NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1236167873|ref|WP_094960845|]
View 

MULTISPECIES: phenylacetate--CoA ligase PaaK [Providencia]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PA_CoA_ligase super family cl31173
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ...
 12-433 0e+00

phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]


The actual alignment was detected with superfamily member TIGR02155:

Pssm-ID: 131210 [Multi-domain]  Cd Length: 422  Bit Score: 710.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  12 EFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQIIRI 91
Cdd:TIGR02155   1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  92 HASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTEKQA 171
Cdd:TIGR02155  81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 172 QLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPGVAM 251
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKR-MGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 252 ECADSgESGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVNRNMRRIGKITGRSD 331
Cdd:TIGR02155 240 ECVET-QDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 332 DMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKhPEQ---LTYDERCNICHHLKHRIKSMVGIS 408
Cdd:TIGR02155 319 DMLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELK-PESytlRLHEQASLLAGEIQHTIKQEVGVS 397

                         410       420
                  ....*....|....*....|....*
gi 1236167873 409 TRISIVNCGDIPRSQGKAERVIDTR 433
Cdd:TIGR02155 398 MDVHLVEPGSLPRSEGKARRVVDLR 422
 
Name Accession Description Interval E-value
PA_CoA_ligase TIGR02155
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ...
 12-433 0e+00

phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]


Pssm-ID: 131210 [Multi-domain]  Cd Length: 422  Bit Score: 710.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  12 EFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQIIRI 91
Cdd:TIGR02155   1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  92 HASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTEKQA 171
Cdd:TIGR02155  81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 172 QLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPGVAM 251
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKR-MGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 252 ECADSgESGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVNRNMRRIGKITGRSD 331
Cdd:TIGR02155 240 ECVET-QDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 332 DMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKhPEQ---LTYDERCNICHHLKHRIKSMVGIS 408
Cdd:TIGR02155 319 DMLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELK-PESytlRLHEQASLLAGEIQHTIKQEVGVS 397

                         410       420
                  ....*....|....*....|....*
gi 1236167873 409 TRISIVNCGDIPRSQGKAERVIDTR 433
Cdd:TIGR02155 398 MDVHLVEPGSLPRSEGKARRVVDLR 422
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 9-431 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: 660.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873   9 DPIEFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQI 88
Cdd:COG1541     6 NPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  89 IRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTE 168
Cdd:COG1541    86 VRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEvMGPG 248
Cdd:COG1541   166 RQLRLMQDFGPTVLVGTPSYLLYLAEVAEE-EGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE-VGPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 249 VAMECADsgESGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVN---RNMRRIGK 325
Cdd:COG1541   244 VAYECEA--QDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCpcgRTHPRIGR 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKHPEQLTydercNICHHLKHRIKSMV 405
Cdd:COG1541   322 ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLE-----ALAEAIAAALKAVL 396

                         410       420
                  ....*....|....*....|....*.
gi 1236167873 406 GISTRISIVNCGDIPRSQGKAERVID 431
Cdd:COG1541   397 GLRAEVELVEPGSLPRSEGKAKRVID 422
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 9-433 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: 650.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873   9 DPIEFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQI 88
Cdd:cd05913     1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  89 IRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTE 168
Cdd:cd05913    81 VRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPG 248
Cdd:cd05913   161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEE-EGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 249 VAMECADSGesGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVN---RNMRRIGK 325
Cdd:cd05913   240 VAFECEEKD--GLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCpcgRTHRRIDR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKhPEQLTYDERCNICHHLKHRIKSMV 405
Cdd:cd05913   318 ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVR-PEADDDEKLEALKQRLERHIKSVL 396

                         410       420
                  ....*....|....*....|....*...
gi 1236167873 406 GISTRISIVNCGDIPRSQGKAERVIDTR 433
Cdd:cd05913   397 GVTVEVELVEPGSLPRSEGKAKRVIDKR 424
AMP-binding_C_2 pfam14535
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 338-433 3.08e-35

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: 125.67  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 338 GVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKHPEQLTYDERCNICHHLKHRIKSMVGISTRISIVNCG 417
Cdd:pfam14535   1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEIKDLEALEKRIAKELKSVLGVSVKVELVEPG 80

                          90
                  ....*....|....*.
gi 1236167873 418 DIPRSQGKAERVIDTR 433
Cdd:pfam14535  81 TLPRSEGKAKRVIDLR 96
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 82-348 2.88e-08

