|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1-428 |
0e+00 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 668.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 1 MPRPELEALQTKRLKRMVERIYSLVPFYRRKLDAAGIKPQDILGMEDLLKLPFTRKSDLREQYPFRMFAVEQEEVARIHG 80
Cdd:COG1541 11 LSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEIVRIHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIVMAGGRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVPVSGGNRSRQVTL 160
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 161 IQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEViGPGVAMECr 240
Cdd:COG1541 171 MQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV-GPGVAYEC- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 241 EAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFTSLTKEALPILRYRTGDITALHREVCRCGRTHTRMSRIKGRIDD 320
Cdd:COG1541 249 EAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 321 MLIIRGVNVFPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSEAWFRSiessfgqgnervvQLCKRLQSVVKDT 400
Cdd:COG1541 329 MLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLE-------------ALAEAIAAALKAV 395
|
410 420
....*....|....*....|....*...
gi 1705143246 401 LYVTTKVILKEPKSLPRSEGKAVRVIDQ 428
Cdd:COG1541 396 LGLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| PA_CoA_ligase |
TIGR02155 |
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ... |
1-429 |
0e+00 |
|
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]
Pssm-ID: 131210 [Multi-domain] Cd Length: 422 Bit Score: 644.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 1 MPRPELEALQTKRLKRMVERIYSLVPFYRRKLDAAGIKPQDILGMEDLLKLPFTRKSDLREQYPFRMFAVEQEEVARIHG 80
Cdd:TIGR02155 3 ASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRIHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIVMAGGRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVPVSGGNRSRQVTL 160
Cdd:TIGR02155 83 SSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQVQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 161 IQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVIGPGVAMECR 240
Cdd:TIGR02155 163 IQDFKPDIIMVTPSYMLNLLEELKRMGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAMECV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 241 EAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFTSLTKEALPILRYRTGDITALHREvcrCGRTHTRMSRIKGRIDD 320
Cdd:TIGR02155 243 ETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPG---TARTMRRMDRITGRSDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 321 MLIIRGVNVFPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSEawfrsiESSFGQGNERVVQLCKRLQSVVKDT 400
Cdd:TIGR02155 320 MLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELKP------ESYTLRLHEQASLLAGEIQHTIKQE 393
|
410 420
....*....|....*....|....*....
gi 1705143246 401 LYVTTKVILKEPKSLPRSEGKAVRVIDQR 429
Cdd:TIGR02155 394 VGVSMDVHLVEPGSLPRSEGKARRVVDLR 422
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
1-429 |
0e+00 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 631.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 1 MPRPELEALQTKRLKRMVERIYSLVPFYRRKLDAAGIKPQDILGMEDLLKLPFTRKSDLREQYPFRMFAVEQEEVARIHG 80
Cdd:cd05913 6 MSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKVVRIHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIVMAGGRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVPVSGGNRSRQVTL 160
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 161 IQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVIGPGVAMECr 240
Cdd:cd05913 166 IKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFEC- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 241 EAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFTSLTKEALPILRYRTGDITALHREVCRCGRTHTRMSRIKGRIDD 320
Cdd:cd05913 245 EEKDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 321 MLIIRGVNVFPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSEAwfrsiessfGQGNERVVQLCKRLQSVVKDT 400
Cdd:cd05913 325 MLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPE---------ADDDEKLEALKQRLERHIKSV 395
|
410 420
....*....|....*....|....*....
gi 1705143246 401 LYVTTKVILKEPKSLPRSEGKAVRVIDQR 429
Cdd:cd05913 396 LGVTVEVELVEPGSLPRSEGKAKRVIDKR 424
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
74-339 |
2.01e-35 |
|
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: 133.56 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 74 EVARIHGSSGTSGKPTVVGYTRKDIQRWAELCARSIvmaGGRPGDVFHNAYGYGlFTGGLGLHYGAERLGATVVPVSGGN 153
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG---GLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 154 RSRQVTLIQDFLPRGIGGTPSFilsLAEMMEDMGLKPWTTS-LEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEViG 232
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTL---LARLLKAPESAGYDLSsLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTET-G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 233 PGVAMECREAKDGLH----IAEDHFLPEVIHPQTGEpLPDGEYGELVFTS------------LTKEALPILRYRTGDITA 296
Cdd:cd04433 153 GTVATGPPDDDARKPgsvgRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGpsvmkgywnnpeATAAVDEDGWYRTGDLGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1705143246 297 LHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd04433 232 LDED----GYLY-----IVGRLKDMIKSGGENVYPAEVEAVLL 265
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
326-429 |
3.39e-34 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 122.97 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 326 GVNVFPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSEAWFRSIessfgqgnERVVQLCKRLQSVVKDTLYVTT 405
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEI--------KDLEALEKRIAKELKSVLGVSV 72
|
90 100
....*....|....*....|....
