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Conserved domains on  [gi|1960222483|ref|WP_201911843|]
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MULTISPECIES: phenylacetate--CoA ligase family protein [Aeromonas]

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

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List of domain hits

Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1-308 1.17e-50

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


:

Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 172.64  E-value: 1.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483   1 MHNHYDGLEIRPPALRAQQQLDQLNHQLAHVSQYcsgySSAYRHcRLD----------DLEQLASLPLLDSTDLFAAQqa 70
Cdd:COG1541     1 SEMYWNPIETLSREELEALQLERLRATVARAYEN----SPFYRR-KFDeagvdpddikSLEDLAKLPFTTKEDLRDNY-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483  71 ypPFaGLTGRPASQALRVFSCPGQLAIPEYAGADW-------WGAARALFAAGFKAGEVLLNCHDYHAGPTAFIFDNGAR 143
Cdd:COG1541    74 --PF-GLFAVPLEEIVRIHASSGTTGKPTVVGYTRkdldrwaELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 144 QLGCPVVPCGPDDTQRQLEALRRYQPTGFVGplvtlldlleaaelaeTPTECLRhalLCEV----------THPETA--- 210
Cdd:COG1541   151 RLGATVIPAGGGNTERQLRLMQDFGPTVLVG----------------TPSYLLY---LAEVaeeegidprdLSLKKGifg 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 211 --P--------LEAIHGIAAFNC--LvwQDVGV-VAYESRPGQGFIVNE-SCIVEIIDPASGKPVT-GEdPGQLVVTRLD 275
Cdd:COG1541   212 gePwseemrkeIEERWGIKAYDIygL--TEVGPgVAYECEAQDGLHIWEdHFLVEIIDPETGEPVPeGE-EGELVVTTLT 288
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1960222483 276 LE-YPLLRLAT-DWqGYWLARPSRCGRTNRLLKLV 308
Cdd:COG1541   289 KEaMPLIRYRTgDL-TRLLPEPCPCGRTHPRIGRI 322
 
Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1-308 1.17e-50

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 172.64  E-value: 1.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483   1 MHNHYDGLEIRPPALRAQQQLDQLNHQLAHVSQYcsgySSAYRHcRLD----------DLEQLASLPLLDSTDLFAAQqa 70
Cdd:COG1541     1 SEMYWNPIETLSREELEALQLERLRATVARAYEN----SPFYRR-KFDeagvdpddikSLEDLAKLPFTTKEDLRDNY-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483  71 ypPFaGLTGRPASQALRVFSCPGQLAIPEYAGADW-------WGAARALFAAGFKAGEVLLNCHDYHAGPTAFIFDNGAR 143
Cdd:COG1541    74 --PF-GLFAVPLEEIVRIHASSGTTGKPTVVGYTRkdldrwaELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 144 QLGCPVVPCGPDDTQRQLEALRRYQPTGFVGplvtlldlleaaelaeTPTECLRhalLCEV----------THPETA--- 210
Cdd:COG1541   151 RLGATVIPAGGGNTERQLRLMQDFGPTVLVG----------------TPSYLLY---LAEVaeeegidprdLSLKKGifg 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 211 --P--------LEAIHGIAAFNC--LvwQDVGV-VAYESRPGQGFIVNE-SCIVEIIDPASGKPVT-GEdPGQLVVTRLD 275
Cdd:COG1541   212 gePwseemrkeIEERWGIKAYDIygL--TEVGPgVAYECEAQDGLHIWEdHFLVEIIDPETGEPVPeGE-EGELVVTTLT 288
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1960222483 276 LE-YPLLRLAT-DWqGYWLARPSRCGRTNRLLKLV 308
Cdd:COG1541   289 KEaMPLIRYRTgDL-TRLLPEPCPCGRTHPRIGRI 322
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
8-306 4.23e-28