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 55.68  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  82 AVPMDQIIRIHASSGTTGRPTVVGYTQRDI----DNWADLiarslrsAGTVRGDKV-------HVaYGYglfTGGLGAHY 150
Cdd:PRK07656  162 EVDPDDVADILFTSGTTGRPKGAMLTHRQLlsnaADWAEY-------LGLTEGDRYlaanpffHV-FGY---KAGVNAPL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 151 GAerlGAAVIPMSGGQTEKQAQLIADFKPDVIMVTPSYCLSIIDeLEKIMGGDASkcSLRLGVFGAEPWTESLRTEIETR 230
Cdd:PRK07656  231 MR---GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQ-HPDRSAEDLS--SLRLAVTGAASMPVALLERFESE 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 231 LGIK-ALDIYGLSEVmGPGVAMECAD------SGESGPTIWedHFYPEIISPNTlKTLGAGEHGELV---FTTL------ 294
Cdd:PRK07656  305 LGVDiVLTGYGLSEA-SGVTTFNRLDddrktvAGTIGTAIA--GVENKIVNELG-EEVPVGEVGELLvrgPNVMkgyydd 380

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236167873 295 ---TKEAmpvIRY----RTRDLTHLMQgvNRNMRrigkITGRSDDMMIIRGVNVFPSQIEE 348
Cdd:PRK07656  381 peaTAAA---IDAdgwlHTGDLGRLDE--EGYLY----IVDRKKDMFIVGGFNVYPAEVEE 432
 
Name Accession Description Interval E-value
PA_CoA_ligase TIGR02155
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ...
 12-433 0e+00

phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]


Pssm-ID: 131210 [Multi-domain]  Cd Length: 422  Bit Score: 710.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  12 EFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQIIRI 91
Cdd:TIGR02155   1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  92 HASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTEKQA 171
Cdd:TIGR02155  81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 172 QLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPGVAM 251
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKR-MGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 252 ECADSgESGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVNRNMRRIGKITGRSD 331
Cdd:TIGR02155 240 ECVET-QDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 332 DMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKhPEQ---LTYDERCNICHHLKHRIKSMVGIS 408
Cdd:TIGR02155 319 DMLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELK-PESytlRLHEQASLLAGEIQHTIKQEVGVS 397

                         410       420
                  ....*....|....*....|....*
gi 1236167873 409 TRISIVNCGDIPRSQGKAERVIDTR 433
Cdd:TIGR02155 398 MDVHLVEPGSLPRSEGKARRVVDLR 422
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 9-431 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: 660.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873   9 DPIEFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQI 88
Cdd:COG1541     6 NPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  89 IRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTE 168
Cdd:COG1541    86 VRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEvMGPG 248
Cdd:COG1541   166 RQLRLMQDFGPTVLVGTPSYLLYLAEVAEE-EGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE-VGPG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 249 VAMECADsgESGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVN---RNMRRIGK 325
Cdd:COG1541   244 VAYECEA--QDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCpcgRTHPRIGR 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKHPEQLTydercNICHHLKHRIKSMV 405
Cdd:COG1541   322 ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLE-----ALAEAIAAALKAVL 396

                         410       420
                  ....*....|....*....|....*.
gi 1236167873 406 GISTRISIVNCGDIPRSQGKAERVID 431
Cdd:COG1541   397 GLRAEVELVEPGSLPRSEGKAKRVID 422
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 9-433 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: 650.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873   9 DPIEFASRDEIESLQYSRMKWTLTHAYENVPMYRKKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPMDQI 88
Cdd:cd05913     1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  89 IRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGGQTE 168
Cdd:cd05913    81 VRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPG 248
Cdd:cd05913   161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEE-EGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 249 VAMECADSGesGPTIWEDHFYPEIISPNTLKTLGAGEHGELVFTTLTKEAMPVIRYRTRDLTHLMQGVN---RNMRRIGK 325
Cdd:cd05913   240 VAFECEEKD--GLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCpcgRTHRRIDR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKhPEQLTYDERCNICHHLKHRIKSMV 405
Cdd:cd05913   318 ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVR-PEADDDEKLEALKQRLERHIKSVL 396

                         410       420
                  ....*....|....*....|....*...
gi 1236167873 406 GISTRISIVNCGDIPRSQGKAERVIDTR 433
Cdd:cd05913   397 GVTVEVELVEPGSLPRSEGKAKRVIDKR 424
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 91-352 3.19e-40

