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Conserved domains on  [gi|495965167|ref|WP_008689746|]
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MULTISPECIES: PaaI family thioesterase [Longicatena]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-142 8.21e-22

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.61  E-value: 8.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  16 RRLQAQNTINAMMEMRVLSINinKKQVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNF 94
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVE--PGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTIELNINF 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495965167  95 DKGIAEHETLVIEGYCDHVGSRIVQARAIAhFSDSNALVATANGSYAV 142
Cdd:COG2050   87 LRPARLGDRLTAEARVVRRGRRLAVVEVEV-TDEDGKLVATATGTFAV 133
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-142 8.21e-22

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.61  E-value: 8.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  16 RRLQAQNTINAMMEMRVLSINinKKQVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNF 94
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVE--PGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTIELNINF 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495965167  95 DKGIAEHETLVIEGYCDHVGSRIVQARAIAhFSDSNALVATANGSYAV 142
Cdd:COG2050   87 LRPARLGDRLTAEARVVRRGRRLAVVEVEV-TDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-142 1.90e-19

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 77.98  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  27 MMEMRVLSINinKKQVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNFdKGIAEHETLV 105
Cdd:cd03443    1 LLGIRVVEVG--PGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSaLPPGALAVTVDLNVNY-LRPARGGDLT 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495965167 106 IEGYCDHVGSRIVQARAIAhFSDSNALVATANGSYAV 142
Cdd:cd03443   78 ARARVVKLGRRLAVVEVEV-TDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 57-118 1.48e-07

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 46.09  E-value: 1.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495965167   57 GHMHGGMLSTAMDITMGCA--SYIFSDASFTpTIQMSVNFDKGIAEHETLVIEGYCDHVGSRIV 118
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAarRLGGSQQVVV-VVELSIDFLRPARLGDRLTVEARVVRLGRTSA 64
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 41-142 5.32e-05

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167   41 QVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNFDKGIAEhETLVIEGYCDHVGSRiVQ 119
Cdd:TIGR00369  17 FLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLcNSGGQAVVGLELNANHLRPARE-GKVRAIAQVVHLGRQ-TG 94

                          90       100
                  ....*....|....*....|...
gi 495965167  120 ARAIAHFSDSNALVATANGSYAV 142
Cdd:TIGR00369  95 VAEIEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-142 8.21e-22

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.61  E-value: 8.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  16 RRLQAQNTINAMMEMRVLSINinKKQVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNF 94
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVE--PGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTIELNINF 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495965167  95 DKGIAEHETLVIEGYCDHVGSRIVQARAIAhFSDSNALVATANGSYAV 142
Cdd:COG2050   87 LRPARLGDRLTAEARVVRRGRRLAVVEVEV-TDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-142 1.90e-19

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 77.98  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  27 MMEMRVLSINinKKQVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNFdKGIAEHETLV 105
Cdd:cd03443    1 LLGIRVVEVG--PGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSaLPPGALAVTVDLNVNY-LRPARGGDLT 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495965167 106 IEGYCDHVGSRIVQARAIAhFSDSNALVATANGSYAV 142
Cdd:cd03443   78 ARARVVKLGRRLAVVEVEV-TDEDGKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 42-141 1.84e-10

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 54.40  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  42 VILQFPVQKWQLNPAGHMHGGMLSTAMDITMG-CASYIFSDASFTPTIQMSVNFDKGIAEHETLVIEGYCDHVGSRIVQA 120
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGaAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|.
gi 495965167 121 RAIAhFSDSNALVATANGSYA 141
Cdd:cd03440   81 EVEV-RNEDGKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 57-118 1.48e-07

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 46.09  E-value: 1.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495965167   57 GHMHGGMLSTAMDITMGCA--SYIFSDASFTpTIQMSVNFDKGIAEHETLVIEGYCDHVGSRIV 118
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAarRLGGSQQVVV-VVELSIDFLRPARLGDRLTVEARVVRLGRTSA 64
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 41-142 5.32e-05

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167   41 QVILQFPVQKWQLNPAGHMHGGMLSTAMDITMGCASYI-FSDASFTPTIQMSVNFDKGIAEhETLVIEGYCDHVGSRiVQ 119
Cdd:TIGR00369  17 FLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLcNSGGQAVVGLELNANHLRPARE-GKVRAIAQVVHLGRQ-TG 94

                          90       100
                  ....*....|....*....|...
gi 495965167  120 ARAIAHFSDSNALVATANGSYAV 142
Cdd:TIGR00369  95 VAEIEIVDEQGRLCALSRGTTAV 117
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
52-136 2.10e-03

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 36.31  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965167  52 QLNPAGHMHGGMLSTAMDITMGCASYIFSDASFTpTIQM-SVNFDKGIAEHETLVIEGYCDHVGSR----IVQARAIAHF 126
Cdd:COG1607   17 DTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVV-TASVdSVDFLRPVRVGDIVELYARVVRVGRTsmevGVEVWAEDLR 95

                         90
                 ....*....|
gi 495965167 127 SDSNALVATA 136
Cdd:COG1607   96 TGERRLVTEA 105
 
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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