gi 1705143246 406 KVILKEPKSLPRSEGKAVRVIDQR 429
Cdd:pfam14535 73 KVELVEPGTLPRSEGKAKRVIDLR 96
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
75-339 |
4.14e-24 |
|
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: 103.74 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 75 VARIHGSSGTSGKPTVVGYTRKDIQRWAELCARSIvmaGGRPGDVFHNA----YGYGLFTGGLGlhygAERLGATVVPVS 150
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAL---GLTPGDVVLVAlplfHVFGLTVGLLA----PLLAGATLVLLP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 151 GGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKpwTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEv 230
Cdd:COG0318 175 RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYD--LSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTE- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 231 IGPGVAMECREAKDGLHIAEDHFLPEV---IHPQTGEPLPDGEYGELVFTS------------LTKEALPILRYRTGDIT 295
Cdd:COG0318 252 TSPVVTVNPEDPGERRPGSVGRPLPGVevrIVDEDGRELPPGEVGEIVVRGpnvmkgywndpeATAEAFRDGWLRTGDLG 331
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1705143246 296 ALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:COG0318 332 RLDED----GYLY-----IVGRKKDMIISGGENVYPAEVEEVLA 366
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
73-339 |
9.17e-15 |
|
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: 75.72 E-value: 9.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 73 EEVARIHGSSGTSGKPTVVGYTRKDIQrWAelcARSIVMAGG-RPGDV-------FHNAyGYGLFTGGLGLHygaerlGA 144
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLL-WN---AVNALAALDlGPDDVllvvaplFHIG-GLGVFTLPTLLR------GG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 145 TVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFIlslaEMMEDMGLKPWT--TSLEYGIFGAEPWSEEMRQTLEEKwGIDAL 222
Cdd:cd17631 167 TVVILRKFDPETVLDLIERHRVTSFFLVPTMI----QALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQAR-GVKFV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 223 DIYGLSEvIGPGVAMecREAKDglHIAE------DHFLPEV-IHPQTGEPLPDGEYGELVFTS------------LTKEA 283
Cdd:cd17631 242 QGYGMTE-TSPGVTF--LSPED--HRRKlgsagrPVFFVEVrIVDPDGREVPPGEVGEIVVRGphvmagywnrpeATAAA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1705143246 284 LPILRYRTGDITALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd17631 317 FRDGWFHTGDLGRLDED----GYLY-----IVDRKKDMIISGGENVYPAEVEDVLY 363
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-325 |
8.02e-14 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 72.73 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKP-----------TVVGYTRKDIQRWAELCARSIVMAggrPGDVFHnAYGYGLFTgglglhYGAERLGATVVPV 149
Cdd:pfam00501 163 TSGTTGKPkgvmlthrnlvANVLSIKRVRPRGFGLGPDDRVLS---TLPLFH-DFGLSLGL------LGPLLAGATVVLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 150 SGGNR---SRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKpwTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYG 226
Cdd:pfam00501 233 PGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL--LSSLRLVLSGGAPLPPELARRFRELFGGALVNGYG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 227 LSEVIGP-----------------GVAMECREAKdglhiaedhflpeVIHPQTGEPLPDGEYGELVFTS----------- 278
Cdd:pfam00501 311 LTETTGVvttplpldedlrslgsvGRPLPGTEVK-------------IVDDETGEPVPPGEPGELCVRGpgvmkgylndp 377
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1705143246 279 -LTKEALPILR-YRTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIR 325
Cdd:pfam00501 378 eLTAEAFDEDGwYRTGDLGRRDED----GYL-----EIVGRKKDQIKLG 417
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
33-338 |
8.18e-12 |
|
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: 66.76 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 33 DAAGIKPQDILGMEDLLKLpfTRKSDLREQY----PFRMFAVEQEEVARIHGSSGTSGKPTVVGYTrkdiQRWAElcARS 108
Cdd:cd05923 108 VDAQVMDAIFQSGVRVLAL--SDLVGLGEPEsagpLIEDPPREPEQPAFVFYTSGTTGLPKGAVIP----QRAAE--SRV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 109 IVM---AGGRPGDvfHNAYgYGLF-----TGGLGLHYGAERLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLA 180
Cdd:cd05923 180 LFMstqAGLRHGR--HNVV-LGLMplyhvIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 181 EMMEDMGLKpwTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVIGPGVAMECREA---KDGLHiAEDHFLPev 257
Cdd:cd05923 257 AAAEFAGLK--LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGtemRPGFF-SEVRIVR-- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 258 IHPQTGEPLPDGEYGELVFTSL--------------TKEALPILRYRTGDITALHREvcrcGRThtrmsRIKGRIDDMLI 323
Cdd:cd05923 332 IGGSPDEALANGEEGELIVAAAadaaftgylnqpeaTAKKLQDGWYRTGDVGYVDPS----GDV-----RILGRVDDMII 402
|
330
....*....|....*
gi 1705143246 324 IRGVNVFPSELEAVL 338
Cdd:cd05923 403 SGGENIHPSEIERVL 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
71-338 |
5.43e-11 |
|
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: 64.04 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 71 EQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAelcARSIVMAGGRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVPVS 150
Cdd:cd05935 82 ELDDLALIPYTSGTTGLPKGCMHTHFSAAANA---LQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 151 GGNRSRQVTLIQDFLPRGIGGTPSFILSLaemMEDMGLKP--WTTSLEYGIfGAEPWSEEMRQTLEEKWGIDALDIYGLS 228
Cdd:cd05935 159 RWDRETALELIEKYKVTFWTNIPTMLVDL---LATPEFKTrdLSSLKVLTG-GGAPMPPAVAEKLLKLTGLRFVEGYGLT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 229 EVIGPG-VAMECREAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFT------------SLTKEALPILR----YRT 291
Cdd:cd05935 235 ETMSQThTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRgpqifkgywnrpEETEESFIEIKgrrfFRT 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1705143246 292 GDITALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:cd05935 315 GDLGYMDEE----GYFF-----FVDRVKRMINVSGFKVWPAEVEAKL 352
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
74-345 |
1.64e-10 |
|
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: 62.13 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 74 EVARIHGSSGTSGKPT-VVGYTRKDIQRWAELCARSIVMAGGR-----PgdVFHNaYGY--GLFTGGLGlhygaerlGAT 145
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgVMCAHRQTLRAAAAWADCADLTEDDRyliinP--FFHT-FGYkaGIVACLLT--------GAT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 146 VVPVSGGNRSRQVTLIQD----FLPrgigGTPSFILSlaeMMEDMGLKPWT-TSLEYGIFGAEPWSEEMRQTLEEKWGID 220
Cdd:cd17638 70 VVPVAVFDVDAILEAIEReritVLP----GPPTLFQS---LLDHPGRKKFDlSSLRAAVTGAATVPVELVRRMRSELGFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 221 A-LDIYGLSEVigpGVAMECREAKDglhiaedhflPEVIHPQTGEPLPDGEY-----GELVF------------TSLTKE 282