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: 146.66  E-value: 3.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  91 IHASSGTTGRPTVVGYTQRdidNWADLIARSLRSAGTVRGDKVHVAYGYGlFTGGLGAHYGAERLGAAVIPMSGGQTEKQ 170
Cdd:cd04433     5 ILYTSGTTGKPKGVVLSHR---NLLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFDPEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 171 AQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASkcSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPGVA 250
Cdd:cd04433    81 LELIEREKVTILLGVPTLLARLLKAPES-AGYDLS--SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 251 MeCADSGESGP-TIW--EDHFYPEIISPNTlKTLGAGEHGELVFTT------------LTKEAMPVIRYRTRDLTHLMQg 315
Cdd:cd04433   158 G-PPDDDARKPgSVGrpVPGVEVRIVDPDG-GELPPGEIGELVVRGpsvmkgywnnpeATAAVDEDGWYRTGDLGRLDE- 234

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1236167873 316 vNRNMRrigkITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd04433   235 -DGYLY----IVGRLKDMIKSGGENVYPAEVEAVLLG 266
AMP-binding_C_2 pfam14535
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 338-433 3.08e-35

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: 125.67  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 338 GVNVFPSQIEEQIMQFKELSPHYQLEIGRQGNMDNLSVRVELKHPEQLTYDERCNICHHLKHRIKSMVGISTRISIVNCG 417
Cdd:pfam14535   1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEIKDLEALEKRIAKELKSVLGVSVKVELVEPG 80

                          90
                  ....*....|....*.
gi 1236167873 418 DIPRSQGKAERVIDTR 433
Cdd:pfam14535  81 TLPRSEGKAKRVIDLR 96
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 94-352 1.86e-23

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: 102.20  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDIDNWADLIARSLRSAgtvRGDKVHVA----YGYGLFTGGLGAHYgaerLGAAVIPMSGGQTEK 169
Cdd:COG0318   108 TSGTTGRPKGVMLTHRNLLANAAAIAAALGLT---PGDVVLVAlplfHVFGLTVGLLAPLL----AGATLVLLPRFDPER 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 170 QAQLIADFKPDVIMVTPSYCLSIIDELEKiMGGDASkcSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEvMGPGV 249
Cdd:COG0318   181 VLELIERERVTVLFGVPTMLARLLRHPEF-ARYDLS--SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTE-TSPVV 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 250 AMECADSGESGP-TIweDHFYP----EIISPNTlKTLGAGEHGELVF------------TTLTKEAMPVIRYRTRDLTHL 312
Cdd:COG0318   257 TVNPEDPGERRPgSV--GRPLPgvevRIVDEDG-RELPPGEVGEIVVrgpnvmkgywndPEATAEAFRDGWLRTGDLGRL 333

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1236167873 313 M-QGvnrnmrRIgKITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:COG0318   334 DeDG------YL-YIVGRKKDMIISGGENVYPAEVEEVLAA 367
AMP-binding pfam00501
AMP-binding enzyme;
94-337 4.05e-15

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 76.58  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTVRGDKVHVAY-----GYGLFTGGLGAHYgaerLGAAVIPMSGGQT- 167
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTlplfhDFGLSLGLLGPLL----AGATVVLPPGFPAl 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 168 --EKQAQLIADFKPDVIMVTPSYCLSIideLEKIMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEvM 245
Cdd:pfam00501 239 dpAALLELIERYKVTVLYGVPTLLNML---LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTE-T 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 246 GPGVAM------ECADSGESGPTIWEDHFYpeIISPNTLKTLGAGEHGELVF------------TTLTKEAMPVIR-YRT 306
Cdd:pfam00501 315 TGVVTTplpldeDLRSLGSVGRPLPGTEVK--IVDDETGEPVPPGEPGELCVrgpgvmkgylndPELTAEAFDEDGwYRT 392

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1236167873 307 RDLthlmqGVnrnMRRIG--KITGRSDDMMIIR 337
Cdd:pfam00501 393 GDL-----GR---RDEDGylEIVGRKKDQIKLG 417
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 82-352 4.89e-11

