IED ID | IndEnz0010000200 |
Enzyme Type ID | esterase000200 |
Protein Name |
Cytosolic acyl coenzyme A thioester hydrolase EC 3.1.2.2 Acyl-CoA thioesterase 7 Brain acyl-CoA hydrolase BACH CTE-IIa CTE-II Long chain acyl-CoA thioester hydrolase |
Gene Name | Acot7 Bach |
Organism | Mus musculus (Mouse) |
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLGHCVTMGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENILTGTKKLTNKATLWYVPLSLKNVDKVLEVPPIVYLRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTEPQP |
Enzyme Length | 381 |
Uniprot Accession Number | Q91V12 |
Absorption | |
Active Site | ACT_SITE 67; /evidence=ECO:0000269|PubMed:17563367; ACT_SITE 256; /evidence=ECO:0000269|PubMed:17563367 |
Activity Regulation | |
Binding Site | |
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:15288813};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:15288813}; 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:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000250|UniProtKB:Q64559}; 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:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:Q64559};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:Q64559}; |
DNA Binding | |
EC Number | 3.1.2.2 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (Probable). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (Probable). May play an important physiological function in brain (Probable). {ECO:0000305|PubMed:15288813}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:15288813}. |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (3); Beta strand (14); Chain (1); Compositional bias (1); Domain (2); Helix (6); Modified residue (3); Mutagenesis (2); Region (1); Sequence conflict (1); Turn (3) |
Keywords | 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Serine esterase |
Interact With | Itself |
Induction | INDUCTION: Up-Regulated in activated macrophages. {ECO:0000269|PubMed:17563367}. |
Subcellular Location | SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm, cytosol {ECO:0000305|PubMed:15288813}.; SUBCELLULAR LOCATION: [Isoform D]: Cytoplasm, cytosol {ECO:0000305|PubMed:15288813}. |
Modified Residue | MOD_RES 169; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154; MOD_RES 199; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154; MOD_RES 284; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (4) |
Cross Reference PDB | 2Q2B; 2V1O; 4ZV3; 6VFY; |
Mapped Pubmed ID | 10725249; 11217851; 12466851; 12520002; 14610273; 14681479; 15226823; 16455042; 16602821; 16615898; 17514357; 17967808; 18324622; 18799693; 19455133; 21267068; 22034435; 23459938; 23649344; 25760036; 26861785; 26930384; 27133129; 28416579; 28705898; 31039008; 31676684; |
Motif | |
Gene Encoded By | |
Mass | 42,537 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for palmitoyl-CoA (isoform A at 30 degrees Celsius) {ECO:0000269|PubMed:15288813}; KM=12 uM for palmitoyl-CoA (isoform D at 30 degrees Celsius) {ECO:0000269|PubMed:15288813}; |
Metal Binding | |
Rhea ID | RHEA:16645; RHEA:16646; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:40059; RHEA:40060; RHEA:30143; RHEA:30144; RHEA:30139; RHEA:30140; RHEA:40139; RHEA:40140 |
Cross Reference Brenda | 3.1.2.2;3.1.2.20; |