NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488630032|ref|WP_002566721|]
View 

phenylacetate--CoA ligase [Enterocloster bolteae]

Protein Classification

phenylacetate--CoA ligase family protein( domain architecture ID 11446184)

phenylacetate--CoA ligase family protein similar to Staphylococcus aureus CapK, which is required for the biosynthesis of type 1 capsular polysaccharide

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 2-408 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: 582.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   2 KMKESQFLLIKEQLKKLTAKECFYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGT 79
Cdd:COG1541   15 ELEALQLERLRATVARAYENSPFYRRKFDeaGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEIVRIHASSGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  80 TGTPVIIPYTQKDVDDWALMFARCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDM 159
Cdd:COG1541   95 TGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRLMQDF 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 160 KSTVLCATSSYALLLAEEIAKRGIG-ERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAINCEKQGA 238
Cdd:COG1541  175 GPTVLVGTPSYLLYLAEVAEEEGIDpRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV-GPGVAYECEAQDG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 239 MHYWDDYIYIEIVDPRTGEVLPDGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGDCPCGSPYPRIGTLIGRTDDMVKVK 318
Cdd:COG1541  254 LHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIR 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 319 GVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKYALEIEIQNQFKGRIGLTPVVKLVELGELPRS 398
Cdd:COG1541  334 GVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAALKAVLGLRAEVELVEPGSLPRS 413

                        410
                 ....*....|
gi 488630032 399 EKKSTRVFDN 408
Cdd:COG1541  414 EGKAKRVIDR 423
 
Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 2-408 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: 582.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   2 KMKESQFLLIKEQLKKLTAKECFYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGT 79
Cdd:COG1541   15 ELEALQLERLRATVARAYENSPFYRRKFDeaGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEIVRIHASSGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  80 TGTPVIIPYTQKDVDDWALMFARCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDM 159
Cdd:COG1541   95 TGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRLMQDF 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 160 KSTVLCATSSYALLLAEEIAKRGIG-ERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAINCEKQGA 238
Cdd:COG1541  175 GPTVLVGTPSYLLYLAEVAEEEGIDpRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV-GPGVAYECEAQDG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 239 MHYWDDYIYIEIVDPRTGEVLPDGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGDCPCGSPYPRIGTLIGRTDDMVKVK 318
Cdd:COG1541  254 LHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIR 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 319 GVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKYALEIEIQNQFKGRIGLTPVVKLVELGELPRS 398
Cdd:COG1541  334 GVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAALKAVLGLRAEVELVEPGSLPRS 413

                        410
                 ....*....|
gi 488630032 399 EKKSTRVFDN 408
Cdd:COG1541  414 EGKAKRVIDR 423
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 24-409 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: 536.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  24 FYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGTTGTPVIIPYTQKDVDDWALMFA 101
Cdd:cd05913   32 FYRRKFAaaGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 102 RCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDMKSTVLCATSSYALLLAEEIAKR 181
Cdd:cd05913  112 RCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 182 GI-GERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVYGPGIAINCEKQGAMHYWDDYIYIEIVDPRTGEVLP 260
Cdd:cd05913  192 GIdPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFECEEKDGLHIWEDHFIPEIIDPETGEPVP 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 261 DGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGDCPCGSPYPRIGTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASSE 340
Cdd:cd05913  272 PGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPH 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488630032 341 YQVMVDHLMGKDVLTLFVETNPSINKY----ALEIEIQNQFKGRIGLTPVVKLVELGELPRSEKKSTRVFDNR 409
Cdd:cd05913  352 YQLILTRQEHLDELTIKVEVRPEADDDekleALKQRLERHIKSVLGVTVEVELVEPGSLPRSEGKAKRVIDKR 424
PA_CoA_ligase TIGR02155
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ...
 24-409 3.79e-138

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: 401.51  E-value: 3.79e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   24 FYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGTTGTPVIIPYTQKDVDDWALMFA 101
Cdd:TIGR02155  29 HYRKAFDaaGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRIHASSGTTGKPTVVGYTQNDIDTWSSVVA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  102 RCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDMKSTVLCATSSYALLLAEEIAKR 181
Cdd:TIGR02155 109 RSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQVQLIQDFKPDIIMVTPSYMLNLLEELKRM 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  182 GIG-ERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVYGPGIAINC-EKQGAMHYWDDYIYIEIVDPRTGEVL 259
Cdd:TIGR02155 189 GIDpAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAMECvETQDGLHIWEDHFYPEIIDPHTGEVL 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  260 PDGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGdcpCGSPYPRIGTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASS 339
Cdd:TIGR02155 269 PDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPG---TARTMRRMDRITGRSDDMLIIRGVNVFPTQLEEVILKMDELSP 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488630032  340 EYQVMVDHLMGKDVLTLFVETNPSIN-------KYALEIEIQNQFKGRIGLTPVVKLVELGELPRSEKKSTRVFDNR 409
Cdd:TIGR02155 346 HYQLELTRNGHMDELTLKVELKPESYtlrlheqASLLAGEIQHTIKQEVGVSMDVHLVEPGSLPRSEGKARRVVDLR 422
AMP-binding_C_2 pfam14535
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 319-409 3.76e-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: 122.20  E-value: 3.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  319 GVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKY-----ALEIEIQNQFKGRIGLTPVVKLVELG 393
Cdd:pfam14535   1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEikdleALEKRIAKELKSVLGVSVKVELVEPG 80

                          90
                  ....*....|....*.
gi 488630032  394 ELPRSEKKSTRVFDNR 409
Cdd:pfam14535  81 TLPRSEGKAKRVIDLR 96
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 77-336 4.62e-09

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 58.27  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  77 SGTTGTP--VIIPYTQKdvddWALMFARCYEMaGITNLDR-IQITPGY--GLWTAGI-GFQLGAErlgamTVPMGPGNTD 150
Cdd:PRK06187 176 SGTTGHPkgVVLSHRNL----FLHSLAVCAWL-KLSRDDVyLVIVPMFhvHAWGLPYlALMAGAK-----QVIPRRFDPE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 151 KQLRMMMDMKSTVLCA--TSSYALLLAEEIAKRGIGeriHLKKGVIGS--------ERWGEKmrnriaaeLGVDLFDIYG 220
Cdd:PRK06187 246 NLLDLIETERVTFFFAvpTIWQMLLKAPRAYFVDFS---SLRLVIYGGaalppallREFKEK--------FGIDLVQGYG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 221 LTEVyGPGIAINCEKQGAMHYWDDYI---------YIEIVDPRtGEVLP--DGEVGEIVITT---------LKKEGAPLI 280
Cdd:PRK06187 315 MTET-SPVVSVLPPEDQLPGQWTKRRsagrplpgvEARIVDDD-GDELPpdGGEVGEIIVRGpwlmqgywnRPEATAETI 392