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: 64.17  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  82 AVPMDQIIRIHASSGTTGRPTVVGYTQRdidNWADLIARSLRSAGTVRGDK-VHVAygyGLF-TGGLGAHYGAERL-GAA 158
Cdd:cd17631    94 KVLFDDLALLMYTSGTTGRPKGAMLTHR---NLLWNAVNALAALDLGPDDVlLVVA---PLFhIGGLGVFTLPTLLrGGT 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 159 VIPMSGGQTEKQAQLIADFKPDVIMVTPsyclSIIDEL---EKIMGGDASkcSLRLGVFGAEPWTESLRTEIETRlGIKA 235
Cdd:cd17631   168 VVILRKFDPETVLDLIERHRVTSFFLVP----TMIQALlqhPRFATTDLS--SLRAVIYGGAPMPERLLRALQAR-GVKF 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 236 LDIYGLSEvMGPGVAMECAdsgesgptiwEDHF-------YP------EIISPNTlKTLGAGEHGELVFTT--------- 293
Cdd:cd17631   241 VQGYGMTE-TSPGVTFLSP----------EDHRrklgsagRPvffvevRIVDPDG-REVPPGEVGEIVVRGphvmagywn 308

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236167873 294 ---LTKEAMPVIRYRTRDLTHlmqgvnrnMRRIG--KITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd17631   309 rpeATAAAFRDGWFHTGDLGR--------LDEDGylYIVDRKKDMIISGGENVYPAEVEDVLYE 364
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 86-348 2.14e-10

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 61.91  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  86 DQIIRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLrsaGTVRGDKVHVAYG----YGLFTGGLGA-HYGAerlgAAVI 160
Cdd:cd05917     2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERL---GLTEQDRLCIPVPlfhcFGSVLGVLAClTHGA----TMVF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 161 PMSGGQTEKQAQLIADFKPDVIMVTPSYclsIIDELEKIMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDI-Y 239
Cdd:cd05917    75 PSPSFDPLAVLEAIEKEKCTALHGVPTM---FIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 240 GLSEVmGPGVAM-ECADSGES-----GPTIweDHFYPEIISPNTLKTLGAGEHGELV---FTTL---------TKEAMPV 301
Cdd:cd05917   152 GMTET-SPVSTQtRTDDSIEKrvntvGRIM--PHTEAKIVDPEGGIVPPVGVPGELCirgYSVMkgywndpekTAEAIDG 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1236167873 302 IR-YRTRDLTHL-MQGVnrnmrriGKITGRSDDMMIIRGVNVFPSQIEE 348
Cdd:cd05917   229 DGwLHTGDLAVMdEDGY-------CRIVGRIKDMIIRGGENIYPREIEE 270
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 86-352 9.05e-10

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


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 60.47  E-value: 9.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  86 DQIIRIHASSGTTGRPTVVGYTQRDIdnwADLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSGG 165
Cdd:cd05903    93 DAVALLLFTSGTTGEPKGVMHSHNTL---SASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 166 QTEKQAQLIADFKPDVIMVTPSYCLSIIDELEKimgGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVM 245
Cdd:cd05903   170 DPDKALALMREHGVTFMMGATPFLTDLLNAVEE---AGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECP 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 246 GPGVAMECADSGESGPTIWEDHFYPEI-ISPNTLKTLGAGEHGELVFTT------------LTKEAMPVIRYRTRDLTHL 312
Cdd:cd05903   247 GAVTSITPAPEDRRLYTDGRPLPGVEIkVVDDTGATLAPGVEGELLSRGpsvflgyldrpdLTADAAPEGWFRTGDLARL 326

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1236167873 313 MQGvnrnmrriG--KITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd05903   327 DED--------GylRITGRSKDIIIRGGENIPVLEVEDLLLG 360
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 94-352 7.14e-09

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: 57.47  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDIDNWADLIARSLrsAGTVRGDKVHVA----YGYGLFTGGLGAHYgaerLGAAVIPMSGGQT-E 168
Cdd:cd05919    99 SSGTTGPPKGVMHAHRDPLLFADAMAREA--LGLTPGDRVFSSakmfFGYGLGNSLWFPLA----VGASAVLNPGWPTaE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEkimGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGPG 248
Cdd:cd05919   173 RVLATLARFRPTVLYGVPTFYANLLDSCA---GSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIF 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 249 VAMECAD--SGESG-PTIWedhFYPEIISPNTlKTLGAGEHGELVFTTLTKEAM-------PVIR-----YRTRDLthlm 313
Cdd:cd05919   250 LSNRPGAwrLGSTGrPVPG---YEIRLVDEEG-HTIPPGEEGDLLVRGPSAAVGywnnpekSRATfnggwYRTGDK---- 321

