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Conserved domains on  [gi|814584429|ref|WP_046383638|]
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MULTISPECIES: PaaI family thioesterase [Pseudomonas]

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 ...
 39-151 1.46e-10

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 55.72  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  39 HVVAEHQPEAKYSGWPDLVYGGLIAMLVDCHSNWTAMAyHYRAEQRepgslpridCVTGHLGIKFIKPTPLGVTLTLRAR 118
Cdd:COG2050   32 RAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANS-ALPPGRR---------AVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 814584429 119 VEGDVGRKSRVVCEVYAGD-VLTAIGDSVFVRVD 151
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDgKLVATATGTFAVLP 135
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 39-151 1.46e-10

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 55.72  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  39 HVVAEHQPEAKYSGWPDLVYGGLIAMLVDCHSNWTAMAyHYRAEQRepgslpridCVTGHLGIKFIKPTPLGVTLTLRAR 118
Cdd:COG2050   32 RAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANS-ALPPGRR---------AVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 814584429 119 VEGDVGRKSRVVCEVYAGD-VLTAIGDSVFVRVD 151
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDgKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 39-149 1.50e-07

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: 47.17  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  39 HVVAEHQPEAKYSGWPDLVYGGLIAMLVDchsnwTAMAYHYRAeQREPGSLpridCVTGHLGIKFIKPTPLGvTLTLRAR 118
Cdd:cd03443   13 RVVLRLPVRPRHLNPGGIVHGGAIATLAD-----TAGGLAALS-ALPPGAL----AVTVDLNVNYLRPARGG-DLTARAR 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 814584429 119 VEGDVGRKSRVVCEVYAGD-VLTAIGDSVFVR 149
Cdd:cd03443   82 VVKLGRRLAVVEVEVTDEDgKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 57-142 1.65e-04

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: 38.39  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429   57 VYGGLIAMLVDchsnwTAMAYHYRAEqrepgSLPRIDCVTGHLGIKFIKPTPLGVTLTLRARVEgDVGRKSRVV-CEVYA 135
Cdd:pfam03061   4 VHGGVYLALAD-----EAAGAAARRL-----GGSQQVVVVVELSIDFLRPARLGDRLTVEARVV-RLGRTSAVVeVEVRD 72


                  ....*..
gi 814584429  136 GDVLTAI 142
Cdd:pfam03061  73 EDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 39-151 1.46e-10

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 55.72  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  39 HVVAEHQPEAKYSGWPDLVYGGLIAMLVDCHSNWTAMAyHYRAEQRepgslpridCVTGHLGIKFIKPTPLGVTLTLRAR 118
Cdd:COG2050   32 RAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANS-ALPPGRR---------AVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 814584429 119 VEGDVGRKSRVVCEVYAGD-VLTAIGDSVFVRVD 151
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDgKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 39-149 1.50e-07

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: 47.17  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  39 HVVAEHQPEAKYSGWPDLVYGGLIAMLVDchsnwTAMAYHYRAeQREPGSLpridCVTGHLGIKFIKPTPLGvTLTLRAR 118
Cdd:cd03443   13 RVVLRLPVRPRHLNPGGIVHGGAIATLAD-----TAGGLAALS-ALPPGAL----AVTVDLNVNYLRPARGG-DLTARAR 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 814584429 119 VEGDVGRKSRVVCEVYAGD-VLTAIGDSVFVR 149
Cdd:cd03443   82 VVKLGRRLAVVEVEVTDEDgKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 57-148 3.66e-05

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: 40.54  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  57 VYGGLIAMLVDCHSNWTAMAYHyraeqrepgsLPRIDCVTGHLGIKFIKPTPLGVTLTLRARVEGDVGRKSRVVCEVYAG 136
Cdd:cd03440   18 VHGGLLLALADEAAGAAAARLG----------GRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNE 87

                         90
                 ....*....|...
gi 814584429 137 D-VLTAIGDSVFV 148
Cdd:cd03440   88 DgKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 57-142 1.65e-04

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: 38.39  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429   57 VYGGLIAMLVDchsnwTAMAYHYRAEqrepgSLPRIDCVTGHLGIKFIKPTPLGVTLTLRARVEgDVGRKSRVV-CEVYA 135
Cdd:pfam03061   4 VHGGVYLALAD-----EAAGAAARRL-----GGSQQVVVVVELSIDFLRPARLGDRLTVEARVV-RLGRTSAVVeVEVRD 72


                  ....*..
gi 814584429  136 GDVLTAI 142
Cdd:pfam03061  73 EDGRLVA 79
COG5496 COG5496
Predicted thioesterase [General function prediction only];
95-150 1.79e-03

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 36.31  E-value: 1.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 814584429  95 VTGHLGIKFIKPTPLGVTLTLRARVEGDVGRksRVVCEVYAGDVLTAIGDSVFVRV 150
Cdd:COG5496   59 VGTEVDVKHLAPTPVGMTVTVTAELTEVDGR--RLTFEVEAFDEAGLIGEGTHERF 112
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 57-151 5.16e-03

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 35.24  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814584429  57 VYGGLIAMLVDCHSNWTAMAYhyrAEQRepgslpridCVTGHL-GIKFIKPTPLGVTLTLRARVEgDVGRKS-RVVCEVY 134
Cdd:cd03442   25 IFGGWLLEWMDELAGIAAYRH---AGGR---------VVTASVdRIDFLKPVRVGDVVELSARVV-YTGRTSmEVGVEVE 91

                         90       100
                 ....*....|....*....|...
gi 814584429 135 AGDV------LTAIGDSVFVRVD 151
Cdd:cd03442   92 AEDPltgerrLVTSAYFTFVALD 114
 
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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