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Conserved domains on  [gi|446106528|ref|WP_000184383|]
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MULTISPECIES: acyl-CoA thioesterase [Bacilli]

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 6.96e-61

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 185.38  E-value: 6.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  10 SMSESKCYKNRQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446106528  90 SSMEVVVQIRIDDVFNNKHDLAALSYLTFVALDDEGKPKHVPGVYPEDDVEKWFYDTAPQRVERRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 6.96e-61

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 185.38  E-value: 6.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  10 SMSESKCYKNRQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446106528  90 SSMEVVVQIRIDDVFNNKHDLAALSYLTFVALDDEGKPKHVPGVYPEDDVEKWFYDTAPQRVERRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 9.13e-44

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: 141.17  E-value: 9.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528   9 KSMSESKCYKNRQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAG 88
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446106528  89 TSSMEVVVQIRIDDVFNNKHDLAALSYLTFVALDDEGKPKHVP 131
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PLN02647 PLN02647
acyl-CoA thioesterase
 36-166 3.78e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 74.83  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  36 GTLMANIDEIAAITAMKHAGAQ--------VVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSSMEV---VVQIRIDDVf 104
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIqleVIQPTKDES- 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446106528 105 NNKHDLAALSYLTFVALDDE-GKPKHVPGVYPEDDVEKWFYDTAPQRVERRKARRIESKQTIE 166
Cdd:PLN02647 193 NTSDSVALTANFTFVARDSKtGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFE 255
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 4.91e-16

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: 68.82  E-value: 4.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446106528   30 HHTMFGGTLMANIDEIAAITAMKHAGA-QVVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSSMEVVVQIRIDD 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 22-119 2.89e-03

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 35.78  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528   22 VFPQDTNHHHTMFGGTLMANIDEI--AAITAMKHAGAQVVTASTdSVDFLKPIKTGDiLQYVAMVSYAGtsSMEVVVQIR 99
Cdd:TIGR00369  24 VDERTLQPFGSLHGGVSAALADTAgsAAGYLCNSGGQAVVGLEL-NANHLRPAREGK-VRAIAQVVHLG--RQTGVAEIE 99

                          90       100
                  ....*....|....*....|
gi 446106528  100 IddvFNNKHDLAALSYLTFV 119
Cdd:TIGR00369 100 I---VDEQGRLCALSRGTTA 116
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 6.96e-61

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 185.38  E-value: 6.96e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  10 SMSESKCYKNRQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAGT 89
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446106528  90 SSMEVVVQIRIDDVFNNKHDLAALSYLTFVALDDEGKPKHVPGVYPEDDVEKWFYDTAPQRVERRK 155
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 9.13e-44

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: 141.17  E-value: 9.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528   9 KSMSESKCYKNRQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAG 88
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446106528  89 TSSMEVVVQIRIDDVFNNKHDLAALSYLTFVALDDEGKPKHVP 131
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PLN02647 PLN02647
acyl-CoA thioesterase
 36-166 3.78e-16

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 74.83  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  36 GTLMANIDEIAAITAMKHAGAQ--------VVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSSMEV---VVQIRIDDVf 104
Cdd:PLN02647 114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIqleVIQPTKDES- 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446106528 105 NNKHDLAALSYLTFVALDDE-GKPKHVPGVYPEDDVEKWFYDTAPQRVERRKARRIESKQTIE 166
Cdd:PLN02647 193 NTSDSVALTANFTFVARDSKtGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFE 255
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 4.91e-16

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: 68.82  E-value: 4.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446106528   30 HHTMFGGTLMANIDEIAAITAMKHAGA-QVVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSSMEVVVQIRIDD 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
24-131 1.18e-15

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 69.50  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  24 PQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSSMEVVVQIRIDDV 103
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446106528 104 FNN---KHDLAALSYLTFVALDDEGKPKHVP 131
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRALP 130
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 20-119 2.02e-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: 62.88  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  20 RQVFPQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTD-SVDFLKPIKTGDILQYVAMVSYAGTSSMEVVVQI 98
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEV 84

                         90       100
                 ....*....|....*....|.
gi 446106528  99 riddvFNNKHDLAALSYLTFV 119
Cdd:cd03440   85 -----RNEDGKLVATATATFV 100
PLN02647 PLN02647
acyl-CoA thioesterase
 24-161 1.72e-08

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 52.87  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  24 PQDTNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTDSVDFLKPIKTGDILQYVAMVSYAGTSS-------MEVVV 96
Cdd:PLN02647 299 PQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENseqplinVEVVA 378

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446106528  97 -----QIRIDDVFNNkhdlaalSYLTFvALDDEGKPKH---VPGVYPEDDVEkwfydtAPQRVERRKARRIES 161
Cdd:PLN02647 379 hvtrpELRSSEVSNT-------FYFTF-TVRPEAAMKNgfkIRNVVPATEEE------ARRILERMDAEHLVS 437
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 27-124 1.85e-07

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 48.02  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  27 TNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTD-SVDFLKPIKTGDILQYVAMVSYAGTSSmeVVVQIRIddvFN 105
Cdd:COG2050   44 LNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEARVVRRGRRL--AVVEVEV---TD 118

                         90
                 ....*....|....*....
gi 446106528 106 NKHDLAALSYLTFVALDDE 124
Cdd:COG2050  119 EDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-119 5.53e-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: 43.32  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  27 TNHHHTMFGGTLMANIDEIAAITAMKHAGAQVVTASTD-SVDFLKPIKTGDiLQYVAMVSYAGTSSmeVVVQIRIddvFN 105
Cdd:cd03443   25 LNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGD-LTARARVVKLGRRL--AVVEVEV---TD 98

                         90
                 ....*....|....
gi 446106528 106 NKHDLAALSYLTFV 119
Cdd:cd03443   99 EDGKLVATARGTFA 112
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 50-143 2.05e-03

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: 36.80  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528  50 AMKHAGAQVVTASTdSVDFLKPIKTGDILQYVAMVSYAGTSSMEVVVQIRIDDvfnnKHDLAALSYLTFVALD-DEGKPK 128
Cdd:COG0824   49 ELEEEGIGLVVVEA-EIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRAD----DGELLATGETVLVFVDlETGRPV 123

                         90
                 ....*....|....*
gi 446106528 129 HVPgvypeDDVEKWF 143
Cdd:COG0824  124 PLP-----DELRAAL 133
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 22-119 2.89e-03

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 35.78  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106528   22 VFPQDTNHHHTMFGGTLMANIDEI--AAITAMKHAGAQVVTASTdSVDFLKPIKTGDiLQYVAMVSYAGtsSMEVVVQIR 99
Cdd:TIGR00369  24 VDERTLQPFGSLHGGVSAALADTAgsAAGYLCNSGGQAVVGLEL-NANHLRPAREGK-VRAIAQVVHLG--RQTGVAEIE 99

                          90       100
                  ....*....|....*....|
gi 446106528  100 IddvFNNKHDLAALSYLTFV 119
Cdd:TIGR00369 100 I---VDEQGRLCALSRGTTA 116
 
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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