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1236167873 314 qgVNRNMRRIGKITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd05919   322 --FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQ 358
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 82-348 2.88e-08

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 55.68  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  82 AVPMDQIIRIHASSGTTGRPTVVGYTQRDI----DNWADLiarslrsAGTVRGDKV-------HVaYGYglfTGGLGAHY 150
Cdd:PRK07656  162 EVDPDDVADILFTSGTTGRPKGAMLTHRQLlsnaADWAEY-------LGLTEGDRYlaanpffHV-FGY---KAGVNAPL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 151 GAerlGAAVIPMSGGQTEKQAQLIADFKPDVIMVTPSYCLSIIDeLEKIMGGDASkcSLRLGVFGAEPWTESLRTEIETR 230
Cdd:PRK07656  231 MR---GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQ-HPDRSAEDLS--SLRLAVTGAASMPVALLERFESE 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 231 LGIK-ALDIYGLSEVmGPGVAMECAD------SGESGPTIWedHFYPEIISPNTlKTLGAGEHGELV---FTTL------ 294
Cdd:PRK07656  305 LGVDiVLTGYGLSEA-SGVTTFNRLDddrktvAGTIGTAIA--GVENKIVNELG-EEVPVGEVGELLvrgPNVMkgyydd 380

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236167873 295 ---TKEAmpvIRY----RTRDLTHLMQgvNRNMRrigkITGRSDDMMIIRGVNVFPSQIEE 348
Cdd:PRK07656  381 peaTAAA---IDAdgwlHTGDLGRLDE--EGYLY----IVDRKKDMFIVGGFNVYPAEVEE 432
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 94-289 6.16e-07

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: 51.47  E-value: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDidnwadLIARSL----RSAGTVRGDKV--------HVaYGYGLFTgglgahYGAERLGAAVIP 161
Cdd:cd05904   166 SSGTTGRSKGVMLTHRN------LIAMVAqfvaGEGSNSDSEDVflcvlpmfHI-YGLSSFA------LGLLRLGATVVV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 162 MSGGQTEKQAQLIADFKPDVIMVTPSYCLSIIDeleKIMGGDASKCSLRLGVFGAEPWTESLRTEIETRL-GIKALDIYG 240
Cdd:cd05904   233 MPRFDLEELLAAIERYKVTHLPVVPPIVLALVK---SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYG 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1236167873 241 LSEvMGPGVAMECADSGESGP-----TI---WEdhfyPEIISPNTLKTLGAGEHGEL 289
Cdd:cd05904   310 MTE-STGVVAMCFAPEKDRAKygsvgRLvpnVE----AKIVDPETGESLPPNQTGEL 361
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 94-352 2.49e-06

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: 49.67  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDIDNWADLIARSLrsaGTVRGDKVHVAYGYGLFTGGLG-AHYGAERLGAAVIPMSGGQTEKQ-A 171
Cdd:cd05959   171 SSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYGLGnSLTFPLSVGATTVLMPERPTPAAvF 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 172 QLIADFKPDVIMVTPS-YCLSIIDELEKIMGGDaskcSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMG---- 246
Cdd:cd05959   248 KRIRRYRPTVFFGVPTlYAAMLAAPNLPSRDLS----SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHifls 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 247 --PGvAMECADSGESGPTiwedhFYPEIISPNTLKTlGAGEHGELVFTTLTKEAMPVIRY-RTRDlthLMQGV-----NR 318
Cdd:cd05959   324 nrPG-RVRYGTTGKPVPG-----YEVELRDEDGGDV-ADGEPGELYVRGPSSATMYWNNRdKTRD---TFQGEwtrtgDK 393

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1236167873 319 NMRRI-GKIT--GRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd05959   394 YVRDDdGFYTyaGRADDMLKVSGIWVSPFEVESALVQ 430
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 95-352 3.20e-06