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488630032 281 R---YRTHDLSRIvpgdcpcgSPYPRIgTLIGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:PRK06187 393 DggwLHTGDVGYI--------DEDGYL-YITDRIKDVIISGGENIYPRELEDALYGHPA 442
 
Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 2-408 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: 582.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   2 KMKESQFLLIKEQLKKLTAKECFYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGT 79
Cdd:COG1541   15 ELEALQLERLRATVARAYENSPFYRRKFDeaGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEIVRIHASSGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  80 TGTPVIIPYTQKDVDDWALMFARCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDM 159
Cdd:COG1541   95 TGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRLMQDF 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 160 KSTVLCATSSYALLLAEEIAKRGIG-ERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAINCEKQGA 238
Cdd:COG1541  175 GPTVLVGTPSYLLYLAEVAEEEGIDpRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV-GPGVAYECEAQDG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 239 MHYWDDYIYIEIVDPRTGEVLPDGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGDCPCGSPYPRIGTLIGRTDDMVKVK 318
Cdd:COG1541  254 LHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIR 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 319 GVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKYALEIEIQNQFKGRIGLTPVVKLVELGELPRS 398
Cdd:COG1541  334 GVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALAEAIAAALKAVLGLRAEVELVEPGSLPRS 413

                        410
                 ....*....|
gi 488630032 399 EKKSTRVFDN 408
Cdd:COG1541  414 EGKAKRVIDR 423
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 24-409 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: 536.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  24 FYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGTTGTPVIIPYTQKDVDDWALMFA 101
Cdd:cd05913   32 FYRRKFAaaGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 102 RCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDMKSTVLCATSSYALLLAEEIAKR 181
Cdd:cd05913  112 RCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 182 GI-GERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVYGPGIAINCEKQGAMHYWDDYIYIEIVDPRTGEVLP 260
Cdd:cd05913  192 GIdPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFECEEKDGLHIWEDHFIPEIIDPETGEPVP 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 261 DGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGDCPCGSPYPRIGTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASSE 340
Cdd:cd05913  272 PGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPH 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488630032 341 YQVMVDHLMGKDVLTLFVETNPSINKY----ALEIEIQNQFKGRIGLTPVVKLVELGELPRSEKKSTRVFDNR 409
Cdd:cd05913  352 YQLILTRQEHLDELTIKVEVRPEADDDekleALKQRLERHIKSVLGVTVEVELVEPGSLPRSEGKAKRVIDKR 424
PA_CoA_ligase TIGR02155
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ...
 24-409 3.79e-138

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: 401.51  E-value: 3.79e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   24 FYKHKLE--GVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGTTGTPVIIPYTQKDVDDWALMFA 101
Cdd:TIGR02155  29 HYRKAFDaaGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRIHASSGTTGKPTVVGYTQNDIDTWSSVVA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  102 RCYEMAGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRMMMDMKSTVLCATSSYALLLAEEIAKR 181
Cdd:TIGR02155 109 RSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQVQLIQDFKPDIIMVTPSYMLNLLEELKRM 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  182 GIG-ERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVYGPGIAINC-EKQGAMHYWDDYIYIEIVDPRTGEVL 259
Cdd:TIGR02155 189 GIDpAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAMECvETQDGLHIWEDHFYPEIIDPHTGEVL 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  260 PDGEVGEIVITTLKKEGAPLIRYRTHDLSRIVPGdcpCGSPYPRIGTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASS 339
Cdd:TIGR02155 269 PDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPG---TARTMRRMDRITGRSDDMLIIRGVNVFPTQLEEVILKMDELSP 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488630032  340 EYQVMVDHLMGKDVLTLFVETNPSIN-------KYALEIEIQNQFKGRIGLTPVVKLVELGELPRSEKKSTRVFDNR 409
Cdd:TIGR02155 346 HYQLELTRNGHMDELTLKVELKPESYtlrlheqASLLAGEIQHTIKQEVGVSMDVHLVEPGSLPRSEGKARRVVDLR 422
AMP-binding_C_2 pfam14535
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 319-409 3.76e-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: 122.20  E-value: 3.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  319 GVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKY-----ALEIEIQNQFKGRIGLTPVVKLVELG 393
Cdd:pfam14535   1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEikdleALEKRIAKELKSVLGVSVKVELVEPG 80

                          90
                  ....*....|....*.
gi 488630032  394 ELPRSEKKSTRVFDNR 409
Cdd:pfam14535  81 TLPRSEGKAKRVIDLR 96
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 76-398 1.49e-29

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: 117.00  E-value: 1.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDvddWALMFARCYEMAGITNLDRIQITPGYGlWTAGIGFQLGAERLGAMTVPMGPGNTDKQLRM 155
Cdd:cd04433    8 TSGTTGKPKGVVLSHRN---LLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFDPEAALEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 156 MMDMKSTVLCATSSYALLLAEEIAKRGIGERiHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAINCEK 235
Cdd:cd04433   84 IEREKVTILLGVPTLLARLLKAPESAGYDLS-SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTET-GGTVATGPPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 236 QGAMHYWD-----DYIYIEIVDPRTGEvLPDGEVGEIVITT-------LKKEGAPL-----IRYRTHDLSRIVPGDcpcg 298
Cdd:cd04433  162 DDARKPGSvgrpvPGVEVRIVDPDGGE-LPPGEIGELVVRGpsvmkgyWNNPEATAavdedGWYRTGDLGRLDEDG---- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 299 spYPRIgtlIGRTDDMVKVKGVNIFPSQIEELLSSIEGAsSEYQVM-VDHLMGKDVLTLFVETNPSINkyALEIEIQNQF 377
Cdd:cd04433  237 --YLYI---VGRLKDMIKSGGENVYPAEVEAVLLGHPGV-AEAAVVgVPDPEWGERVVAVVVLRPGAD--LDAEELRAHV 308

                        330       340
                 ....*....|....*....|..
gi 488630032 378 KGRIGLTPVVK-LVELGELPRS 398
Cdd:cd04433  309 RERLAPYKVPRrVVFVDALPRT 330
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 76-398 2.50e-20