Cdd:cd17638 143 TvLTAYGLTEA---GVATMCRPGDD----------AETVATTCGRACPGFEVriaddGEVLVrgynvmqgylddPEATAE 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1705143246 283 ALPILRY-RTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELA 345
Cdd:cd17638 210 AIDADGWlHTGDVGELDER----GYL-----RITDRLKDMYIVGGFNVYPAEVEGALAEHPGVA 264
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
64-345 |
1.73e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 62.61 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 64 PFRMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQR----WAELcarsivmAGGRPGD-------VFHNaYGYglfTGG 132
Cdd:PRK07656 157 AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSnaadWAEY-------LGLTEGDrylaanpFFHV-FGY---KAG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 133 LglhYGAERLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSL--AEMMEDMGLKpwttSLEYGIFGAEPWSEEMR 210
Cdd:PRK07656 226 V---NAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLlqHPDRSAEDLS----SLRLAVTGAASMPVALL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 211 QTLEEKWGID-ALDIYGLSEviGPGVAMECREAKDGLHIAE------DHFLPEVIHPQtGEPLPDGEYGELVF------- 276
Cdd:PRK07656 299 ERFESELGVDiVLTGYGLSE--ASGVTTFNRLDDDRKTVAGtigtaiAGVENKIVNEL-GEEVPVGEVGELLVrgpnvmk 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1705143246 277 -----TSLTKEAlpiLRY----RTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELA 345
Cdd:PRK07656 376 gyyddPEATAAA---IDAdgwlHTGDLGRLDEE----GYL-----YIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVA 441
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
70-339 |
6.60e-10 |
|
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: 60.71 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 70 VEQEEVARIHGSSGTSGKPTVVGYTRKDI--------QRWAELCARSIVMAGGRPgdVFHnAYGYGLFTgglglhYGAER 141
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLiamvaqfvAGEGSNSDSEDVFLCVLP--MFH-IYGLSSFA------LGLLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 142 LGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLA--EMMEDMGLKpwttSLEYGIFGAEPWSEEMRQTLEEKW-G 218
Cdd:cd05904 226 LGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVksPIVDKYDLS----SLRQIMSGAAPLGKELIEAFRAKFpN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 219 IDALDIYGLSEViGPGVAMECREAKDGLHIAEDHFLPE-----VIHPQTGEPLPDGEYGELVF----------------- 276
Cdd:cd05904 302 VDLGQGYGMTES-TGVVAMCFAPEKDRAKYGSVGRLVPnveakIVDPETGESLPPNQTGELWIrgpsimkgylnnpeata 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1705143246 277 TSLTKEA-LpilryRTGDItalhrevcrCGRTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd05904 381 ATIDKEGwL-----HTGDL---------CYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLL 430
|
|
| aden_form_hyp |
TIGR02304 |
putative adenylate-forming enzyme; Members of this family form a distinct clade within a ... |
157-363 |
8.13e-10 |
|
putative adenylate-forming enzyme; Members of this family form a distinct clade within a larger family of proteins that also includes coenzyme F390 synthetase, an enzyme known in Methanobacterium thermoautotrophicum and a few other methanogenic archaea. That enzyme adenylates coenzyme F420 to F390, a reversible process, during oxygen stress. Other informative homologies include domains of the non-ribosomal peptide synthetases involved in activation by adenylation. The family defined by this model is likely to be of an adenylate-forming enzyme related to but distinct from coenzyme F390 synthetase.
Pssm-ID: 274074 [Multi-domain] Cd Length: 430 Bit Score: 60.30 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 157 QVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLkpwTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVIgpgVA 236
Cdd:TIGR02304 179 HIKRLNQRKPSIIVAPPSVLRALALEVMEGEL---TIKPKKVISVAEVLEPQDRELIRNVFKNTVHQIYQATEGF---LA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 237 MECREAKdgLHIAED--HFLPEVIHpQTGEPLPdgeygelVFTSLTKEALPILRYRTGDITALHREVCRCGRTHTRMSRI 314
Cdd:TIGR02304 253 STCRCGT--LHLNEDlvHIEKQYLD-EHKRFVP-------IITDFTRTTQPIVRYRLNDILVESEQPCSCGSATMAIERI 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1705143246 315 KGRIDDMLII-----RGVNVFPSELEAVLLNFEELAPHYQLVVTrekSIDQLTL 363
Cdd:TIGR02304 323 EGRQDDIFQLitrsgDEQTVFPDFIRRVILFTLPLIVEYRVLQT---GSAQLEL 373
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
64-345 |
1.37e-09 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 60.13 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 64 PFRMFAVEQEEVARIHGSSGTSGKP--------TVVGYTRKDIQRWAELcarsivmaggRPGDVFHNAYGYGLFTGGLGL 135
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPkgvvhthgGYLVHAATTAKYVLDL----------KPGDVFWCTADIGWATGHSYI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 136 HYGAERLGATVVPVSG----GNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTTSLEYgIFGA-EPWSEEMR 210
Cdd:COG0365 245 VYGPLLNGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRL-LGSAgEPLNPEVW 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 211 QTLEEKWGIDALDIYGLSE----VIGPGVAMECRE---AKDGLHIAedhflPEVIHPQtGEPLPDGEYGELV----FTSL 279
Cdd:COG0365 324 EWWYEAVGVPIVDGWGQTEtggiFISNLPGLPVKPgsmGKPVPGYD-----VAVVDED-GNPVPPGEEGELVikgpWPGM 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 280 TKEalpILR----------------YRTGDitalhreVCRC---GRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVLLN 340
Cdd:COG0365 398 FRG---YWNdperyretyfgrfpgwYRTGD-------GARRdedGYFW-----ILGRSDDVINVSGHRIGTAEIESALVS 462
|
....*
gi 1705143246 341 FEELA 345
Cdd:COG0365 463 HPAVA 467
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
64-345 |
4.50e-09 |
|
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: 57.96 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 64 PFRMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELCArSIVMAGGRPGDV-------FHnAYGyglFTGGLGLH 136
Cdd:cd05936 116 LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIK-AWLEDLLEGDDVvlaalplFH-VFG---LTVALLLP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 137 YgaeRLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDmgLKPWTTSLEYGIFGAEPWSEEMRQTLEEK 216
Cdd:cd05936 191 L---ALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLCISGGAPLPVEVAERFEEL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 217 WGIDALDIYGLSEViGPGVAMECREAKD-----GLhiaedhFLP----EVIHPQtGEPLPDGEYGEL------VFT---- 277