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: 49.06  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  95 SGTTGRP-TVVGyTQRdidNWADLIARSLRSAGTVRGDKV--HVAYGyglFTGGLGAHYGAERLGAAVIPMSGGQT---E 168
Cdd:cd05930   102 SGSTGKPkGVMV-EHR---GLVNLLLWMQEAYPLTPGDRVlqFTSFS---FDVSVWEIFGALLAGATLVVLPEEVRkdpE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 169 KQAQLIADFKPDVIMVTPSYCLSIIDELEkimggDASKCSLRLGVFGAEPWTESLRTEIETRL-GIKALDIYGLSEVMGP 247
Cdd:cd05930   175 ALADLLAEEGITVLHLTPSLLRLLLQELE-----LAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVD 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 248 GVAMECAdsgesgptiwEDHFYPEIIS-----PNT--------LKTLGAGEHGELVFTT------------LTKEA---- 298
Cdd:cd05930   250 ATYYRVP----------PDDEEDGRVPigrpiPNTrvyvldenLRPVPPGVPGELYIGGaglargylnrpeLTAERfvpn 319

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1236167873 299 --MPVIR-YRTRDLTHLmqgvnrnmRRIGKIT--GRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd05930   320 pfGPGERmYRTGDLVRW--------LPDGNLEflGRIDDQVKIRGYRIELGEIEAALLA 370
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 208-352 1.18e-05

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 47.34  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 208 SLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEVMGP-GVAMECADSGESGPtiwEDHF----YP----EI-ISPNT 277
Cdd:PRK07470  281 SLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNiTVLPPALHDAEDGP---DARIgtcgFErtgmEVqIQDDE 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 278 LKTLGAGEHGEL------VFT------TLTKEAMPVIRYRTRDLTHLmqgvnrNMRRIGKITGRSDDMMIIRGVNVFPSQ 345
Cdd:PRK07470  358 GRELPPGETGEIcvigpaVFAgyynnpEANAKAFRDGWFRTGDLGHL------DARGFLYITGRASDMYISGGSNVYPRE 431


                  ....*..
gi 1236167873 346 IEEQIMQ 352
Cdd:PRK07470  432 IEEKLLT 438
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 86-352 1.23e-05

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


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 47.47  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  86 DQIIRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAgtvRGDKVHVAYGYGLFTGGLGA-----HYgaerLGAAVI 160
Cdd:cd05958    97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRL---REDDRFVGSPPLAFTFGLGGvllfpFG----VGASGV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 161 PMSGGQTEKQAQLIADFKPDVIMVTPSYCLSIIdELEKIMGGDASkcSLRLGVFGAEPWTESLRTEIETRLGIKALDIYG 240
Cdd:cd05958   170 LLEEATPDLLLSAIARYKPTVLFTAPTAYRAML-AHPDAAGPDLS--SLRKCVSAGEALPAALHRAWKEATGIPIIDGIG 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 241 LSEVMGPGVAM--ECADSGESGPTIweDHFYPEIISPNTlKTLGAGEHGELVFTTLTKeampvirYRtrdltHLMQGVNR 318
Cdd:cd05958   247 STEMFHIFISArpGDARPGATGKPV--PGYEAKVVDDEG-NPVPDGTIGRLAVRGPTG-------CR-----YLADKRQR 311

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1236167873 319 NMRRIGKIT----------------GRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd05958   312 TYVQGGWNItgdtysrdpdgyfrhqGRSDDMIVSGGYNIAPPEVEDVLLQ 361
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 96-351 1.81e-05

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 46.70  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  96 GTTGRPTVVGYTQRDI--DNWAdLIARSLRSAGTVrgdkvhVAYGYGLF-------TGGLGAHYGAErlgaAVIPMSGGQ 166
Cdd:cd05944    12 GTTGTPKLAQHTHSNEvyNAWM-LALNSLFDPDDV------LLCGLPLFhvngsvvTLLTPLASGAH----VVLAGPAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 167 TEKQA-----QLIADFKPDVIMVTPSyclsIIDELEKImGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGL 241
Cdd:cd05944    81 RNPGLfdnfwKLVERYRITSLSTVPT----VYAALLQV-PVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 242 SE------VMGPGVAMECADSGESGPtiwedHFYPEII----SPNTLKTLGAGEHGELVFTTLTkeAMPVIRYRTRDLTH 311
Cdd:cd05944   156 TEatclvaVNPPDGPKRPGSVGLRLP-----YARVRIKvldgVGRLLRDCAPDEVGEICVAGPG--VFGGYLYTEGNKNA 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1236167873 312 LMQGVNRNMRRIGK--------ITGRSDDMMIIRGVNVFPSQIEEQIM 351
Cdd:cd05944   229 FVADGWLNTGDLGRldadgylfITGRAKDLIIRGGHNIDPALIEEALL 276
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 95-251 3.34e-05