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: 92.57  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDVDDWALMFARCYemaGITNLDRI-QITP---GYGlWTAGIgfqLGAERLGAMTVPMGPGNTDK 151
Cdd:COG0318  108 TSGTTGRPKGVMLTHRNLLANAAAIAAAL---GLTPGDVVlVALPlfhVFG-LTVGL---LAPLLAGATLVLLPRFDPER 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 152 QLRMMMDMKSTVLCATSS--YALLLAEEIAKRGIGeriHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGI 229
Cdd:COG0318  181 VLELIERERVTVLFGVPTmlARLLRHPEFARYDLS---SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET-SPVV 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 230 AINcekqgAMHYWDDYIY----------IEIVDPrTGEVLPDGEVGEIVI---------TTLKKEGAPLIR---YRTHDL 287
Cdd:COG0318  257 TVN-----PEDPGERRPGsvgrplpgveVRIVDE-DGRELPPGEVGEIVVrgpnvmkgyWNDPEATAEAFRdgwLRTGDL 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 288 SRIVP-GDCpcgspyprigTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASseyQVMV----DHLMGkDVLTLFVETNP 362
Cdd:COG0318  331 GRLDEdGYL----------YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA---EAAVvgvpDEKWG-ERVVAFVVLRP 396

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 488630032 363 SINkyALEIEIQNQFKGRIGLTPVVKLVE-LGELPRS 398
Cdd:COG0318  397 GAE--LDAEELRAFLRERLARYKVPRRVEfVDELPRT 431
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 76-398 1.84e-13

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: 71.72  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDvddwALMFAR--CYEMAGITNLDRIQITP----GYGLwTAGIGFQLGAerlGAMTVPM-GPGN 148
Cdd:cd05919   99 SSGTTGPPKGVMHAHRD----PLLFADamAREALGLTPGDRVFSSAkmffGYGL-GNSLWFPLAV---GASAVLNpGWPT 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 149 TDKQLRMMMDMKSTVLCATSS-YALLLAEEIAKRGIGERIHLkkGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVygp 227
Cdd:cd05919  171 AERVLATLARFRPTVLYGVPTfYANLLDSCAGSPDALRSLRL--CVSAGEALPRGLGERWMEHFGGPILDGIGATEV--- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 228 GIAINCEKQGAMHY--------WDDyiyIEIVDPrTGEVLPDGEVGEIVIttlKKEGAPLIRYRTHDLSR-------IVP 292
Cdd:cd05919  246 GHIFLSNRPGAWRLgstgrpvpGYE---IRLVDE-EGHTIPPGEEGDLLV---RGPSAAVGYWNNPEKSRatfnggwYRT 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 293 GDCPC----GSPYPRigtliGRTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLF-VETNPSINKY 367
Cdd:cd05919  319 GDKFCrdadGWYTHA-----GRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFvVLKSPAAPQE 393

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488630032 368 ALEIEIQNQFKGRIGLTPVVKLVE-LGELPRS 398
Cdd:cd05919  394 SLARDIHRHLLERLSAHKVPRRIAfVDELPRT 425
AMP-binding pfam00501
AMP-binding enzyme;
5-318 4.26e-13

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 70.42  E-value: 4.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032    5 ESQFLLIKEQLKKLTAKECFYKHKlEGVNVNQIQSQEDFEKLPFTWKGDLREAYPLGLMAAPEEKIVRIHSSSGTTGTPV 84
Cdd:pfam00501  93 GAKVLITDDALKLEELLEALGKLE-VVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPK 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   85 IIPYTQKD-VDDWALMFARCYEMAGITNLDRIQITPGYGlWTAG-IGFQLGAERLGAMTVPMGPGNTDKQLRMMMDMKS- 161
Cdd:pfam00501 172 GVMLTHRNlVANVLSIKRVRPRGFGLGPDDRVLSTLPLF-HDFGlSLGLLGPLLAGATVVLPPGFPALDPAALLELIERy 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  162 --TVLCATSS-YALLLAEEIAKRGIgeRIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAINCEKQGA 238
Cdd:pfam00501 251 kvTVLYGVPTlLNMLLEAGAPKRAL--LSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTET-TGVVTTPLPLDED 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  239 MHY--------WDDYIYIeiVDPRTGEVLPDGEVGEIVI-----------------TTLKKEGAplirYRTHDLSRIVPg 293
Cdd:pfam00501 328 LRSlgsvgrplPGTEVKI--VDDETGEPVPPGEPGELCVrgpgvmkgylndpeltaEAFDEDGW----YRTGDLGRRDE- 400

                         330       340
                  ....*....|....*....|....*..
gi 488630032  294 DcpcgspypriGTL--IGRTDDMVKVK 318
Cdd:pfam00501 401 D----------GYLeiVGRKKDQIKLG 417
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 67-331 1.12e-12

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: 69.29  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  67 EEKIVRIHSSSGTTGTPVIIPYTQKdvddwaLMFARCYEMAGITNLDRIQI-----TPG--YGLWTAGIGFQLgaerLGA 139
Cdd:cd05972   80 AEDPALIYFTSGTTGLPKGVLHTHS------YPLGHIPTAAYWLGLRPDDIhwniaDPGwaKGAWSSFFGPWL----LGA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 140 MTV--PMGPGNTDKQLRMMMDMKSTVLCAT-SSYALLLAEEIAKRgigERIHLKKGVIGSERWGEKMRNRIAAELGVDLF 216
Cdd:cd05972  150 TVFvyEGPRFDAERILELLERYGVTSFCGPpTAYRMLIKQDLSSY---KFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 217 DIYGLTEVygpGIAI-NCE----KQGAMHYWDDYIYIEIVDpRTGEVLPDGEVGEIVITTL-----------KKEGAPLI 280
Cdd:cd05972  227 DGYGQTET---GLTVgNFPdmpvKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPppglflgyvgdPEKTEASI 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488630032 281 R---YRTHDLSRIVPGdcpcGSPYprigtLIGRTDDMVKVKGVNIFPSQIEELL 331
Cdd:cd05972  303 RgdyYLTGDRAYRDED----GYFW-----FVGRADDIIKSSGYRIGPFEVESAL 347
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 77-336 3.16e-10

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: 61.39  E-value: 3.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  77 SGTTGTP--VIIPYtqkdvddwalmfarcyemAGITNL-----DRIQITPGYG-LWTAGIGFQLGAERL------GAMTV 142
Cdd:cd05930  102 SGSTGKPkgVMVEH------------------RGLVNLllwmqEAYPLTPGDRvLQFTSFSFDVSVWEIfgallaGATLV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 143 PMGPG---NTDKQLRMMMDMKSTVLCATSSYALLLAEEIAKRGIGeriHLKKGVIGserwGEKMRNRIAAEL-----GVD 214
Cdd:cd05930  164 VLPEEvrkDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALP---SLRLVLVG----GEALPPDLVRRWrellpGAR 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 215 LFDIYGLTEVygpGIAINCEKQGAMHYWDDYI---------YIEIVDPRtGEVLPDGEVGEIVITT-------LKKEG-- 276
Cdd:cd05930  237 LVNLYGPTEA---TVDATYYRVPPDDEEDGRVpigrpipntRVYVLDEN-LRPVPPGVPGELYIGGaglargyLNRPElt 312

