NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501333045|ref|WP_012364680|]
View 

MULTISPECIES: acyl-CoA thioesterase [Burkholderia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-131 2.59e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 169.59  E-value: 2.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045   7 ELPAKQPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGN 86
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501333045  87 TSVTVDVEVYAQRMRlMGEIVKVTEATLTYVATGPDRKPRQLPPL 131
Cdd:COG1607   81 TSMEVGVEVWAEDLR-TGERRLVTEAYFTFVAVDEDGKPRPVPPL 124
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-131 2.59e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 169.59  E-value: 2.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045   7 ELPAKQPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGN 86
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501333045  87 TSVTVDVEVYAQRMRlMGEIVKVTEATLTYVATGPDRKPRQLPPL 131
Cdd:COG1607   81 TSMEVGVEVWAEDLR-TGERRLVTEAYFTFVAVDEDGKPRPVPPL 124
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 12-129 7.45e-41

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: 131.92  E-value: 7.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  12 QPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNTSVTV 91
Cdd:cd03442    7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501333045  92 DVEVYAQRMRlMGEIVKVTEATLTYVATGPDRKPRQLP 129
Cdd:cd03442   87 GVEVEAEDPL-TGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
8-130 1.42e-36

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 121.50  E-value: 1.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045   8 LPAKQPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNT 87
Cdd:PRK10694   7 VPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTT 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501333045  88 SVTVDVEVYAQRM--RLMGEIVKVTEATLTYVATGPDRKPRQLPP 130
Cdd:PRK10694  87 SISINIEVWVKKVasEPIGQRYKATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-103 4.02e-14

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: 62.66  E-value: 4.02e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501333045   27 HGDVFGGWIMSQVDIAGSIpASQRANG--RVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNTSVTVDVEVYAQRMRLM 103
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA-AARRLGGsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-131 2.59e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 169.59  E-value: 2.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045   7 ELPAKQPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGN 86
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501333045  87 TSVTVDVEVYAQRMRlMGEIVKVTEATLTYVATGPDRKPRQLPPL 131
Cdd:COG1607   81 TSMEVGVEVWAEDLR-TGERRLVTEAYFTFVAVDEDGKPRPVPPL 124
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 12-129 7.45e-41

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: 131.92  E-value: 7.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  12 QPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNTSVTV 91
Cdd:cd03442    7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501333045  92 DVEVYAQRMRlMGEIVKVTEATLTYVATGPDRKPRQLP 129
Cdd:cd03442   87 GVEVEAEDPL-TGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
8-130 1.42e-36

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 121.50  E-value: 1.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045   8 LPAKQPALRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNT 87
Cdd:PRK10694   7 VPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTT 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501333045  88 SVTVDVEVYAQRM--RLMGEIVKVTEATLTYVATGPDRKPRQLPP 130
Cdd:PRK10694  87 SISINIEVWVKKVasEPIGQRYKATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 27-103 4.02e-14

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: 62.66  E-value: 4.02e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501333045   27 HGDVFGGWIMSQVDIAGSIpASQRANG--RVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNTSVTVDVEVYAQRMRLM 103
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA-AARRLGGsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 15-117 1.94e-12

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: 59.03  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  15 LRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVN-SFVFKQPVFVGDLLSFYATIIRTGNTSVTVDV 93
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90       100
                 ....*....|....*....|....
gi 501333045  94 EVYAQRMRLmgeivkVTEATLTYV 117
Cdd:cd03440   83 EVRNEDGKL------VATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 15-123 1.00e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.64  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  15 LRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVNSFV-FKQPVFVGDLLSFYATIIRTGNTSVTVDV 93
Cdd:COG2050   35 LRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNInFLRPARLGDRLTAEARVVRRGRRLAVVEV 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 501333045  94 EVYAQRMRLmgeivkVTEATLTYVATGPDR 123
Cdd:COG2050  115 EVTDEDGKL------VATATGTFAVLPKRP 138
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 45-130 2.66e-06

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: 43.73  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  45 IPASQRANGRVATVAVNSFV-FKQPVFVGDLLSFYATIIRTGNTSVTVDVEVYAQRmrlMGEIvkVTEATLTYVATGPD- 122
Cdd:COG0824   45 LSYAELEEEGIGLVVVEAEIdYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRAD---DGEL--LATGETVLVFVDLEt 119


                 ....*...
gi 501333045 123 RKPRQLPP 130
Cdd:COG0824  120 GRPVPLPD 127
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 15-117 5.19e-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: 42.54  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  15 LRVVPQPHDANVHGDVFGGWIMSQVDIAGSIPASQRANGRVATVAVN-SFVFKQPVFVGDLLsFYATIIRTGNTSVTVDV 93
Cdd:cd03443   16 LRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLT-ARARVVKLGRRLAVVEV 94

                         90       100
                 ....*....|....*....|....
gi 501333045  94 EVYAQRMRLmgeivkVTEATLTYV 117
Cdd:cd03443   95 EVTDEDGKL------VATARGTFA 112
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
30-114 5.61e-06

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 42.95  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  30 VFGGWIMSqvdIAGSIPASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATII----RTGNTSVTVDVEVYAQRmrlmGE 105
Cdd:COG2030   53 AHGMLTLS---LASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTLRTTVTNQD----GE 125


                 ....*....
gi 501333045 106 IVKVTEATL 114
Cdd:COG2030  126 VVLTGEATV 134
PLN02647 PLN02647
acyl-CoA thioesterase
 20-97 1.15e-04

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 40.16  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501333045  20 QPHDANVHGDVFGGWIMSQV-DIAGSIpASQRANGRVATVAVNSFVFKQPVFVGDLLSFYATIIRTGNTSVT---VDVEV 95
Cdd:PLN02647 298 QPQQRNIHGRIFGGFLMRRAfELAFST-AYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSEqplINVEV 376


                 ..
gi 501333045  96 YA 97
Cdd:PLN02647 377 VA 378
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 55-114 2.86e-03

YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239538 [Multi-domain]  Cd Length: 140  Bit Score: 35.62  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501333045  55 VATVAVNSFVFKQPVFVGDLLSFYATII-------RTGNTSVTVDVEVYAQRmrlmGEIVKVTEATL 114
Cdd:cd03454   75 GGSPGIDELRWPRPVRPGDTLSVEVEVLdkrpsrsRPDRGIVTLRSETLNQR----GEVVLTFEATV 137
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH