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Conserved domains on  [gi|991994423|ref|WP_060981809|]
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PaaI family thioesterase [Vibrio splendidus]

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 ...
 48-142 1.72e-14

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 65.73  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  48 RAKIVPTDKAEGYDGIMQGGIVTTLHDSAM---LHCLFQSSIKAMTVSLTSRFHHPILIGQELEVCAQWVKSRRNIHFLE 124
Cdd:COG2050   34 VLRLPVRPEHLNPPGTVHGGALAALADSAAglaANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVE 113

                         90
                 ....*....|....*....
gi 991994423 125 SKITQ-NGTLCSSAQSQFM 142
Cdd:COG2050  114 VEVTDeDGKLVATATGTFA 132
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 48-142 1.72e-14

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 65.73  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  48 RAKIVPTDKAEGYDGIMQGGIVTTLHDSAM---LHCLFQSSIKAMTVSLTSRFHHPILIGQELEVCAQWVKSRRNIHFLE 124
Cdd:COG2050   34 VLRLPVRPEHLNPPGTVHGGALAALADSAAglaANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVE 113

                         90
                 ....*....|....*....
gi 991994423 125 SKITQ-NGTLCSSAQSQFM 142
Cdd:COG2050  114 VEVTDeDGKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 48-142 8.63e-11

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: 55.26  E-value: 8.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  48 RAKIVPTDKAEGYDGIMQGGIVTTLHDSAM---LHCLFQSSIKAMTVSLTSRFHHPILIGqELEVCAQWVKSRRNIHFLE 124
Cdd:cd03443   15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGglaALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVE 93

                         90
                 ....*....|....*....
gi 991994423 125 SKITQ-NGTLCSSAQSQFM 142
Cdd:cd03443   94 VEVTDeDGKLVATARGTFA 112
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 48-142 1.72e-14

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 65.73  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  48 RAKIVPTDKAEGYDGIMQGGIVTTLHDSAM---LHCLFQSSIKAMTVSLTSRFHHPILIGQELEVCAQWVKSRRNIHFLE 124
Cdd:COG2050   34 VLRLPVRPEHLNPPGTVHGGALAALADSAAglaANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVE 113

                         90
                 ....*....|....*....
gi 991994423 125 SKITQ-NGTLCSSAQSQFM 142
Cdd:COG2050  114 VEVTDeDGKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 48-142 8.63e-11

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: 55.26  E-value: 8.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  48 RAKIVPTDKAEGYDGIMQGGIVTTLHDSAM---LHCLFQSSIKAMTVSLTSRFHHPILIGqELEVCAQWVKSRRNIHFLE 124
Cdd:cd03443   15 VLRLPVRPRHLNPGGIVHGGAIATLADTAGglaALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVE 93

                         90
                 ....*....|....*....
gi 991994423 125 SKITQ-NGTLCSSAQSQFM 142
Cdd:cd03443   94 VEVTDeDGKLVATARGTFA 112
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 61-142 2.04e-07

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: 46.31  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  61 DGIMQGGIVTTLHDSAMLHCLFQSSIK---AMTVSLTSRFHHPILIGQELEVCAQWVKSRRNIHFLESKIT-QNGTLCSS 136
Cdd:cd03440   15 GGIVHGGLLLALADEAAGAAAARLGGRglgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVAT 94


                 ....*.
gi 991994423 137 AQSQFM 142
Cdd:cd03440   95 ATATFV 100
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 96-137 3.47e-03

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 35.56  E-value: 3.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 991994423  96 RFHHPILIGQELEVCAQWVKSRRNIHFLESKITQNGTLCSSA 137
Cdd:COG0764   91 KFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEA 132
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 61-142 8.43e-03

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 33.86  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991994423  61 DGIMQGGIVTTLHDSAMLHCLFQSSIKAMTVSL--TSRFHHPILIGQELEVCAQWVKSRRNIHFLESKITQN-GTLCSSA 137
Cdd:cd00556   14 DRRVFGGQLAAQSDLAALRTVPRPHGASGFASLdhHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASA 93


                 ....*
gi 991994423 138 QSQFM 142
Cdd:cd00556   94 TQSFL 98
 
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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