| IED ID | IndEnz0010000326 |
| Enzyme Type ID | esterase000326 |
| Protein Name |
Acyl-coenzyme A thioesterase 11 Acyl-CoA thioesterase 11 EC 3.1.2.- Acyl-CoA thioester hydrolase 11 Adipose-associated thioesterase Brown fat-inducible thioesterase BFIT Palmitoyl-coenzyme A thioesterase EC 3.1.2.2 |
| Gene Name | ACOT11 BFIT KIAA0707 THEA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MIQNVGNHLRRGLASVFSNRTSRKSALRAGNDSAMADGEGYRNPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASEDLCSEKQWNVCKALATFVARREITKVKLKQITPRTEEEKMEHSVAAERRRMRLVYADTIKDLLANCAIQGDLESRDCSRMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKCCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVAKINSRFGYLQDT |
| Enzyme Length | 607 |
| Uniprot Accession Number | Q8WXI4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 181; /note=Coenzyme A; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:22897136};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:22897136}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:22897136};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:22897136}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:22897136};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:22897136}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+); Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371; Evidence={ECO:0000269|PubMed:22897136};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence={ECO:0000305|PubMed:22897136}; |
| DNA Binding | |
| EC Number | 3.1.2.-; 3.1.2.2 |
| Enzyme Function | FUNCTION: Has an acyl-CoA thioesterase activity with a preference for the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in the mitochondrial beta-oxidation pathway. {ECO:0000269|PubMed:22897136}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:22897136}. |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (12); Binding site (1); Chain (1); Domain (3); Erroneous initiation (1); Helix (5); Modified residue (2); Natural variant (5); Region (3); Sequence conflict (2); Transit peptide (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Mitochondrion;Phosphoprotein;Reference proteome;Repeat;Serine esterase;Transit peptide |
| Interact With | Q53TS8; Q9NP86; Q9NQT4; Q8WXD5; Q8WUI4-6; O14964; O15481; Q13064; P51687 |
| Induction | INDUCTION: By cold exposure and repressed by heat exposure. |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:22897136}. Cytoplasm {ECO:0000269|PubMed:22897136}. |
| Modified Residue | MOD_RES 15; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8VHQ9; MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8VHQ9 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3FO5; 6VVQ; |
| Mapped Pubmed ID | 15638818; 16423998; 16934754; 16940157; 19170545; 19913121; 20235792; 20338778; 20379614; 20470824; 20628086; 22465940; 23700546; 23901139; 24732803; 25002576; 32820071; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,492 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 5 min(-1) for the hydrolysis of hexadecanoyl-CoA (PubMed:22897136). kcat is 3.5 min(-1) for the hydrolysis of tetradecanoyl-CoA (PubMed:22897136). kcat is 2.3 min(-1) for the hydrolysis of dodecanoyl-CoA (PubMed:22897136). kcat is 0.2 min(-1) for the hydrolysis of butanoyl-CoA (PubMed:22897136). {ECO:0000269|PubMed:22897136}; |
| Metal Binding | |
| Rhea ID | RHEA:16645; RHEA:16646; RHEA:40119; RHEA:40120; RHEA:30135; RHEA:30136; RHEA:40111; RHEA:40112 |
| Cross Reference Brenda |