Cdd:cd05936 266 TGVPIVEGYGLTET-SPVVAVNPLDGPRkpgsiGI------PLPgtevKIVDDD-GEELPPGEVGELwvrgpqVMKgywn 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 278 --SLTKEALPILRYRTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELA 345
Cdd:cd05936 338 rpEETAEAFVDGWLRTGDIGYMDED----GYF-----FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVA 398
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-340 |
4.84e-09 |
|
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: 58.07 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIvmaGGRPGDV-------FH-NAYGYGLftgglglhYGAERLGATVVPVSGG 152
Cdd:cd05934 89 TSGTTGPPKGVVITHANLTFAGYYSARRF---GLGEDDVyltvlplFHiNAQAVSV--------LAALSVGATLVLLPRF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 153 NRSRQVTLIQDF---LPRGIGGTPSFILSLAEMMEDMGLKPWTtsleygIFGAEPWSEEMRQtLEEKWGIDALDIYGLSE 229
Cdd:cd05934 158 SASRFWSDVRRYgatVTNYLGAMLSYLLAQPPSPDDRAHRLRA------AYGAPNPPELHEE-FEERFGVRLLEGYGMTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 230 ----VIGP----------GVAMECREAKdglhIAEDHflpevihpqtGEPLPDGEYGELVFTSL---------------T 280
Cdd:cd05934 231 tivgVIGPrdeprrpgsiGRPAPGYEVR----IVDDD----------GQELPAGEPGELVIRGLrgwgffkgyynmpeaT 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 281 KEALPILRYRTGDITALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVLLN 340
Cdd:cd05934 297 AEAMRNGWFHTGDLGYRDAD----GFFY-----FVDRKKDMIRRRGENISSAEVERAILR 347
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
23-348 |
2.61e-08 |
|
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: 55.75 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 23 SLVPFYRRKLDAAGIKPQDILGMEDLLKLPftRKSDLREQYPfrmfaveqEEVARIHGSSGTSGKPTVVGYTRKDIqrwA 102
Cdd:cd05906 127 ELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLPQSRP--------DDLALLMLTSGSTGFPKAVPLTHRNI---L 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 103 ELCARSIVMAGGRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVPVSGGNRSRQVTLIQDFLPR-GIGGT--PSFILSL 179
Cdd:cd05906 194 ARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRyRVTITwaPNFAFAL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 180 -AEMMEDMGLKPWT-TSLEYGIFGAEPWSEEM-RQTLEekwgidALDIYGL-SEVIGPGVAM--------ECREAKDGLH 247
Cdd:cd05906 274 lNDLLEEIEDGTWDlSSLRYLVNAGEAVVAKTiRRLLR------LLEPYGLpPDAIRPAFGMtetcsgviYSRSFPTYDH 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 248 IAEDHFL------PEV---IHPQTGEPLPDGEYGEL------VFT------SLTKEAL-PILRYRTGDItalhrevcrcG 305
Cdd:cd05906 348 SQALEFVslgrpiPGVsmrIVDDEGQLLPEGEVGRLqvrgpvVTKgyynnpEANAEAFtEDGWFRTGDL----------G 417
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1705143246 306 RTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELAPHY 348
Cdd:cd05906 418 FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
81-339 |
7.53e-08 |
|
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: 54.30 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIVmaGGRPGDVFHNA----YGYGLftgGLGLHYgAERLGATVVPVSGGNRSR 156
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNVL--GIREDDVCFSAaklfFAYGL---GNSLTF-PLSVGATTVLMPERPTPA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 157 QV-TLIQDFLPRGIGGTPSFILSL--AEMMEDMGLKpwttSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVigp 233
Cdd:cd05959 245 AVfKRIRRYRPTVFFGVPTLYAAMlaAPNLPSRDLS----SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEM--- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 234 gvamecreakdgLHIaedhFL---PEVIHPQT----------------GEPLPDGEYGELVFT------------SLTKE 282
Cdd:cd05959 318 ------------LHI----FLsnrPGRVRYGTtgkpvpgyevelrdedGGDVADGEPGELYVRgpssatmywnnrDKTRD 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1705143246 283 ALPILRYRTGDitalhREVCRCGRTHTrmsrIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd05959 382 TFQGEWTRTGD-----KYVRDDDGFYT----YAGRADDMLKVSGIWVSPFEVESALV 429
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
257-421 |
9.41e-08 |
|
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: 54.17 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 257 VIHPQTGEPLPDGEYGEL---------------VFTSLTKEALPILR----YRTGDITALHRevcrcGRTHtrmsrIKGR 317
Cdd:cd05931 368 IVDPETGRELPDGEVGEIwvrgpsvasgywgrpEATAETFGALAATDeggwLRTGDLGFLHD-----GELY-----ITGR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 318 IDDMLIIRGVNVFPSELEAVLLNF-EELAPHYQLVVtrekSIDQLTLEVEVSEAwfrsiESSFGQGNERVVQLCKRL-QS 395
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEAhPALRPGCVAAF----SVPDDGEERLVVVA-----EVERGADPADLAAIAAAIrAA 508
|
170 180
....*....|....*....|....*..
gi 1705143246 396 VVKDTLYVTTKVILKEPKSLPR-SEGK 421
Cdd:cd05931 509 VAREHGVAPADVVLVRPGSIPRtSSGK 535
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-338 |
2.36e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 52.88 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 82 SGTSGKPTVVGYTRKDIQRWAELCARSIVMaggRPGDV-------FHnaygyglfTGGLGLHYGAERLGAT-VVPvsggn 153
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKL---SRDDVylvivpmFH--------VHAWGLPYLALMAGAKqVIP----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 154 RSRQVTLIQDF--LPRgiggtPSFILSLAEMMEDMGLKP-----WTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYG 226
Cdd:PRK06187 240 RRFDPENLLDLieTER-----VTFFFAVPTIWQMLLKAPrayfvDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 227 LSEvIGPGVAMecreakdgLHiAEDHFLPEVIHPQT----------------GEPLP--DGEYGELVFTS---------- 278
Cdd:PRK06187 315 MTE-TSPVVSV--------LP-PEDQLPGQWTKRRSagrplpgvearivdddGDELPpdGGEVGEIIVRGpwlmqgywnr 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1705143246 279 --LTKEALPILRYRTGDITALHRE--VcrcgrthtrmsRIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:PRK06187 385 peATAETIDGGWLHTGDVGYIDEDgyL-----------YITDRIKDVIISGGENIYPRELEDAL 437
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
39-275 |
3.00e-07 |
|
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: 52.33 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 39 PQDILGMEDL-------------LKLPFTRKSDLREQYpfrMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELC 105
Cdd:cd05909 103 DARIVYLEDLrakiskadkckafLAGKFPPKWLLRIFG---VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 106 ARSI------VMAGGRPgdVFHnAYGyglFTGGLGLhygAERLGATVVPVSGGNRSRQVT-LIQDFLPRGIGGTPSFILS 178
Cdd:cd05909 180 TAIFdpnpedVVFGALP--FFH-SFG---LTGCLWL---PLLSGIKVVFHPNPLDYKKIPeLIYDKKATILLGTPTFLRG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 179 LAEMMEDMGLKpwttSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSE---VIGPGVA-MECREAKDGLHIAEDHFL 254
Cdd:cd05909 251 YARAAHPEDFS----SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEcspVISVNTPqSPNKEGTVGRPLPGMEVK 326
|
250 260
....*....|....*....|.