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488630032 277 ---------APLIR-YRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:cd05930  313 aerfvpnpfGPGERmYRTGDLVRWLPD-----------GNLefLGRIDDQVKIRGYRIELGEIEAALLAHPG 373
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
76-397 5.85e-10

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 60.90  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDVDDWALMFARCyeMAGITNLDRIqitpgygLWTAGIGF-------QLGAERLGAMTV-----P 143
Cdd:COG0365  192 TSGTTGKPKGVVHTHGGYLVHAATTAKY--VLDLKPGDVF-------WCTADIGWatghsyiVYGPLLNGATVVlyegrP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 144 MGPgNTDKQLRMMMDMKSTVLCAT-SSYALLLAEEIAKRGIGERIHLKkgVIGS--ERWGEKMRNRIAAELGVDLFDIYG 220
Cdd:COG0365  263 DFP-DPGRLWELIEKYGVTVFFTApTAIRALMKAGDEPLKKYDLSSLR--LLGSagEPLNPEVWEWWYEAVGVPIVDGWG 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 221 LTEVYG------PGIAInceKQGAMHY----WDdyiyIEIVDPrTGEVLPDGEVGEIVIttlkKEGAP--LIRY-----R 283
Cdd:COG0365  340 QTETGGifisnlPGLPV---KPGSMGKpvpgYD----VAVVDE-DGNPVPPGEEGELVI----KGPWPgmFRGYwndpeR 407

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 284 THD--LSRI----VPGDcpcgspYPRI---G--TLIGRTDDMVKVKGVNIFPSQIEELLSSIEGasseyqVM------VD 346
Cdd:COG0365  408 YREtyFGRFpgwyRTGD------GARRdedGyfWILGRSDDVINVSGHRIGTAEIESALVSHPA------VAeaavvgVP 475

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488630032 347 HLMGKDVLTLFVETNPSINKY-ALEIEIQNQFKGRIGltPVV---KLVELGELPR 397
Cdd:COG0365  476 DEIRGQVVKAFVVLKPGVEPSdELAKELQAHVREELG--PYAyprEIEFVDELPK 528
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 76-398 9.37e-10

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: 60.08  E-value: 9.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDVDDWALMFARcyEMAGITNLDRIQITP----GYGLWTAGIgFQLGAerlGAMTVPMGPGNT-D 150
Cdd:cd05959  171 SSGSTGRPKGVVHLHADIYWTAELYAR--NVLGIREDDVCFSAAklffAYGLGNSLT-FPLSV---GATTVLMPERPTpA 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 151 KQLRMMMDMKSTVLCATSS-YALLLAEEIAKRGIGERIHLkkGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEVygpgI 229
Cdd:cd05959  245 AVFKRIRRYRPTVFFGVPTlYAAMLAAPNLPSRDLSSLRL--CVSAGEALPAEVGERWKARFGLDILDGIGSTEM----L 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 230 AINCE-KQGAMHYW------DDYiYIEIVDPRTGEVlPDGEVGEIVIttlkKEGAPLIRY--RTHDLSRIVPGdcpcgsP 300
Cdd:cd05959  319 HIFLSnRPGRVRYGttgkpvPGY-EVELRDEDGGDV-ADGEPGELYV----RGPSSATMYwnNRDKTRDTFQG------E 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 301 YPRIG-----------TLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKY-A 368
Cdd:cd05959  387 WTRTGdkyvrdddgfyTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSeA 466

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488630032 369 LEIEIQNQFKGRIGLTPVVKLVE-LGELPRS 398
Cdd:cd05959  467 LEEELKEFVKDRLAPYKYPRWIVfVDELPKT 497
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 77-336 4.62e-09

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 58.27  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  77 SGTTGTP--VIIPYTQKdvddWALMFARCYEMaGITNLDR-IQITPGY--GLWTAGI-GFQLGAErlgamTVPMGPGNTD 150
Cdd:PRK06187 176 SGTTGHPkgVVLSHRNL----FLHSLAVCAWL-KLSRDDVyLVIVPMFhvHAWGLPYlALMAGAK-----QVIPRRFDPE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 151 KQLRMMMDMKSTVLCA--TSSYALLLAEEIAKRGIGeriHLKKGVIGS--------ERWGEKmrnriaaeLGVDLFDIYG 220
Cdd:PRK06187 246 NLLDLIETERVTFFFAvpTIWQMLLKAPRAYFVDFS---SLRLVIYGGaalppallREFKEK--------FGIDLVQGYG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 221 LTEVyGPGIAINCEKQGAMHYWDDYI---------YIEIVDPRtGEVLP--DGEVGEIVITT---------LKKEGAPLI 280
Cdd:PRK06187 315 MTET-SPVVSVLPPEDQLPGQWTKRRsagrplpgvEARIVDDD-GDELPpdGGEVGEIIVRGpwlmqgywnRPEATAETI 392

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488630032 281 R---YRTHDLSRIvpgdcpcgSPYPRIgTLIGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:PRK06187 393 DggwLHTGDVGYI--------DEDGYL-YITDRIKDVIISGGENIYPRELEDALYGHPA 442
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 76-399 3.55e-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: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 55.13  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQKDVDDWALMFARCYEMAgiTNLDRIQITPGYGLWTAGIGFQLGAERLGAMTV---PMGPGNTDKQ 152
Cdd:cd05971   96 TSGTTGPPKGALHAHRVLLGHLPGVQFPFNLF--PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVlahRMTKFDPKAA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 153 LRMMMDMKSTVLCATSSyALLLAEEIAKRGIGERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTE---VYGPGI 229
Cdd:cd05971  174 LDLMSRYGVTTAFLPPT-ALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTEcnlVIGNCS 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 230 AINCEKQGAM------HYwddyiyIEIVDPRtGEVLPDGEVGEIVITTlkKEGAPLIRYRTHDLSRIVPgdcPCGSpYPR 303
Cdd:cd05971  253 ALFPIKPGSMgkpipgHR------VAIVDDN-GTPLPPGEVGEIAVEL--PDPVAFLGYWNNPSATEKK---MAGD-WLL 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 304 IGTL-----------IGRTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINKY-ALEI 371
Cdd:cd05971  320 TGDLgrkdsdgyfwyVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdALAR 399

                        330       340
                 ....*....|....*....|....*....
gi 488630032 372 EIQNQFKGRIGLTPVVKLVE-LGELPRSE 399
Cdd:cd05971  400 EIQELVKTRLAAHEYPREIEfVNELPRTA 428
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 248-332 7.78e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 54.28  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDPRTGEVLPDGEVGEIVITT---LK------KEGAPLIR---YRTHDLSRIVPGdcpcgspypriGTL--IGRTDD 313
Cdd:PRK06178 398 FKICDFETGELLPLGAEGEIVVRTpslLKgywnkpEATAEALRdgwLHTGDIGKIDEQ-----------GFLhyLGRRKE 466

