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Conserved domains on  [gi|2567559077|ref|WP_306461457|]
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PaaI family thioesterase [Colwellia ponticola]

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 ...
 52-162 1.90e-15

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 68.82  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  52 VARFTPSDIFTAIPGFVYGGMTASLIDChgTGSASAMAFLAQKRemgtlpplRFVTGALNINFLAPTPQGVELTLIGRFS 131
Cdd:COG2050    34 VLRLPVRPEHLNPPGTVHGGALAALADS--AAGLAANSALPPGR--------RAVTIELNINFLRPARLGDRLTAEARVV 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2567559077 132 EVKDRKIVVDITL-SANDVVCSTAQVIAVLMP 162
Cdd:COG2050   104 RRGRRLAVVEVEVtDEDGKLVATATGTFAVLP 135
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 52-162 1.90e-15

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 68.82  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  52 VARFTPSDIFTAIPGFVYGGMTASLIDChgTGSASAMAFLAQKRemgtlpplRFVTGALNINFLAPTPQGVELTLIGRFS 131
Cdd:COG2050    34 VLRLPVRPEHLNPPGTVHGGALAALADS--AAGLAANSALPPGR--------RAVTIELNINFLRPARLGDRLTAEARVV 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2567559077 132 EVKDRKIVVDITL-SANDVVCSTAQVIAVLMP 162
Cdd:COG2050   104 RRGRRLAVVEVEVtDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 52-155 1.72e-13

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: 62.96  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  52 VARFTPSDIFTAIPGFVYGGMTASLIDchgtgsaSAMAFLAqkreMGTLPPLR-FVTGALNINFLAPTPQGVeLTLIGRF 130
Cdd:cd03443    15 VLRLPVRPRHLNPGGIVHGGAIATLAD-------TAGGLAA----LSALPPGAlAVTVDLNVNYLRPARGGD-LTARARV 82

                          90       100
                  ....*....|....*....|....*.
gi 2567559077 131 SEVKDRKIVVDITL-SANDVVCSTAQ 155
Cdd:cd03443    83 VKLGRRLAVVEVEVtDEDGKLVATAR 108
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 66-148 1.13e-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: 46.86  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  66 GFVYGGMTASLIDchgtgSASAMAFLAQKRemgtlPPLRFVTGALNINFLAPTPQGVELTLIGRFSEVKDRKIVVDITLS 145
Cdd:pfam03061   2 GVVHGGVYLALAD-----EAAGAAARRLGG-----SQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVR 71


                  ...
gi 2567559077 146 AND 148
Cdd:pfam03061  72 DED 74
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 52-162 1.90e-15

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 68.82  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  52 VARFTPSDIFTAIPGFVYGGMTASLIDChgTGSASAMAFLAQKRemgtlpplRFVTGALNINFLAPTPQGVELTLIGRFS 131
Cdd:COG2050    34 VLRLPVRPEHLNPPGTVHGGALAALADS--AAGLAANSALPPGR--------RAVTIELNINFLRPARLGDRLTAEARVV 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2567559077 132 EVKDRKIVVDITL-SANDVVCSTAQVIAVLMP 162
Cdd:COG2050   104 RRGRRLAVVEVEVtDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 52-155 1.72e-13

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: 62.96  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  52 VARFTPSDIFTAIPGFVYGGMTASLIDchgtgsaSAMAFLAqkreMGTLPPLR-FVTGALNINFLAPTPQGVeLTLIGRF 130
Cdd:cd03443    15 VLRLPVRPRHLNPGGIVHGGAIATLAD-------TAGGLAA----LSALPPGAlAVTVDLNVNYLRPARGGD-LTARARV 82

                          90       100
                  ....*....|....*....|....*.
gi 2567559077 131 SEVKDRKIVVDITL-SANDVVCSTAQ 155
Cdd:cd03443    83 VKLGRRLAVVEVEVtDEDGKLVATAR 108
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 66-148 1.13e-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: 46.86  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  66 GFVYGGMTASLIDchgtgSASAMAFLAQKRemgtlPPLRFVTGALNINFLAPTPQGVELTLIGRFSEVKDRKIVVDITLS 145
Cdd:pfam03061   2 GVVHGGVYLALAD-----EAAGAAARRLGG-----SQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVR 71


                  ...
gi 2567559077 146 AND 148
Cdd:pfam03061  72 DED 74
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 50-159 1.58e-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: 47.08  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559077  50 VTVARFTPSDIFTAipGFVYGGMTASLIDchgtgsaSAMAFLAqkrEMGTLPPLRFVTGALNINFLAPTPQGVELTLIGR 129
Cdd:cd03440     2 VLRLTVTPEDIDGG--GIVHGGLLLALAD-------EAAGAAA---ARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAE 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2567559077 130 FSEVKDRKIVVDITLSAND-VVCSTAQVIAV 159
Cdd:cd03440    70 VVRVGRSSVTVEVEVRNEDgKLVATATATFV 100
 
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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