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: 112.33  E-value: 4.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483   8 LEIRPPALRAQQQLDQLNHQLAHVSQYCSGYSSAYRHCRLD-----DLEQLASLPLLDSTDLFAAQQaYPPFAGltgrPA 82
Cdd:cd05913     3 IETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDpddikSLDDLRKLPFTTKEDLRDNYP-FGLFAV----PR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483  83 SQALRVFSCPGQLAIPEYAG-----ADWWG--AARALFAAGFKAGEVLLNCHDYHAGPTAFIFDNGARQLGCPVVPCGPD 155
Cdd:cd05913    78 EKVVRIHASSGTTGKPTVVGytkndLDVWAelVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 156 DTQRQLEALRRYQPTGFVGplvtlldlleaaelaeTPTECLrhaLLCEVTH-----PETAPL------------------ 212
Cdd:cd05913   158 NTERQLQLIKDFGPTVLCC----------------TPSYAL---YLAEEAEeegidPRELSLkvgifgaepwteemrkri 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 213 EAIHGIAAFNCLVWQDVG--VVAYESRPGQGFIVNESC-IVEIIDPASGKPVTGEDPGQLVVTRLDLEY-PLLRlatdwq 288
Cdd:cd05913   219 ERRLGIKAYDIYGLTEIIgpGVAFECEEKDGLHIWEDHfIPEIIDPETGEPVPPGEVGELVFTTLTKEAmPLIR------ 292
                         330       340
                  ....*....|....*....|....*
gi 1960222483 289 gYW---LAR----PSRCGRTNRLLK 306
Cdd:cd05913   293 -YRtrdITRllpgPCPCGRTHRRID 316
 
Name Accession Description Interval E-value
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1-308 1.17e-50

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 172.64  E-value: 1.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483   1 MHNHYDGLEIRPPALRAQQQLDQLNHQLAHVSQYcsgySSAYRHcRLD----------DLEQLASLPLLDSTDLFAAQqa 70
Cdd:COG1541     1 SEMYWNPIETLSREELEALQLERLRATVARAYEN----SPFYRR-KFDeagvdpddikSLEDLAKLPFTTKEDLRDNY-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483  71 ypPFaGLTGRPASQALRVFSCPGQLAIPEYAGADW-------WGAARALFAAGFKAGEVLLNCHDYHAGPTAFIFDNGAR 143
Cdd:COG1541    74 --PF-GLFAVPLEEIVRIHASSGTTGKPTVVGYTRkdldrwaELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 144 QLGCPVVPCGPDDTQRQLEALRRYQPTGFVGplvtlldlleaaelaeTPTECLRhalLCEV----------THPETA--- 210
Cdd:COG1541   151 RLGATVIPAGGGNTERQLRLMQDFGPTVLVG----------------TPSYLLY---LAEVaeeegidprdLSLKKGifg 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 211 --P--------LEAIHGIAAFNC--LvwQDVGV-VAYESRPGQGFIVNE-SCIVEIIDPASGKPVT-GEdPGQLVVTRLD 275
Cdd:COG1541   212 gePwseemrkeIEERWGIKAYDIygL--TEVGPgVAYECEAQDGLHIWEdHFLVEIIDPETGEPVPeGE-EGELVVTTLT 288
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1960222483 276 LE-YPLLRLAT-DWqGYWLARPSRCGRTNRLLKLV 308
Cdd:COG1541   289 KEaMPLIRYRTgDL-TRLLPEPCPCGRTHPRIGRI 322
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
8-306 4.23e-28

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: 112.33  E-value: 4.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483   8 LEIRPPALRAQQQLDQLNHQLAHVSQYCSGYSSAYRHCRLD-----DLEQLASLPLLDSTDLFAAQQaYPPFAGltgrPA 82
Cdd:cd05913     3 IETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDpddikSLDDLRKLPFTTKEDLRDNYP-FGLFAV----PR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483  83 SQALRVFSCPGQLAIPEYAG-----ADWWG--AARALFAAGFKAGEVLLNCHDYHAGPTAFIFDNGARQLGCPVVPCGPD 155
Cdd:cd05913    78 EKVVRIHASSGTTGKPTVVGytkndLDVWAelVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 156 DTQRQLEALRRYQPTGFVGplvtlldlleaaelaeTPTECLrhaLLCEVTH-----PETAPL------------------ 212
Cdd:cd05913   158 NTERQLQLIKDFGPTVLCC----------------TPSYAL---YLAEEAEeegidPRELSLkvgifgaepwteemrkri 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960222483 213 EAIHGIAAFNCLVWQDVG--VVAYESRPGQGFIVNESC-IVEIIDPASGKPVTGEDPGQLVVTRLDLEY-PLLRlatdwq 288
Cdd:cd05913   219 ERRLGIKAYDIYGLTEIIgpGVAFECEEKDGLHIWEDHfIPEIIDPETGEPVPPGEVGELVFTTLTKEAmPLIR------ 292
                         330       340
                  ....*....|....*....|....*
gi 1960222483 289 gYW---LAR----PSRCGRTNRLLK 306
Cdd:cd05913   293 -YRtrdITRllpgPCPCGRTHRRID 316
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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