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 45.95  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  95 SGTTGRPTVVGYTQRDIDnwadLIARSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAA-VIPMSGgQTEKQAQL 173
Cdd:PRK06187  176 SGTTGHPKGVVLSHRNLF----LHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKqVIPRRF-DPENLLDL 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1236167873 174 IADFKPDVIMVTPSyCLSIIDELEKIMGGDASkcSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEvMGPGVAM 251
Cdd:PRK06187  251 IETERVTFFFAVPT-IWQMLLKAPRAYFVDFS--SLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTE-TSPVVSV 324
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 326-352 5.86e-05

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: 44.70  E-value: 5.86e-05
                          10        20
                  ....*....|....*....|....*..
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQIMQ 352
Cdd:cd17633   226 LVGRESDMIIIGGINIFPTEIESVLKA 252
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 54-291 5.87e-05

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


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 45.21  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  54 DFKQLSDIEKFpytTKQDLRENYPFSTFAVPM----DQIIRIHASSGTTGRPTVVGYTQRDI----DNWADLIARSLRSA 125
Cdd:cd17642   151 DYKGYQCLYTF---ITQNLPPGFNEYDFKPPSfdrdEQVALIMNSSGSTGLPKGVQLTHKNIvarfSHARDPIFGNQIIP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 126 GTVRGDKVHVAYGYGLFTgglgaHYGAERLGAAVIPMSGGQTEKQAQLIADFKPDVIMVTPSYcLSIIDELEKIMGGDAS 205
Cdd:cd17642   228 DTAILTVIPFHHGFGMFT-----TLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTL-FAFFAKSTLVDKYDLS 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 206 kcSLRLGVFGAEPWTESLRTEIETRLGIKAL-DIYGLSEVMGPGVAMECADS--GESGPTIweDHFYPEIISPNTLKTLG 282
Cdd:cd17642   302 --NLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDkpGAVGKVV--PFFYAKVVDLDTGKTLG 377


                  ....*....
gi 1236167873 283 AGEHGELVF 291
Cdd:cd17642   378 PNERGELCV 386
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 94-347 7.20e-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: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  94 SSGTTGRPTVVGYTQRDIDNWADLIARSlrsAGTVRGDK---------VHVAYGYGLFTGGLGahygaerLGAAVIPMSG 164
Cdd:cd05923   158 TSGTTGLPKGAVIPQRAAESRVLFMSTQ---AGLRHGRHnvvlglmplYHVIGFFAVLVAALA-------LDGTYVVVEE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 165 GQTEKQAQLIADFKPDVIMVTPSYclsiIDEL-EKIMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSE 243
Cdd:cd05923   228 FDPADALKLIEQERVTSLFATPTH----LDALaAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 244 VMGPGVAMECADSGESGPTiwedhFYPEI----ISPNTLKTLGAGEHGELVFTTLTKEAMpvIRYRTR---DLTHLMQGV 316
Cdd:cd05923   304 AMNSLYMRDARTGTEMRPG-----FFSEVrivrIGGSPDEALANGEEGELIVAAAADAAF--TGYLNQpeaTAKKLQDGW 376

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1236167873 317 NRNMRRI-----GK--ITGRSDDMMIIRGVNVFPSQIE 347
Cdd:cd05923   377 YRTGDVGyvdpsGDvrILGRVDDMIISGGENIHPSEIE 414
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 85-290 1.17e-04

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: 44.39  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  85 MDQIIRIHASSGTTGRPTVVGYTQRDIdnWADLIArSLRSAGTVRGDKVHVAYGYGLFTGGLGAHYGAERLGAAVIPMSG 164
Cdd:cd05935    83 LDDLALIPYTSGTTGLPKGCMHTHFSA--AANALQ-SAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 165 GQTEKQAQLIADFKPDVIMVTPSyclSIIDELEKIMGGDASKCSLRLGVFGAEPWTESLRTEIETRLGIKALDIYGLSEV 244
Cdd:cd05935   160 WDRETALELIEKYKVTFWTNIPT---MLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 245 MGP--------------GVAMECADSgesgptiwedhfypEIISPNTLKTLGAGEHGELV 290
Cdd:cd05935   237 MSQthtnpplrpklqclGIP*FGVDA--------------RVIDIETGRELPPNEVGEIV 282
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 85-287 2.73e-04