gi 1705143246 255 peVIHPQTGEPLPDGEYGELV 275
Cdd:cd05909 327 --IVSVETHEEVPIGEGGLLL 345
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
66-338 |
5.23e-07 |
|
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: 51.69 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 66 RMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELCARSIVmaGGRPGD-VFHNA---YGYGLftgGLGLHYGAEr 141
Cdd:cd05919 84 RLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAL--GLTPGDrVFSSAkmfFGYGL---GNSLWFPLA- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 142 LGATVVPVSGG-NRSRQVTLIQDFLPRGIGGTPSFILSLaeMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGID 220
Cdd:cd05919 158 VGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANL--LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 221 ALDIYGLSEVIGPGVAMECREAKDG-----LHIAEDHFLPEvihpqTGEPLPDGEYGELVFTSLTkEALPILRYRTGDIT 295
Cdd:cd05919 236 ILDGIGATEVGHIFLSNRPGAWRLGstgrpVPGYEIRLVDE-----EGHTIPPGEEGDLLVRGPS-AAVGYWNNPEKSRA 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1705143246 296 ALHREVCRCGRTHTRMS----RIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:cd05919 310 TFNGGWYRTGDKFCRDAdgwyTHAGRADDMLKVGGQWVSPVEVESLI 356
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
261-338 |
7.26e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 51.20 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 261 QTGEPLPDGEYGELVFTS------------LTKEALPILRYRTGDITALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVN 328
Cdd:PRK06178 404 ETGELLPLGAEGEIVVRTpsllkgywnkpeATAEALRDGWLHTGDIGKIDEQ----GFLH-----YLGRRKEMLKVNGMS 474
|
90
....*....|
gi 1705143246 329 VFPSELEAVL 338
Cdd:PRK06178 475 VFPSEVEALL 484
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
143-347 |
8.08e-07 |
|
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: 50.74 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 143 GATVVPVSGGNRSRQV-TLIQDFLPRGIGGTPS-FIlslAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGID 220
Cdd:cd05917 69 GATMVFPSPSFDPLAVlEAIEKEKCTALHGVPTmFI---AELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 221 ALDI-YGLSEViGPGVAMEcrEAKDGL-------HIAEDHFLPEVIHPQTGEPLPDGEYGELVFT------------SLT 280
Cdd:cd05917 146 DVTIaYGMTET-SPVSTQT--RTDDSIekrvntvGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRgysvmkgywndpEKT 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1705143246 281 KEALPILR-YRTGDITALHrEVCRCgrthtrmsRIKGRIDDMLIIRGVNVFPSELEavllnfEELAPH 347
Cdd:cd05917 223 AEAIDGDGwLHTGDLAVMD-EDGYC--------RIVGRIKDMIIRGGENIYPREIE------EFLHTH 275
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
218-340 |
9.79e-07 |
|
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: 50.76 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 218 GIDALDIYGLSEVIGPGVAMECREAKDGLHIAE----------DHFLPE---VIHPQTGEPLP-DGE-YGELVF------ 276
Cdd:cd12118 271 GFDVTHVYGLTETYGPATVCAWKPEWDELPTEErarlkarqgvRYVGLEevdVLDPETMKPVPrDGKtIGEIVFrgnivm 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 277 ------TSLTKEALPILRYRTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVLLN 340
Cdd:cd12118 351 kgylknPEATAEAFRGGWFHSGDLAVIHPD----GYI-----EIKDRSKDIIISGGENISSVEVEGVLYK 411
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-345 |
1.06e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 50.77 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 69 AVEQEEVARIHGSSGTSGKPtvvgytrkdiqRWAELCARSIV---------MAGGRPGD--------VFHnAYGYGLfTG 131
Cdd:PRK05605 215 RPTPDDVALILYTSGTTGKP-----------KGAQLTHRNLFanaaqgkawVPGLGDGPervlaalpMFH-AYGLTL-CL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 132 GLGLHYGAERLgatVVPvsggnrSRQVTLIQD--------FLPrgigGTPSFILSLAEMMEDMGLKpwTTSLEYGIFGAE 203
Cdd:PRK05605 282 TLAVSIGGELV---LLP------APDIDLILDamkkhpptWLP----GVPPLYEKIAEAAEERGVD--LSGVRNAFSGAM 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 204 PWSEEMRQTLEEKWGIDALDIYGLSE----VIGPGVAMECREAKDGLHiaedhfLPE----VIHPQT-GEPLPDGEYGEL 274
Cdd:PRK05605 347 ALPVSTVELWEKLTGGLLVEGYGLTEtspiIVGNPMSDDRRPGYVGVP------FPDtevrIVDPEDpDETMPDGEEGEL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 275 ------VFT------SLTKEALPILRYRTGDITalhrevcrcgrthtRMS-----RIKGRIDDMLIIRGVNVFPSELEAV 337
Cdd:PRK05605 421 lvrgpqVFKgywnrpEETAKSFLDGWFRTGDVV--------------VMEedgfiRIVDRIKELIITGGFNVYPAEVEEV 486
|
....*...