                         90
                 ....*....|....*....
gi 488630032 314 MVKVKGVNIFPSQIEELLS 332
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLG 485
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 212-333 4.24e-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. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 51.91  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 212 GVDLFDIYGLTEVYGPGIAINCEKQGAMH--YWDDYIYIEIVDPRTGEVlPDGEVGEIVITTLK------------KEGA 277
Cdd:cd05934  219 GVRLLEGYGMTETIVGVIGPRDEPRRPGSigRPAPGYEVRIVDDDGQEL-PAGEPGELVIRGLRgwgffkgyynmpEATA 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488630032 278 PLIR---YRTHDLSRIVPGdcpcGSPYprigtLIGRTDDMVKVKGVNIFPSQIEELLSS 333
Cdd:cd05934  298 EAMRngwFHTGDLGYRDAD----GFFY-----FVDRKKDMIRRRGENISSAEVERAILR 347
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 189-336 4.43e-07

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: 51.84  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 189 LKKGVIGserwGEKMRNRIAAEL---GVDLFDIYGLTEVyGPGIAINC-----EKQGAMHYWDDYIYIEIVDPRTGEVlP 260
Cdd:cd17631  215 LRAVIYG----GAPMPERLLRALqarGVKFVQGYGMTET-SPGVTFLSpedhrRKLGSAGRPVFFVEVRIVDPDGREV-P 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 261 DGEVGEIVITTLK---------KEGAPLIR---YRTHDLSRIvPGDcpcgspypriG--TLIGRTDDMVKVKGVNIFPSQ 326
Cdd:cd17631  289 PGEVGEIVVRGPHvmagywnrpEATAAAFRdgwFHTGDLGRL-DED----------GylYIVDRKKDMIISGGENVYPAE 357

                        170
                 ....*....|
gi 488630032 327 IEELLSSIEG 336
Cdd:cd17631  358 VEDVLYEHPA 367
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 256-409 7.89e-07

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 51.24  E-value: 7.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 256 GEVLPDGEVGEIVIttlKKEGAPLIRYRTHDLSR--------IVPGDcpcgspyprIGTL--------IGRTDDMVKVKG 319
Cdd:PRK12406 342 GRPLPQGEIGEIYS---RIAGNPDFTYHNKPEKRaeidrggfITSGD---------VGYLdadgylflCDRKRDMVISGG 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 320 VNIFPSQIEELLSSIEG---------ASSEYqvmvdhlmgKDVLTLFVETNPSInkyALEIE-IQNQFKGRIGLTPVVKL 389
Cdd:PRK12406 410 VNIYPAEIEAVLHAVPGvhdcavfgiPDAEF---------GEALMAVVEPQPGA---TLDEAdIRAQLKARLAGYKVPKH 477

                        170       180
                 ....*....|....*....|.
gi 488630032 390 VEL-GELPRSEkkSTRVFDNR 409
Cdd:PRK12406 478 IEImAELPRED--SGKIFKRR 496
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 68-398 8.14e-07

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: 50.94  E-value: 8.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  68 EKIVRIHSSSGTTGTPVIIPYTQKDVDDWALMFARCYemaGITNLDRIQITPGYGLWTAGIGFQLGAERLGAMTVPMGPG 147
Cdd:cd05935   84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWT---GLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 148 NTDKQLRMMMDMKSTVLCATSSyalLLAEEIAKRGIGERIHLKKGVIGSERW------GEKMRNRIaaelGVDLFDIYGL 221
Cdd:cd05935  161 DRETALELIEKYKVTFWTNIPT---MLVDLLATPEFKTRDLSSLKVLTGGGApmppavAEKLLKLT----GLRFVEGYGL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 222 TEV-----YGPGIAINCEKQGAMHYWDDyiyIEIVDPRTGEVLPDGEVGEIVITtlkkegAPLI------RYRTHDLSRI 290
Cdd:cd05935  234 TETmsqthTNPPLRPKLQCLGIP*FGVD---ARVIDIETGRELPPNEVGEIVVR------GPQIfkgywnRPEETEESFI 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 291 VPGdcpcGSPYPRIGTL-----------IGRTDDMVKVKGVNIFPSQIEELLSSIEgASSEYQVMV--DHLMGKDVLTLF 357
Cdd:cd05935  305 EIK----GRRFFRTGDLgymdeegyfffVDRVKRMINVSGFKVWPAEVEAKLYKHP-AI*EVCVISvpDERVGEEVKAFI 379

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 488630032 358 VeTNPSINKYALEIEIQNQFKGRIGLTPVVKLVEL-GELPRS 398
Cdd:cd05935  380 V-LRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFvDELPRS 420
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 76-331 1.38e-06

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: 50.40  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTPVIIPYTQkdvDDWALMFARCYEMAGITNLDR----IQITPGYGLWTAGIgfqLGAERLGAMTVPMGPGNTDK 151
Cdd:cd05920  147 SGGTTGTPKLIPRTH---NDYAYNVRASAEVCGLDQDTVylavLPAAHNFPLACPGV---LGTLLAGGRVVLAPDPSPDA 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 152 QLRMMMDMKSTVLCATSSYALLLAEEIAKRGIGERiHLKKGVIGSERWGEKMRNRIAAELGVDLFDIYGLTEvyG----- 226
Cdd:cd05920  221 AFPLIEREGVTVTALVPALVSLWLDAAASRRADLS-SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--Gllnyt 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 227 ----PGIAInCEKQGAMHYWDDyiYIEIVDPRTGEVlPDGEVGEivittLKKEGAPLIR------------------YRT 284
Cdd:cd05920  298 rlddPDEVI-IHTQGRPMSPDD--EIRVVDEEGNPV-PPGEEGE-----LLTRGPYTIRgyyrapehnaraftpdgfYRT 368

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488630032 285 HDLSRIVPGdcpcgspypriGTLI--GRTDDMVKVKGVNIFPSQIEELL 331
Cdd:cd05920  369 GDLVRRTPD-----------GYLVveGRIKDQINRGGEKIAAEEVENLL 406
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 248-328 1.94e-06

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: 49.93  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDPRTGEVLPDGEVGEIVI------------------TTLKKEGAPLIRY-RTHDLSRIVPGD---Cpcgspyprig 305
Cdd:cd05931  366 VRIVDPETGRELPDGEVGEIWVrgpsvasgywgrpeataeTFGALAATDEGGWlRTGDLGFLHDGElyiT---------- 435

