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Conserved domains on  [gi|499594648|ref|WP_011275382|]
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MULTISPECIES: acyl-CoA thioesterase [Bacteria]

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];
10-155 6.28e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 198.09  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  10 SMSESKSYKAKQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499594648  90 SSMEVCVQIIIEDVLNKERHLAALSFLTFVALDDNGKPVQVPDVYPESKVEKWFYESAPKRVQRRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 6.28e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 198.09  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  10 SMSESKSYKAKQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499594648  90 SSMEVCVQIIIEDVLNKERHLAALSFLTFVALDDNGKPVQVPDVYPESKVEKWFYESAPKRVQRRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 1.58e-46

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: 148.10  E-value: 1.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648   9 KSMSESKSYKAKQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAG 88
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499594648  89 TSSMEVCVQIIIEDVLNKERHLAALSFLTFVALDDNGKPVQVP 131
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
24-132 1.36e-18

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 77.21  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQIIIEDV 103
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499594648 104 LNK---ERHLAALSFLTFVALDDNGKPVQVPD 132
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 2.58e-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: 67.28  E-value: 2.58e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499594648   30 HHTMFGGSLMANIDEIAAITAMKHANA-QVVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQIIIED 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 6.28e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 198.09  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  10 SMSESKSYKAKQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499594648  90 SSMEVCVQIIIEDVLNKERHLAALSFLTFVALDDNGKPVQVPDVYPESKVEKWFYESAPKRVQRRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 1.58e-46

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: 148.10  E-value: 1.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648   9 KSMSESKSYKAKQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAG 88
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499594648  89 TSSMEVCVQIIIEDVLNKERHLAALSFLTFVALDDNGKPVQVP 131
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
24-132 1.36e-18

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 77.21  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQIIIEDV 103
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499594648 104 LNK---ERHLAALSFLTFVALDDNGKPVQVPD 132
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 2.58e-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: 67.28  E-value: 2.58e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499594648   30 HHTMFGGSLMANIDEIAAITAMKHANA-QVVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQIIIED 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PLN02647 PLN02647
acyl-CoA thioesterase
 36-166 1.59e-13

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 67.51  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  36 GSLMANIDEIAAITAMKHANAQ--------VVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQII--IEDVLN 105
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIqpTKDESN 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499594648 106 KERHLAALSFLTFVALD-DNGKPVQVPDVYPESKVEKWFYESAPKRVQRRKDRREESKNTIE 166
Cdd:PLN02647 194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFE 255
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 20-119 8.62e-13

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: 61.34  E-value: 8.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  20 KQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQI 98
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEV 84

                         90       100
                 ....*....|....*....|.
gi 499594648  99 IiedvlNKERHLAALSFLTFV 119
Cdd:cd03440   85 R-----NEDGKLVATATATFV 100
PLN02647 PLN02647
acyl-CoA thioesterase
 24-93 1.74e-06

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 46.71  E-value: 1.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGTSSME 93
Cdd:PLN02647 299 PQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSE 368
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 27-122 2.40e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 44.93  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  27 TNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVqiiieDVLN 105
Cdd:COG2050   44 LNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEARVVRRGRRLAVVEV-----EVTD 118

                         90
                 ....*....|....*..
gi 499594648 106 KERHLAALSFLTFVALD 122
Cdd:COG2050  119 EDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-102 2.64e-06

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: 44.09  E-value: 2.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499594648  27 TNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSyEAMVSYAGTSSMEVCVQIIIED 102
Cdd:cd03443   25 LNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTA-RARVVKLGRRLAVVEVEVTDED 100
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 50-136 8.48e-04

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 37.57  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648  50 AMKHANAQVVTASTdSVDFLRPIKTGDITSYEAMVSYAGTSSMEVCVQIIIEDvlnkERHLAALSFLTFVALD-DNGKPV 128
Cdd:COG0824   49 ELEEEGIGLVVVEA-EIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRAD----DGELLATGETVLVFVDlETGRPV 123


                 ....*...
gi 499594648 129 QVPDVYPE 136
Cdd:COG0824  124 PLPDELRA 131
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 28-121 8.61e-04

Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed uncharacterized domain often found as a standalone protein. The member from Shewanella oneidensis is described from crystallography work as a putative thioesterase because it belongs to the HotDog clan of enzymes. About half of the members of this family are fused to an Acetyltransf_1 domain pfam00583.


Pssm-ID: 430649  Cd Length: 144  Bit Score: 38.00  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594648   28 NHHHTMFGGSLMAnideIAAITA-------MKHA--NAQVVTASTDsVDFLRPIK---------------TGDITSYEAm 83
Cdd:pfam09500  41 NHHGTMFAGSIYT----LATLTGwgllwllLKEAglEGDIVLADGN-IRYLKPVTgdptarvslptpeawSGFLSRLAR- 114

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499594648   84 vsyAGTSSMEVCVQIIIEDVLnkerhlaALSFL-TFVAL 121
Cdd:pfam09500 115 ---GGKARITLEVEIYSGGEL-------AAEFTgRYVVL 143
PRK13339 PRK13339
malate:quinone oxidoreductase; Reviewed
 134-167 2.68e-03

malate:quinone oxidoreductase; Reviewed


Pssm-ID: 183983  Cd Length: 497  Bit Score: 37.37  E-value: 2.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 499594648 134 YPESKVEKWFYESAPKRVQRRKDRREESKNTIEF 167
Cdd:PRK13339 380 YPEARAEDWRLYTAGKRVQVIKDTPEHGKGFIQF 413
 
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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