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Conserved domains on  [gi|501231842|ref|WP_012274860|]
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MULTISPECIES: acyl-CoA thioesterase [Gammaproteobacteria]

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];
9-131 2.35e-47

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 149.17  E-value: 2.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   9 PIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGR 88
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501231842  89 SSIQMMVEVWSDDPLSSEWRKVTEAAFVFVAIDGSGRTRSVPR 131
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
9-131 2.35e-47

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 149.17  E-value: 2.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   9 PIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGR 88
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501231842  89 SSIQMMVEVWSDDPLSSEWRKVTEAAFVFVAIDGSGRTRSVPR 131
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-130 4.04e-42

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: 135.39  E-value: 4.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   9 PIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGR 88
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501231842  89 SSIQMMVEVWSDDPLSSEWRKVTEAAFVFVAIDGSGRTRSVP 130
Cdd:cd03442   82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
4-130 1.22e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 124.20  E-value: 1.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   4 LEQEDPIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQT 83
Cdd:PRK10694   1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501231842  84 LEIGRSSIQMMVEVW----SDDPLSSEWRkVTEAAFVFVAIDGSGRTRSVP 130
Cdd:PRK10694  81 VKTGTTSISINIEVWvkkvASEPIGQRYK-ATEALFTYVAVDPEGKPRALP 130
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-102 1.82e-13

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: 61.12  E-value: 1.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501231842   29 FGDIFGGWLVAQMDLAGTAMASRVAGG-RVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGRSSIQMMVEVWSDDP 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
9-131 2.35e-47

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 149.17  E-value: 2.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   9 PIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGR 88
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501231842  89 SSIQMMVEVWSDDPLSSEWRKVTEAAFVFVAIDGSGRTRSVPR 131
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-130 4.04e-42

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: 135.39  E-value: 4.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   9 PIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGR 88
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501231842  89 SSIQMMVEVWSDDPLSSEWRKVTEAAFVFVAIDGSGRTRSVP 130
Cdd:cd03442   82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
4-130 1.22e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 124.20  E-value: 1.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   4 LEQEDPIPQGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAIDRMAFLVPVAVGAQLSFYTQT 83
Cdd:PRK10694   1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501231842  84 LEIGRSSIQMMVEVW----SDDPLSSEWRkVTEAAFVFVAIDGSGRTRSVP 130
Cdd:PRK10694  81 VKTGTTSISINIEVWvkkvASEPIGQRYK-ATEALFTYVAVDPEGKPRALP 130
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-102 1.82e-13

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: 61.12  E-value: 1.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501231842   29 FGDIFGGWLVAQMDLAGTAMASRVAGG-RVATVAIDRMAFLVPVAVGAQLSFYTQTLEIGRSSIQMMVEVWSDDP 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 17-118 2.41e-10

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: 53.63  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842  17 LQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAID-RMAFLVPVAVGAQLSFYTQTLEIGRSSIQMMV 95
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90       100
                 ....*....|....*....|...
gi 501231842  96 EVWSDDPlssewRKVTEAAFVFV 118
Cdd:cd03440   83 EVRNEDG-----KLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 2-101 9.27e-07

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: 9.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231842   2 IELEQEDPipqGDLALQITALPRETNGFGDIFGGWLVAQMDLAGTAMASRVAGGRVATVAID-RMAFLVPVAVGAQLSFY 80
Cdd:COG2050   23 IELVEVEP---GRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAE 99

                         90       100
                 ....*....|....*....|.
gi 501231842  81 TQTLEIGRSSIQMMVEVWSDD 101
Cdd:COG2050  100 ARVVRRGRRLAVVEVEVTDED 120
 
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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