gi 1705143246 338 LLNFEELA 345
Cdd:PRK05605 487 LREHPGVE 494
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
36-339 |
1.94e-06 |
|
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: 49.90 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 36 GIKPQDILGMEDLLKLPFTRksdlREQYPFRMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELcARSIVMAGGR 115
Cdd:cd05911 113 DDKPDGVLSIEDLLSPTLGE----EDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQ-VQTFLYGNDG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 116 PGDV-------FHnayGYGLFTGglgLHYGAerLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMmeDMGL 188
Cdd:cd05911 188 SNDVilgflplYH---IYGLFTT---LASLL--NGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKS--PLLD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 189 KPWTTSLEYGIFGAEPWSEEMRQTLEEKWGIDAL-DIYGLSEViGPGVAMecreAKDGLHI--AEDHFLP----EVIHPQ 261
Cdd:cd05911 258 KYDLSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTET-GGILTV----NPDGDDKpgSVGRLLPnveaKIVDDD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 262 TGEPLPDGEYGELVFTSLTK--------EALPILR-----YRTGDItALHREVcrcGRTHtrmsrIKGRIDDMLIIRGVN 328
Cdd:cd05911 333 GKDSLGPNEPGEICVRGPQVmkgyynnpEATKETFdedgwLHTGDI-GYFDED---GYLY-----IVDRKKELIKYKGFQ 403
|
330
....*....|.
gi 1705143246 329 VFPSELEAVLL 339
Cdd:cd05911 404 VAPAELEAVLL 414
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
66-339 |
2.26e-06 |
|
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: 49.64 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 66 RMFAVEQEEVARIHGSSGTSGKPTVVGYTrkdiQRWAelcARSIVMAGG----RPGDVFHNAYGYGLFTGGLGLHYGAER 141
Cdd:cd05972 74 KAIVTDAEDPALIYFTSGTTGLPKGVLHT----HSYP---LGHIPTAAYwlglRPDDIHWNIADPGWAKGAWSSFFGPWL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 142 LGATVVpVSGGNR---SRQVTLIQDFLPRGIGGTPSfilSLAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEKWG 218
Cdd:cd05972 147 LGATVF-VYEGPRfdaERILELLERYGVTSFCGPPT---AYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 219 IDALDIYGLSEVigpgvamecreakdGLHIAEDHFLPevIHP----------------QTGEPLPDGEYGELV------- 275
Cdd:cd05972 223 LPIRDGYGQTET--------------GLTVGNFPDMP--VKPgsmgrptpgydvaiidDDGRELPPGEEGDIAiklpppg 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705143246 276 ----FTSLTKEALPILR---YRTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd05972 287 lflgYVGDPEKTEASIRgdyYLTGDRAYRDED----GYF-----WFVGRADDIIKSSGYRIGPFEVESALL 348
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
65-339 |
4.38e-06 |
|
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: 48.53 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 65 FRMFAVEQE--EVARIHGSSGTSGKP--------TVVGYTRKDIQRWaelcarsivmaGGRPGDVFHNAYGYGLFTGGLG 134
Cdd:cd05903 83 FRQFDPAAMpdAVALLLFTSGTTGEPkgvmhshnTLSASIRQYAERL-----------GLGPGDVFLVASPMAHQTGFVY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 135 LHYGAERLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKPwtTSLEYGIFGAEPWSEEMRQTLE 214
Cdd:cd05903 152 GFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPL--SRLRTFVCGGATVPRSLARRAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 215 EKWGIDALDIYGLSEVigPGVAMECREAKDGLHIAED-HFLPEV---IHPQTGEPLPDGEYGELVFTS------------ 278
Cdd:cd05903 230 ELLGAKVCSAYGSTEC--PGAVTSITPAPEDRRLYTDgRPLPGVeikVVDDTGATLAPGVEGELLSRGpsvflgyldrpd 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705143246 279 LTKEALPILRYRTGDitalhrevcRCGRTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd05903 308 LTADAAPEGWFRTGD---------LARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
179-339 |
6.74e-05 |
|
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: 44.63 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 179 LAEMMEDMGLKPWTTsleYGifgaepwSEEMRQTLEEKwgidALDIYGLSEVigpGVAMECREakdgLHIAEDhflpEVI 258
Cdd:cd17630 127 LLERAADRGIPLYTT---YG-------MTETASQVATK----RPDGFGRGGV---GVLLPGRE----LRIVED----GEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 259 HPQtGEPLPDGEYGELVFTSLTKEALpilrYRTGDITALHREvcrcGRTHtrmsrIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:cd17630 182 WVG-GASLAMGYLRGQLVPEFNEDGW----FTTKDLGELHAD----GRLT-----VLGRADNMIISGGENIQPEEIEAAL 247
|
.
gi 1705143246 339 L 339
Cdd:cd17630 248 A 248
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
215-338 |
7.29e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 44.94 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 215 EKWGIDALDIYGLSEVIGPGVAMECREAKDGLHIAED-----------HFLPE--VIHPQTGEPLP-DGE-YGELVF--- 276
Cdd:PRK08162 317 EEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERaqlkarqgvryPLQEGvtVLDPDTMQPVPaDGEtIGEIMFrgn 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705143246 277 ---------TSLTKEALPILRYRTGDITALHREvcrcGRThtrmsRIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:PRK08162 397 ivmkgylknPKATEEAFAGGWFHTGDLAVLHPD----GYI-----KIKDRSKDIIISGGENISSIEVEDVL 458
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
70-345 |
2.29e-04 |
|
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: 43.22 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 70 VEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELCARSIVMAGGRPGDVFHNAYGYGLFTGGLGLhygAERLGATVVPV 149
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFAR---SLLNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 150 SGGNRSRQVTLIQDFLPRGIG---GTPSFILSLAEMMEDMGLKPwtTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDI-- 224
Cdd:cd17650 167 PDEVKLDPAALYDLILKSRITlmeSTPALIRPVMAYVYRNGLDL--SAMRLLIVGSDGCKAQDFKTLAARFGQGMRIIns 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 225 YGLSEV-IGPGVAMECR-EAKDGLHIAEDHFLPEV---IHPQTGEPLPDGEYGELVF------------TSLTKEALPIL 287
Cdd:cd17650 245 YGVTEAtIDSTYYEEGRdPLGDSANVPIGRPLPNTamyVLDERLQPQPVGVAGELYIggagvargylnrPELTAERFVEN 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705143246 288 R-------YRTGDITalhrevcrCGRTHTRMsRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELA 345
Cdd:cd17650 325 PfapgermYRTGDLA--------RWRADGNV-ELLGRVDHQVKIRGFRIELGEIESQLARHPAID 380
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
257-424 |
3.36e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 257 VIHPQTGEPLPDGEYGElVFTSLTKEALPIlrYRTGDITAlHREVCRCGRTHTRMSR----------IKGRIDDMLIIRG 326
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGE-IWASGPSIAHGY--WRNPEASA-KTFVEHDGRTWLRTGDlgflrdgelfVTGRLKDMLIVRG 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 327 VNVFPSELEAVLlnfEElaphyQLVVTREKSIDQLTLEVEVSEAWfrSIESSFGQGNERVV---QLCKRLQSVVKDTLY- 402
Cdd:PRK05691 459 HNLYPQDIEKTV---ER-----EVEVVRKGRVAAFAVNHQGEEGI--GIAAEISRSVQKILppqALIKSIRQAVAEACQe 528
|
170 180
....*....|....*....|...