                         90       100
                 ....*....|....*....|...
gi 488630032 306 tliGRTDDMVKVKGVNIFPSQIE 328
Cdd:cd05931  436 ---GRLKDLIIVRGRNHYPQDIE 455
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 77-331 3.74e-06

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: 48.81  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  77 SGTTGTP--VIIPYtqkdvddwalmfarcyemAGITN-----LDRIQITPG-YGLWTAGIGF------QLGAERLGAMTV 142
Cdd:cd17646  147 SGSTGRPkgVMVTH------------------AGIVNrllwmQDEYPLGPGdRVLQKTPLSFdvsvweLFWPLVAGARLV 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 143 ---PMGPGNTDKQLRMMMDMKSTVLCATSSyalLLAEEIAKRGIGERIHLKKGVIGSERWGEKMRNRIAAELGVDLFDIY 219
Cdd:cd17646  209 varPGGHRDPAYLAALIREHGVTTCHFVPS---MLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLY 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 220 GLTEV-------------YGPGIAINCEKQGAMHYwddyiyieIVDPRtGEVLPDGEVGEIVITtlkkeGAPLIR----- 281
Cdd:cd17646  286 GPTEAaidvthwpvrgpaETPSVPIGRPVPNTRLY--------VLDDA-LRPVPVGVPGELYLG-----GVQLARgylgr 351

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488630032 282 -------------------YRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMVKVKGVNIFPSQIEELL 331
Cdd:cd17646  352 paltaerfvpdpfgpgsrmYRTGDLARWRPD-----------GALefLGRSDDQVKIRGFRVEPGEIEAAL 411
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 200-336 3.80e-06

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: 48.85  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 200 GEKMRNRIAAEL-----GVDLFDIYGLTE--VYGPGIAINCEKQGAmhywddyIYI---------EIVDpRTGEVLPDGE 263
Cdd:cd12115  222 GEPLPRDLVQRLyarlqVERVVNLYGPSEdtTYSTVAPVPPGASGE-------VSIgrplantqaYVLD-RALQPVPLGV 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 264 VGEIVIT--------------TLKK-----EGAPLIRYRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMVKVKGVNI 322
Cdd:cd12115  294 PGELYIGgagvargylgrpglTAERflpdpFGPGARLYRTGDLVRWRPD-----------GLLefLGRADNQVKVRGFRI 362

                        170
                 ....*....|....
gi 488630032 323 FPSQIEELLSSIEG 336
Cdd:cd12115  363 ELGEIEAALRSIPG 376
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 208-269 4.31e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 48.79  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 208 AAELGVDLFDIYGLTEVYGPgiAINCEKQGAmhyWDD----------------YIYIE---IVDPRTGEVLP-DGE-VGE 266
Cdd:PRK08162 316 MEEIGFDLTHVYGLTETYGP--ATVCAWQPE---WDAlplderaqlkarqgvrYPLQEgvtVLDPDTMQPVPaDGEtIGE 390


                 ...
gi 488630032 267 IVI 269
Cdd:PRK08162 391 IMF 393
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 58-269 1.14e-05

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: 47.29  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  58 YPLGLMAAPEEKIVRIHSSSGTTGTPVIIPYTQKDvddwalmfarCYEMAGITNLD-RIQITPGYgLWT------AGIGF 130
Cdd:cd12118  123 DFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRG----------AYLNALANILEwEMKQHPVY-LWTlpmfhcNGWCF 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 131 QLGAERLGAMTVPMGPGNTDKQLRMMMDMKSTVLCA--TSSYALLLAEEIAKRGIGERIH-LKKGVIGSERWGEKMrnri 207
Cdd:cd12118  192 PWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGapTVLNMLANAPPSDARPLPHRVHvMTAGAPPPAAVLAKM---- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 208 aAELGVDLFDIYGLTEVYGPGIAinCEKQGAmhyWD----------------DYIY---IEIVDPRTGEVLP-DGE-VGE 266
Cdd:cd12118  268 -EELGFDVTHVYGLTETYGPATV--CAWKPE---WDelpteerarlkarqgvRYVGleeVDVLDPETMKPVPrDGKtIGE 341


                 ...
gi 488630032 267 IVI 269
Cdd:cd12118  342 IVF 344
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 49-398 2.07e-05

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: 46.40  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  49 TWKGDLREAYPLGLMAAP-EEKIVRIHSSSGTTGTPVIIPYTQKDvddwalMFARCYEMAGITNLDR------IQITP-- 119
Cdd:cd05936  105 SFTDLLAAGAPLGERVALtPEDVAVLQYTSGTTGVPKGAMLTHRN------LVANALQIKAWLEDLLegddvvLAALPlf 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 120 -GYGLWTAG-IGFQLGAerlgamTVPMGPGNTDKQ-LRMMMDMKSTVLCA--TSSYALLLAEEIAKRGIGeriHLKKGVI 194
Cdd:cd05936  179 hVFGLTVALlLPLALGA------TIVLIPRFRPIGvLKEIRKHRVTIFPGvpTMYIALLNAPEFKKRDFS---SLRLCIS 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 195 GSERWGEKMRNRIAAELGVDLFDIYGLTEVyGPGIAIN----CEKQGAMHY--WDdyIYIEIVDPRtGEVLPDGEVGEIV 268
Cdd:cd05936  250 GGAPLPVEVAERFEELTGVPIVEGYGLTET-SPVVAVNpldgPRKPGSIGIplPG--TEVKIVDDD-GEELPPGEVGELW 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 269 IT---------TLKKEGAPLIR---YRTHDLSRIVPgdcpcgSPYPRIgtlIGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:cd05936  326 VRgpqvmkgywNRPEETAEAFVdgwLRTGDIGYMDE------DGYFFI---VDRKKDMIIVGGFNVYPREVEEVLYEHPA 396

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488630032 337 ASSEYQVMVDHLMGKDVLTLFVETNPsiNKYALEIEIQNQFKGRIGLTPVVKLVE-LGELPRS 398
Cdd:cd05936  397 VAEAAVVGVPDPYSGEAVKAFVVLKE--GASLTEEEIIAFCREQLAGYKVPRQVEfRDELPKS 457
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 66-378 2.20e-05

