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Conserved domains on  [gi|15597889|ref|NP_251383|]
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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];
7-147 2.06e-68

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 204.26  E-value: 2.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   7 QLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEV 86
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597889  87 GVKVMTENIHERTVRHTNSCFFTMVAMDDQRRPVAVRPLEPETAIEKRRYAQALARREQRK 147
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-147 2.06e-68

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 204.26  E-value: 2.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   7 QLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEV 86
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597889  87 GVKVMTENIHERTVRHTNSCFFTMVAMDDQRRPVAVRPLEPETAIEKRRYAQALARREQRK 147
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 5-122 2.13e-50

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: 157.73  E-value: 2.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   5 SYQLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSM 84
Cdd:cd03442   5 DTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSM 84

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15597889  85 EVGVKVMTENIHERTVRHTNSCFFTMVAMDDQRRPVAV 122
Cdd:cd03442  85 EVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 23-97 2.16e-15

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: 66.89  E-value: 2.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597889    23 GNVHGGALLKLLDEVAFACAKRYAGRY-VVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEVGVKVMTENIHE 97
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
7-125 2.88e-11

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 57.95  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889    7 QLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEV 86
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15597889   87 GV-----KVMTENIHERtVRHTNScFFTMVAMDDQRRPvavRPL 125
Cdd:PRK10694  91 NIevwvkKVASEPIGQR-YKATEA-LFTYVAVDPEGKP---RAL 129
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-147 2.06e-68

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 204.26  E-value: 2.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   7 QLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEV 86
Cdd:COG1607   6 ELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597889  87 GVKVMTENIHERTVRHTNSCFFTMVAMDDQRRPVAVRPLEPETAIEKRRYAQALARREQRK 147
Cdd:COG1607  86 GVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 5-122 2.13e-50

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: 157.73  E-value: 2.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   5 SYQLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSM 84
Cdd:cd03442   5 DTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSM 84

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15597889  85 EVGVKVMTENIHERTVRHTNSCFFTMVAMDDQRRPVAV 122
Cdd:cd03442  85 EVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 23-97 2.16e-15

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: 66.89  E-value: 2.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597889    23 GNVHGGALLKLLDEVAFACAKRYAGRY-VVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEVGVKVMTENIHE 97
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRL 77
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
7-125 2.88e-11

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 57.95  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889    7 QLTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEV 86
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15597889   87 GV-----KVMTENIHERtVRHTNScFFTMVAMDDQRRPvavRPL 125
Cdd:PRK10694  91 NIevwvkKVASEPIGQR-YKATEA-LFTYVAVDPEGKP---RAL 129
PLN02647 PLN02647
acyl-CoA thioesterase
 50-158 2.63e-10

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 57.88  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   50 VVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSMEVGVKVM-----TENIHERTVRHTNscfFTMVAMDDQRRPVA-VR 123
Cdd:PLN02647 144 LVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIqptkdESNTSDSVALTAN---FTFVARDSKTGKSApVN 220

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15597889  124 PLEPETAIEKRRYAQALARREQRKlmELRYQEIRE 158
Cdd:PLN02647 221 RLSPETEEEKLLFEEAEARNKLRK--KKRGEQKRE 253
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 8-111 1.55e-08

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: 49.78  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   8 LTMSVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYA--GRYVVTLSVDqVIFREPIHVGELVTFLASVNYTGRTSME 85
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|....*.
gi 15597889  86 VGVKvmtenIHERTVRHTNSCFFTMV 111
Cdd:cd03440  80 VEVE-----VRNEDGKLVATATATFV 100
PLN02647 PLN02647
acyl-CoA thioesterase
 11-136 1.78e-08

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 52.48  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   11 SVLMTPDKANFSGNVHGGALLKLLDEVAFACAKRYAGRYVVTLSVDQVIFREPIHVGELVTFLASVNYTGRTSME----- 85
Cdd:PLN02647 294 SLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSEqplin 373

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597889   86 VGVKVMTENIHERTVRHTNSCFFTM-----VAMDDQRRpvaVRPLEPETAIEKRRY 136
Cdd:PLN02647 374 VEVVAHVTRPELRSSEVSNTFYFTFtvrpeAAMKNGFK---IRNVVPATEEEARRI 426
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-94 4.90e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 4.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   1 MEPGSYQLTMSVlmTPDKANFSGNVHGGALLKLLDEVAFACAKRY--AGRYVVTLSVdQVIFREPIHVGELVTFLASVNY 78
Cdd:COG2050  28 VEPGRAVLRLPV--RPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIEL-NINFLRPARLGDRLTAEARVVR 104

                        90
                ....*....|....*.
gi 15597889  79 TGRTSMEVGVKVMTEN 94
Cdd:COG2050 105 RGRRLAVVEVEVTDED 120
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 1-94 1.16e-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: 39.46  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597889   1 MEPGSYQLTMSVlmTPDKANFSGNVHGGALLKLLDEVAFACAKRY--AGRYVVTLSVDqVIFREPIHVGELvTFLASVNY 78
Cdd:cd03443   9 VGPGRVVLRLPV--RPRHLNPGGIVHGGAIATLADTAGGLAALSAlpPGALAVTVDLN-VNYLRPARGGDL-TARARVVK 84

                        90
                ....*....|....*.
gi 15597889  79 TGRTSMEVGVKVMTEN 94
Cdd:cd03443  85 LGRRLAVVEVEVTDED 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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