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 43.37  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873   85 MDQIIRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRsagTVRGDKV-------HvAYGyglFTG--------GLGAH 149
Cdd:PRK08633   781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN---LRNDDVIlsslpffH-SFG---LTVtlwlplleGIKVV 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  150 YGAERLGAAVIpmsggqtekqAQLIADFKPDVIMVTPSYCLSII--DELEKIMGGdaskcSLRLGVFGAEPWTESLRTEI 227
Cdd:PRK08633   854 YHPDPTDALGI----------AKLVAKHRATILLGTPTFLRLYLrnKKLHPLMFA-----SLRLVVAGAEKLKPEVADAF 918

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1236167873  228 ETRLGIKALDIYGLSEvMGPGVAMECADSGESGptIWEDHFYPE-------------IISPNTLKTLGAGEHG 287
Cdd:PRK08633   919 EEKFGIRILEGYGATE-TSPVASVNLPDVLAAD--FKRQTGSKEgsvgmplpgvavrIVDPETFEELPPGEDG 988
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 326-428 5.18e-04

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: 42.23  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 326 ITGRSDDMMIIRGVNVFPSQIEEQImqfKELSPHYQL----------EIGRQgnmdnLSVRVELKHPEQLTYDErcNICH 395
Cdd:cd05931   434 ITGRLKDLIIVRGRNHYPQDIEATA---EEAHPALRPgcvaafsvpdDGEER-----LVVVAEVERGADPADLA--AIAA 503

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1236167873 396 HLKHRIKSMVGISTR-ISIVNCGDIPR-SQGKAER 428
Cdd:cd05931   504 AIRAAVAREHGVAPAdVVLVRPGSIPRtSSGKIQR 538
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 304-360 5.37e-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: 42.27  E-value: 5.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1236167873 304 YRTRDLTHLMqgvNRNMRrigkITGRSDDMMIIRGVNVFPSQIEEQIMQFKELSPHY 360
Cdd:cd05906   411 FRTGDLGFLD---NGNLT----ITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 86-289 5.68e-04

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


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 42.20  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873  86 DQIIRIHASSGTTGRPTVVGYTQRDIDNWADLIARSLRSAGTvRGDKV-------HVaygYGLFTgglgAHYGAERlGAA 158
Cdd:cd05911   146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDG-SNDVIlgflplyHI---YGLFT----TLASLLN-GAT 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236167873 159 VIPMSGGQTEKQAQLIADFKPDVIMVTPSYCLSIID--ELEKImggDASkcSLRLGVFGAEPWTESLRTEIETRLGIKAL 236
Cdd:cd05911   217 VIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKspLLDKY---DLS--SLRVILSGGAPLSKELQELLAKRFPNATI 291

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1236167873 237 -DIYGLSEvMGPGVAMecadsgesgpTIWEDHFYP-----------EIISPNTLKTLGAGEHGEL 289
Cdd:cd05911   292 kQGYGMTE-TGGILTV----------NPDGDDKPGsvgrllpnveaKIVDDDGKDSLGPNEPGEI 345
spore_sigF TIGR02885
RNA polymerase sigma-F factor; Members of this protein family are the RNA polymerase sigma ...
 36-100 4.46e-03

RNA polymerase sigma-F factor; Members of this protein family are the RNA polymerase sigma factor F. Sigma-F is specifically and universally a component of the Firmicutes lineage endospore formation program, and is expressed in the forespore to turn on expression of dozens of genes. It is closely homologous to sigma-G, which is also expressed in the forespore. [Transcription, Transcription factors, Cellular processes, Sporulation and germination]


Pssm-ID: 131931 [Multi-domain]  Cd Length: 231  Bit Score: 38.54  E-value: 4.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1236167873  36 ENVPMYR---KKFDDAGVHPDDFKQLSDIEKFPYTTKQDLRENYPFSTFAVPM-----------DQIIRIHASSGTTGR 100
Cdd:TIGR02885  19 CNLRLVWsivKRFLNRGYEPEDLFQIGCIGLVKAIDKFDLSYDVKFSTYAVPMimgeikrflrdDGIIKVSRSLKELAR 97
 
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