| IED ID | IndEnz0010000327 |
| Enzyme Type ID | esterase000327 |
| Protein Name |
Acetyl-coenzyme A thioesterase EC 3.1.2.1 Acyl-CoA thioester hydrolase 12 Acyl-coenzyme A thioesterase 12 Acyl-CoA thioesterase 12 Cytoplasmic acetyl-CoA hydrolase 1 CACH-1 hCACH-1 START domain-containing protein 15 StARD15 |
| Gene Name | ACOT12 CACH CACH1 STARD15 |
| 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 | MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKPVGKEKIHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTFNNLMKESSKFDDLIFDEEEGAVSTRGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRHINSAFLIYNAADDKENLITFPRIQPISKDDFRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLENPPDDGFVSTF |
| Enzyme Length | 555 |
| Uniprot Accession Number | Q8WYK0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by ADP. Active in the presence of ATP (PubMed:16951743). Cold labile, it dissociates into inactive monomers at low temperature (By similarity). {ECO:0000250|UniProtKB:Q99NB7, ECO:0000269|PubMed:16951743}. |
| Binding Site | BINDING 144; /note=Coenzyme A; /evidence=ECO:0000269|Ref.7 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; Evidence={ECO:0000269|PubMed:16951743};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290; Evidence={ECO:0000305|PubMed:16951743}; 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:0000250|UniProtKB:Q99NB7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence={ECO:0000250|UniProtKB:Q99NB7}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence={ECO:0000250|UniProtKB:Q99NB7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence={ECO:0000250|UniProtKB:Q99NB7}; |
| DNA Binding | |
| EC Number | 3.1.2.1 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:16951743). Preferentially hydrolyzes acetyl-CoA (PubMed:16951743). {ECO:0000269|PubMed:16951743}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16951743}. |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (14); Binding site (1); Chain (1); Domain (3); Helix (9); Modified residue (3); Natural variant (3); Region (3); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Serine esterase |
| Interact With | Itself; O00154-4; P50221; Q6FHY5; P41227; Q9BSU3; Q02548; P26367; Q04864-2; Q96BR9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16951743}. |
| Modified Residue | MOD_RES 33; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0; MOD_RES 159; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0; MOD_RES 228; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3B7K; 4MOB; 4MOC; |
| Mapped Pubmed ID | 11696000; 15638818; 16423998; 16934754; 16940157; 19170545; 20338778; 20379614; 20470824; 22465940; 23700546; 23901139; 24732803; 25002576; 30661930; 31858748; 34285335; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,034 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for acetyl-CoA {ECO:0000269|PubMed:16951743}; Note=kcat is 7000 sec(-1) for the hydrolysis of acetyl-CoA. {ECO:0000269|PubMed:16951743}; |
| Metal Binding | |
| Rhea ID | RHEA:20289; RHEA:20290; RHEA:40111; RHEA:40112; RHEA:40115; RHEA:40116 |
| Cross Reference Brenda | 3.1.2.1; |