gi 1705143246 403 VTTKVILKEPKSLPR-SEGKAVR 424
Cdd:PRK05691 529 APSVVLLLNPGALPKtSSGKLQR 551
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
172-339 |
4.66e-04 |
|
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: 42.29 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 172 TPSFILSLAEmmEDMGLKPWTTSLEYGIFGAE--------PWSE---EMRQTLEEKWGI------------DALDIYGLS 228
Cdd:cd17643 191 TPSAFYQLVE--AADRDGRDPLALRYVIFGGEaleaamlrPWAGrfgLDRPQLVNMYGItettvhvtfrplDAADLPAAA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 229 E-VIG---PGVamecreakdGLHIAEDHflpevihpqtGEPLPDGEYGELV--------------------FTSLTKEAL 284
Cdd:cd17643 269 AsPIGrplPGL---------RVYVLDAD----------GRPVPPGVVGELYvsgagvargylgrpeltaerFVANPFGGP 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1705143246 285 PILRYRTGDitaLHRevcrcgRTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVLL 339
Cdd:cd17643 330 GSRMYRTGD---LAR------RLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
59-340 |
5.26e-04 |
|
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: 42.04 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 59 LREQYPFRMFAVEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELCaRSIVMAGgrPGDV------FHNAYGYgLFTGG 132
Cdd:cd05914 75 LNHSEAKAIFVSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV-KEVVLLG--KGDKilsilpLHHIYPL-TFTLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 133 LGLHYGA-----ERLG---------ATVVPVSGGNRSRQV--TLIQDFLPRgiggtpsfiLSLAEMMEDMGLKPWTTSLE 196
Cdd:cd05914 151 LPLLNGAhvvflDKIPsakiialafAQVTPTLGVPVPLVIekIFKMDIIPK---------LTLKKFKFKLAKKINNRKIR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 197 YGIF----------------GAEPWSEEMRQTLeEKWGIDALDIYGLSEViGPGVAM---------ECREAKDGLHIAED 251
Cdd:cd05914 222 KLAFkkvheafggnikefviGGAKINPDVEEFL-RTIGFPYTIGYGMTET-APIISYsppnrirlgSAGKVIDGVEVRID 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 252 HFLPEVihpQTGEPLPDGE---YGELVFTSLTKEALPILRY-RTGDITALHREvcrcGRTHtrmsrIKGRIDDMLII-RG 326
Cdd:cd05914 300 SPDPAT---GEGEIIVRGPnvmKGYYKNPEATAEAFDKDGWfHTGDLGKIDAE----GYLY-----IRGRKKEMIVLsSG 367
|
330
....*....|....
gi 1705143246 327 VNVFPSELEAVLLN 340
Cdd:cd05914 368 KNIYPEEIEAKINN 381
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
314-344 |
6.57e-04 |
|
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: 41.62 E-value: 6.57e-04
10 20 30
....*....|....*....|....*....|.
gi 1705143246 314 IKGRIDDMLIIRGVNVFPSELEAVLLNFEEL 344
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGI 256
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
262-339 |
1.04e-03 |
|
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: 41.28 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 262 TGEPLPDGEYGELVF-----------------TSLTKEALpilrYRTGDItalhrevCRcgRTHTRMSRIKGRIDDMlII 324
Cdd:COG1021 371 DGNPVPPGEVGELLTrgpytirgyyrapehnaRAFTPDGF----YRTGDL-------VR--RTPDGYLVVEGRAKDQ-IN 436
|
90
....*....|....*.
gi 1705143246 325 R-GVNVFPSELEAVLL 339
Cdd:COG1021 437 RgGEKIAAEEVENLLL 452
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
171-272 |
1.07e-03 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 41.45 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 171 GTPSFILSLA-------EMMEdmglkpwttSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEViGPGVAMEC---R 240
Cdd:PRK08633 878 GTPTFLRLYLrnkklhpLMFA---------SLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATET-SPVASVNLpdvL 947
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1705143246 241 EAKDGLHIAED-----HFLP----EVIHPQTGEPLPDGEYG 272
Cdd:PRK08633 948 AADFKRQTGSKegsvgMPLPgvavRIVDPETFEELPPGEDG 988
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
193-344 |
1.22e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 41.17 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 193 TSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSE---VIGPGVAMECReAKDGLHIAEDHFLPEVIHPQTGEPLPDG 269
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTEsspVTHSNFLWEKR-VPGSIGVPWPDTEAMIMSLETGEALPPG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 270 EYGELV---------FTSLTKEALPILR---YRTGDITALHREvcrcgrthtRMSRIKGRIDDMLIIRGVNVFPSELEAV 337
Cdd:PRK06710 402 EIGEIVvkgpqimkgYWNKPEETAAVLQdgwLHTGDVGYMDED---------GFFYVKDRKKDMIVASGFNVYPREVEEV 472
|
....*..
gi 1705143246 338 LLNFEEL 344
Cdd:PRK06710 473 LYEHEKV 479
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
194-339 |
1.42e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 40.79 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 194 SLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEVIG---------------PGVAM-ECREAKDGLHIAedhflpev 257
Cdd:PRK07470 281 SLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGnitvlppalhdaedgPDARIgTCGFERTGMEVQ-------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 258 IHPQTGEPLPDGEYGEL------VFTSL------TKEALPILRYRTGDITALHREvcrcgrthtRMSRIKGRIDDMLIIR 325
Cdd:PRK07470 353 IQDDEGRELPPGETGEIcvigpaVFAGYynnpeaNAKAFRDGWFRTGDLGHLDAR---------GFLYITGRASDMYISG 423
|
170
....*....|....
