALAKLGYrDITVM 51
Cdd:PRK08401     1 MMKVGIVGGGLAGLTAAISLAKKGF-DVTII 30
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
661-710 7.39e-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: 41.23  E-value: 7.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728  661 PASNIAFQSE--------SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRY 710
Cdd:cd17648     73 PDERIQFILEdtgarvviTNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY 130
PRK12831 PRK12831
putative oxidoreductase; Provisional
23-58 7.43e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.16  E-value: 7.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1917948728   23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEK-HKSVG 58
Cdd:PRK12831   142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEAlHEPGG 177
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
22-61 8.45e-03

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 41.00  E-value: 8.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1917948728   22 TRIGIVGGGPSGLSAAYALAKLGyRDITVMEKhKSVGGMC 61
Cdd:PRK07845     2 TRIVIIGGGPGGYEAALVAAQLG-ADVTVIER-DGLGGAA 39
 
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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