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Conserved domains on  [gi|15600712|ref|NP_254206|]
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acyl-CoA thioesterase [Pseudomonas aeruginosa PAO1]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787832)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016787
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
35-174 5.18e-72

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 214.27  E-value: 5.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  35 QLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEI 114
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712 115 GVKVITENIREQSVRHTNSCFFTMVALDDERKPVAVRPLELETAEQKRRFAQAQQRRQLR 174
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELR 145
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
35-174 5.18e-72

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 214.27  E-value: 5.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  35 QLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEI 114
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712 115 GVKVITENIREQSVRHTNSCFFTMVALDDERKPVAVRPLELETAEQKRRFAQAQQRRQLR 174
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELR 145
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 35-150 2.83e-54

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: 168.52  E-value: 2.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  35 QLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEI 114
Cdd:cd03442   7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600712 115 GVKVITENIREQSVRHTNSCFFTMVALDDERKPVAV 150
Cdd:cd03442  87 GVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-125 1.93e-17

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: 73.06  E-value: 1.93e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600712    51 GNVHGGTLLKYLDEVAYACASRYAGRY-VVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEIGVKVITENIRE 125
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
33-153 3.53e-11

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 57.95  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712   33 NNQLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSM 112
Cdd:PRK10694   9 QGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15600712  113 EIGV-----KVITENIrEQSVRHTNScFFTMVALDDERKPvavRPL 153
Cdd:PRK10694  89 SINIevwvkKVASEPI-GQRYKATEA-LFTYVAVDPEGKP---RAL 129
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
35-174 5.18e-72

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 214.27  E-value: 5.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  35 QLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEI 114
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712 115 GVKVITENIREQSVRHTNSCFFTMVALDDERKPVAVRPLELETAEQKRRFAQAQQRRQLR 174
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELR 145
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 35-150 2.83e-54

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: 168.52  E-value: 2.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  35 QLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEI 114
Cdd:cd03442   7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600712 115 GVKVITENIREQSVRHTNSCFFTMVALDDERKPVAV 150
Cdd:cd03442  87 GVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-125 1.93e-17

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: 73.06  E-value: 1.93e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600712    51 GNVHGGTLLKYLDEVAYACASRYAGRY-VVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEIGVKVITENIRE 125
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 36-139 1.75e-11

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: 57.87  E-value: 1.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  36 LSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYA--GRYVVTLSVDqVIFREPVHVGELVTFLASVNYTGRTSME 113
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|....*.
gi 15600712 114 IGVKvitenIREQSVRHTNSCFFTMV 139
Cdd:cd03440  80 VEVE-----VRNEDGKLVATATATFV 100
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
33-153 3.53e-11

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 57.95  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712   33 NNQLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSM 112
Cdd:PRK10694   9 QGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15600712  113 EIGV-----KVITENIrEQSVRHTNScFFTMVALDDERKPvavRPL 153
Cdd:PRK10694  89 SINIevwvkKVASEPI-GQRYKATEA-LFTYVAVDPEGKP---RAL 129
PLN02647 PLN02647
acyl-CoA thioesterase
 78-188 1.18e-10

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 59.42  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712   78 VVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSMEIGVKVI----TENIREQSVRHTNScfFTMVALDDE-RKPVAVRP 152
Cdd:PLN02647 144 LVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIqptkDESNTSDSVALTAN--FTFVARDSKtGKSAPVNR 221

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15600712  153 LELETAEQKRRFAQAQQRRQLRAELEARYQAIREDG 188
Cdd:PLN02647 222 LSPETEEEKLLFEEAEARNKLRKKKRGEQKREFENG 257
PLN02647 PLN02647
acyl-CoA thioesterase
 44-163 8.06e-07

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 48.25  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712   44 PDMANFSGNVHGGTLLKYLDEVAYACASRYAGRYVVTLSVDQVIFREPVHVGELVTFLASVNYTGRTSME---IGVKVIT 120
Cdd:PLN02647 299 PQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSEqplINVEVVA 378

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15600712  121 ENIREQ--SVRHTNSCFFTM-----VALDDERKPVAVRPlelETAEQKRR 163
Cdd:PLN02647 379 HVTRPElrSSEVSNTFYFTFtvrpeAAMKNGFKIRNVVP---ATEEEARR 425
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 32-122 1.17e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.01  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  32 GNNQLSMTVLMTPDMANFSGNVHGGTLLKYLDEVAYACASRY--AGRYVVTLSVdQVIFREPVHVGELVTFLASVNYTGR 109
Cdd:COG2050  29 EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIEL-NINFLRPARLGDRLTAEARVVRRGR 107

                        90
                ....*....|...
gi 15600712 110 TSMEIGVKVITEN 122
Cdd:COG2050 108 RLAVVEVEVTDED 120
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 36-122 8.19e-04

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: 37.54  E-value: 8.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600712  36 LSMTVlmTPDMANFSGNVHGGTLLKYLDEVAYACASRY--AGRYVVT--LSVDqviFREPVHVGELvTFLASVNYTGRTS 111
Cdd:cd03443  16 LRLPV--RPRHLNPGGIVHGGAIATLADTAGGLAALSAlpPGALAVTvdLNVN---YLRPARGGDL-TARARVVKLGRRL 89

                        90
                ....*....|.
gi 15600712 112 MEIGVKVITEN 122
Cdd:cd03443  90 AVVEVEVTDED 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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