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: 46.56  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  66 PEEKIVRIHSSsGTTGTPVIIPYTQKDV---DDWALMFARCyemagITNLDRIQITP---GYGLwTAGIGFQLgaerLGA 139
Cdd:cd05909  146 PDDPAVILFTS-GSEGLPKGVVLSHKNLlanVEQITAIFDP-----NPEDVVFGALPffhSFGL-TGCLWLPL----LSG 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 140 MTVPMGPGNTD-KQL-RMMMDMKSTVLCATSSYAlllaeeiakRGIGERIH------LKKGVIGSERWGEKMRNRIAAEL 211
Cdd:cd05909  215 IKVVFHPNPLDyKKIpELIYDKKATILLGTPTFL---------RGYARAAHpedfssLRLVVAGAEKLKDTLRQEFQEKF 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 212 GVDLFDIYGLTEVyGPGIAINC----EKQGAMHYWDDYIYIEIVDPRTGEVLPDGEVGEIVIT---------TLKKEGAP 278
Cdd:cd05909  286 GIRILEGYGTTEC-SPVISVNTpqspNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRgpnvmlgylNEPELTSF 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 279 LIR---YRTHDLSRIVP-GDCpcgspyprigTLIGRTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQV--MVDHLMGKD 352
Cdd:cd05909  365 AFGdgwYDTGDIGKIDGeGFL----------TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVvsVPDGRKGEK 434

                        330       340
                 ....*....|....*....|....*....
gi 488630032 353 VLTLFVETNP---SINKYALEIEIQNQFK 378
Cdd:cd05909  435 IVLLTTTTDTdpsSLNDILKNAGISNLAK 463
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 248-398 4.36e-05

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: 45.32  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDpRTGEVLPDGEVGEIVIT------------------TLKKEGAPliRYRTHDLSRIVPGdcpcgspypriGTLI- 308
Cdd:cd05945  283 LVILD-EDGRPVPPGEKGELVISgpsvskgylnnpektaaaFFPDEGQR--AYRTGDLVRLEAD-----------GLLFy 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 309 -GRTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSINkYALEIEIQNQFKGRI--GLTP 385
Cdd:cd05945  349 rGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE-AGLTKAIKAELAERLppYMIP 427

                        170
                 ....*....|...
gi 488630032 386 vVKLVELGELPRS 398
Cdd:cd05945  428 -RRFVYLDELPLN 439
PRK12316 PRK12316
peptide synthase; Provisional
 76-336 4.60e-05

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 46.10  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032   76 SSGTTGTPVIIPYTQKDVDDWALMFARCYemaGITNLDRIqitpgygLWTAGIGFQLGAERL------GAMTVPMGPGNT 149
Cdd:PRK12316 3204 TSGSTGKPKGVGIRHSALSNHLCWMQQAY---GLGVGDRV-------LQFTTFSFDVFVEELfwplmsGARVVLAGPEDW 3273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  150 DKQLRMMMDMKSTVLCATSSYALLLAEEIAKRGIGERIHLKKGVIGSERWGEKMRNRIAAelGVDLFDIYGLTEVYGPGI 229
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVT 3351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  230 AINCEKQGamhywDDYIYIEIVDPRTGEVLPDGE-----VGEIVITTLKKEGAPLIRYRTHDLS--RIVPGDCPCGSPYP 302
Cdd:PRK12316 3352 HWQCVEEG-----KDAVPIGRPIANRACYILDGSlepvpVGALGELYLGGEGLARGYHNRPGLTaeRFVPDPFVPGERLY 3426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 488630032  303 RIGTL-----------IGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:PRK12316 3427 RTGDLaryradgvieyIGRVDHQVKIRGFRIELGEIEARLLEHPW 3471
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 76-333 4.63e-05

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: 45.30  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032  76 SSGTTGTP--VIIPY------TQKDVDDWALMFarCYEMAGITNLDRIQItpgYGLwtagIGFQLGAERLGAMTVPMGPG 147
Cdd:cd05904  166 SSGTTGRSkgVMLTHrnliamVAQFVAGEGSNS--DSEDVFLCVLPMFHI---YGL----SSFALGLLRLGATVVVMPRF 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 148 NTDKQLRMMMDMKSTVLcaTSSYALLLAeeIAKRGIGERIHLK--KGVI-GSERWGEKMRNRIAAEL-GVDLFDIYGLTE 223
Cdd:cd05904  237 DLEELLAAIERYKVTHL--PVVPPIVLA--LVKSPIVDKYDLSslRQIMsGAAPLGKELIEAFRAKFpNVDLGQGYGMTE 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 224 VYGPGIAINCEKQGAMHY---------WDdyiyIEIVDPRTGEVLPDGEVGEIVI-----------------TTLKKEGA 277
Cdd:cd05904  313 STGVVAMCFAPEKDRAKYgsvgrlvpnVE----AKIVDPETGESLPPNQTGELWIrgpsimkgylnnpeataATIDKEGW 388

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488630032 278 plirYRTHDLSRIvPGDcpcgspypriGTL--IGRTDDMVKVKGVNIFPSQIEELLSS 333
Cdd:cd05904  389 ----LHTGDLCYI-DED----------GYLfiVDRLKELIKYKGFQVAPAELEALLLS 431
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 217-332 6.63e-05

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: 44.81  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 217 DIYGLTEVYGPGIAINCEKQGAMHY-WDDYIYIEIVDPRTGEVLPDGEVGEIVIT----------------TLKK--EGa 277
Cdd:cd05923  297 NIYGTTEAMNSLYMRDARTGTEMRPgFFSEVRIVRIGGSPDEALANGEEGELIVAaaadaaftgylnqpeaTAKKlqDG- 375

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488630032 278 pliRYRThdlsrivpGDCPCGSPYPRIgTLIGRTDDMVKVKGVNIFPSQIEELLS 332
Cdd:cd05923  376 ---WYRT--------GDVGYVDPSGDV-RILGRVDDMIISGGENIHPSEIERVLS 418
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 250-336 1.07e-04

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: 44.11  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 250 IVDpRTGEVLPDGEVGEIVIT------------TLKKE---------GAPLirYRTHDLSRIVPGdcpcgspypriGTL- 307
Cdd:cd12117  319 VLD-EDGRPVPPGVPGELYVGgdglalgylnrpALTAErfvadpfgpGERL--YRTGDLARWLPD-----------GRLe 384

                         90       100       110
                 ....*....|....*....|....*....|
gi 488630032 308 -IGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:cd12117  385 fLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 193-336 1.99e-04

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: 43.49  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 193 VIGSER--WGEKMRNRIAAELGVDLFDIYGLTEVYgpgIAINCEKQGAMHYWDDYIYI---------EIVDPRtGEVLPD 261
Cdd:cd17651  259 LTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTETH---VVTALSLPGDPAAWPAPPPIgrpidntrvYVLDAA-LRPVPP 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 262 GEVGEIVITtlkkeGAPLIR------------------------YRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMV 315
Cdd:cd17651  335 GVPGELYIG-----GAGLARgylnrpeltaerfvpdpfvpgarmYRTGDLARWLPD-----------GELefLGRADDQV 398