gi 1705143246 326 GVNVFPSELEAVLL 339
Cdd:PRK07470 424 GSNVYPREIEEKLL 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
73-370 |
1.78e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 41.10 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 73 EEVARIHGSSGTSGKPTVVGYtrkdiqRWAELCARSIVMAG--GRPGDVFHNAYGYGLFTGGLGLHYGAERLGATVVpVS 150
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGI------RHSALSNHLCWMQQayGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVV-LA 3268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 151 GGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTTSLEYGIFGAEPWSEEMRQTLEEkwGIDALDIYGLSE- 229
Cdd:PRK12316 3269 GPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEa 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 230 VIGPGVAMECREAKDGLHIAED-HFLPEVIHPQTGEPLPDGEYGELVF------------TSLTKEAL------PILR-Y 289
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAVPIGRPiANRACYILDGSLEPVPVGALGELYLggeglargyhnrPGLTAERFvpdpfvPGERlY 3426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 290 RTGDItALHREvcrcgrthTRMSRIKGRIDDMLIIRGVNVFPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSE 369
Cdd:PRK12316 3427 RTGDL-ARYRA--------DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGD 3497
|
.
gi 1705143246 370 A 370
Cdd:PRK12316 3498 L 3498
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-339 |
1.83e-03 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 40.49 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 115 RPGDVFHNAYGYGlFTGGLG------LHYGAERLGATVVPVSGGnrsRQVTLIQDFlprgiGGTPSFILSLA-EMMEDMG 187
Cdd:cd05971 129 RDGDLYWTPADWA-WIGGLLdvllpsLYFGVPVLAHRMTKFDPK---AALDLMSRY-----GVTTAFLPPTAlKMMRQQG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 188 --LKPWTTSLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSE---VIGPGVAMecREAKDGL-------HIAEdhflp 255
Cdd:cd05971 200 eqLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTEcnlVIGNCSAL--FPIKPGSmgkpipgHRVA----- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 256 evIHPQTGEPLPDGEYGELVFtsLTKEALPILRY----------------RTGDITAlhrevcrcgRTHTRMSRIKGRID 319
Cdd:cd05971 273 --IVDDNGTPLPPGEVGEIAV--ELPDPVAFLGYwnnpsatekkmagdwlLTGDLGR---------KDSDGYFWYVGRDD 339
|
250 260
....*....|....*....|
gi 1705143246 320 DMLIIRGVNVFPSELEAVLL 339
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLL 359
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
81-338 |
2.89e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 39.73 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 81 SSGTSGKPTVVGYTRKDIQRWAELCARSIVMAggrPGDV------FHNAYGyglFTGGLGLHYGaerlGATVVPVSGGNR 154
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYD---PGAVllaalpFCGVFG---FSTLLGALAG----GAPLVCEPVFDA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 155 SRQVTLIQDF-LPRGIGGTPSFILSLAEMMEDmglKPWTTSLEYGIFGAEPWSEEMRQTLEEKwGIDALDIYGLSEVI-- 231
Cdd:PRK06164 259 ARTARALRRHrVTHTFGNDEMLRRILDTAGER---ADFPSARLFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQal 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 232 ---GPGVAMECREAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFTS------------LTKEAL-PILRYRTGDIT 295
Cdd:PRK06164 335 valQPATDPVSVRIEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRApslmrgyldnpdATARALtDDGYFRTGDLG 414
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1705143246 296 ALhrevcrcgrTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVL 338
Cdd:PRK06164 415 YT---------RGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
194-237 |
3.14e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 39.95 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1705143246 194 SLEYGIFGAEPWSEEMRQTLEEKWGIDALDIYGLSEViGPGVAM 237
Cdd:PRK06814 908 SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTET-APVIAL 950
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
70-344 |
4.89e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 39.05 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 70 VEQEEVARIHGSSGTSGKPTVVGYTRKDIQRWAELCARSIVMAGGRPGD---------VFHnAYGYGLFTGGLglhygaE 140
Cdd:PLN02574 195 IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSdnvylaalpMFH-IYGLSLFVVGL------L 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 141 RLGATVVPVSGGNRSRQVTLIQDFLPRGIGGTPSFILSLAEMMEDMGLKPWTtSLEYGIFGAEPWS----EEMRQTLEEk 216
Cdd:PLN02574 268 SLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLK-SLKQVSCGAAPLSgkfiQDFVQTLPH- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 217 wgIDALDIYGLSE---VIGPGVAMECREAKDGLHIAEDHFLPEVIHPQTGEPLPDGEYGELVFTS-------LTKEALPI 286
Cdd:PLN02574 346 --VDFIQGYGMTEstaVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGpgvmkgyLNNPKATQ 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1705143246 287 LR------YRTGDITALhrevcrcgrTHTRMSRIKGRIDDMLIIRGVNVFPSELEAVLLNFEEL 344
Cdd:PLN02574 424 STidkdgwLRTGDIAYF---------DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
263-370 |
5.01e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 39.03 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 263 GEPLPDGEYGELVFT------------SLTKEALPILRY-RTGDITALHREvcrcgrthtRMSRIKGRIDDMLIIRGVNV 329
Cdd:PRK12492 404 GNELPLGERGELCIKgpqvmkgywqqpEATAEALDAEGWfKTGDIAVIDPD---------GFVRIVDRKKDLIIVSGFNV 474
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1705143246 330 FPSELEAVLLNFEELAPHYQLVVTREKSIDQLTLEVEVSEA 370
Cdd:PRK12492 475 YPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP 515
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
261-342 |
8.74e-03 |
|
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: 38.07 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705143246 261 QTGEPLPDGEYGELVFT------------SLTKEA-LPI------LRYRTGDItALHREVcrcGRThtrmsRIKGRIDDM 321
Cdd:cd12115 284 RALQPVPLGVPGELYIGgagvargylgrpGLTAERfLPDpfgpgaRLYRTGDL-VRWRPD---GLL-----EFLGRADNQ 354
|
90 100
....*....|....*....|.
gi 1705143246 322 LIIRGVNVFPSELEAVLLNFE 342
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIP 375
|
|
| |