                        170       180
                 ....*....|....*....|.
gi 488630032 316 KVKGVNIFPSQIEELLSSIEG 336
Cdd:cd17651  399 KIRGFRIELGEIEAALARHPG 419
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 250-269 2.64e-04

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 43.02  E-value: 2.64e-04
                         10        20
                 ....*....|....*....|
gi 488630032 250 IVDPRTGEVLPDGEVGEIVI 269
Cdd:PRK08314 370 VIDPETLEELPPGEVGEIVV 389
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 306-336 2.83e-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: 42.39  E-value: 2.83e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488630032 306 TLIGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:cd17633  225 YLVGRESDMIIIGGINIFPTEIESVLKAIPG 255
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 248-399 3.50e-04

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: 42.65  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDPrTGEVLPDGEVGEIVITtlkkeGAPLIR------------------YRTHDLSRIVPGDCpcgspyprigTLIG 309
Cdd:cd05906  365 MRIVDD-EGQLLPEGEVGRLQVR-----GPVVTKgyynnpeanaeaftedgwFRTGDLGFLDNGNL----------TITG 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 310 RTDDMVKVKGVNIFPSQIEELLSSIEGASSEYQVMVDHL---MGKDVLTLF--VETNPSINKYALEIEIQNQFKGRIGLT 384
Cdd:cd05906  429 RTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRdpgAETEELAIFfvPEYDLQDALSETLRAIRSVVSREVGVS 508

                        170
                 ....*....|....*..
gi 488630032 385 P--VVKLvELGELPRSE 399
Cdd:cd05906  509 PayLIPL-PKEEIPKTS 524
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 166-269 5.73e-04

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 42.05  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 166 ATSSYAL------LLAEEI--AKRGIGERIHLKKGVigSERWGEKMRNRiaaeLGVDLFDIYGLTEVYGP-GIAINCEKQ 236
Cdd:PRK06155 269 ATVTYLLgamvsiLLSQPAreSDRAHRVRVALGPGV--PAALHAAFRER----FGVDLLDGYGSTETNFViAVTHGSQRP 342

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488630032 237 GAMHYWDDYIYIEIVDpRTGEVLPDGEVGEIVI 269
Cdd:PRK06155 343 GSMGRLAPGFEARVVD-EHDQELPDGEPGELLL 374
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
248-398 7.77e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 41.38  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDPRTGEVlPDGEVGEIVIT---------TLKKEGAPLIR---YRTHDLSRIvpgdcpcgsPYPRIGTLIGRTDDMV 315
Cdd:PRK06839 328 YELIDENKNKV-EVGEVGELLIRgpnvmkeywNRPDATEETIQdgwLCTGDLARV---------DEDGFVYIVGRKKEMI 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 316 KVKGVNIFPSQIEELLSSIEGASSEYQVMVDHLMGKDVLTLFVETNPSinKYALEIEIQNQFKGRIGLTPVVK-LVELGE 394
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS--SVLIEKDVIEHCRLFLAKYKIPKeIVFLKE 475


                 ....
gi 488630032 395 LPRS 398
Cdd:PRK06839 476 LPKN 479
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 200-364 1.53e-03

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: 40.50  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 200 GEKMRNRIAAEL-----GVDLFDIYGLTEVY------------------GPGIAiNCEkqgamhywddyiyIEIVDPRtG 256
Cdd:cd05922  240 GGRLPQETIARLrellpGAQVYVMYGQTEATrrmtylpperilekpgsiGLAIP-GGE-------------FEILDDD-G 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 257 EVLPDGEVGEIVIT-------------TLKKEGAPLIRYRTHDLSRI-VPGDCpcgspyprigTLIGRTDDMVKVKGVNI 322
Cdd:cd05922  305 TPTPPGEPGEIVHRgpnvmkgywndppYRRKEGRGGGVLHTGDLARRdEDGFL----------FIVGRRDRMIKLFGNRI 374

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488630032 323 FPSQIEELLSSIeGASSEYQVMVDHLMGKDVLTLFVETNPSI 364
Cdd:cd05922  375 SPTEIEAAARSI-GLIIEAAAVGLPDPLGEKLALFVTAPDKI 415
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 153-336 1.99e-03

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: 40.37  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 153 LRMMMDMKSTVLCATSS--YALLLAEEiakRGIGERIHLKKGVIGSE--------RWGEKMRNRiaaelGVDLFDIYGLT 222
Cdd:cd17643  177 ARLLRDEGVTVLNQTPSafYQLVEAAD---RDGRDPLALRYVIFGGEaleaamlrPWAGRFGLD-----RPQLVNMYGIT 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 223 EV------------YGPGIA---INCEKQGAMHYwddyiyieIVDPRtGEVLPDGEVGEIVI------------------ 269
Cdd:cd17643  249 ETtvhvtfrpldaaDLPAAAaspIGRPLPGLRVY--------VLDAD-GRPVPPGVVGELYVsgagvargylgrpeltae 319

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488630032 270 --TTLKKEGAPLIRYRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:cd17643  320 rfVANPFGGPGSRMYRTGDLARRLPD-----------GELeyLGRADEQVKIRGFRIELGEIEAALATHPS 379
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 273-350 3.70e-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: 39.31  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 273 KKEGAPLIRYRTHDLSRIVPGdcpcgspypriGTL--IGRTDDMVKVKGVNIFPSQIEELLSSI-----------EGASS 339
Cdd:cd17648  323 RARGRNARLYKTGDLVRWLPS-----------GELeyLGRNDFQVKIRGQRIEPGEVEAALASYpgvrecavvakEDASQ 391

                         90
                 ....*....|.
gi 488630032 340 EYQVMVDHLMG 350
Cdd:cd17648  392 AQSRIQKYLVG 402
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 248-336 4.28e-03

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 39.36  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488630032 248 IEIVDPrTGEVLPDGEVGEIVIT-----------------TLKKEGAplirYRTHDLSRIVPGDcpcgspYPRIgtlIGR 310
Cdd:PRK05677 389 CKVIDD-DGNELPLGEVGELCVKgpqvmkgywqrpeatdeILDSDGW----LKTGDIALIQEDG------YMRI---VDR 454

                         90       100
                 ....*....|....*....|....*.
gi 488630032 311 TDDMVKVKGVNIFPSQIEELLSSIEG 336
Cdd:PRK05677 455 KKDMILVSGFNVYPNELEDVLAALPG 480
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 49-99 7.16e-03

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 38.64  E-value: 7.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488630032  49 TWKGDLREAYPLGL--------MAAPEEKIVRIHSSSGTTGTPVIIPYTQKD-----VDDWALM 99
Cdd:PLN03051  92 SWCDFLGVAAAQGSvggneyspVYAPVESVTNILFSSGTTGEPKAIPWTHLSplrcaSDGWAHM 155
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH