IED Industry Enzyme Database

Detail Information for IndEnz0010000045
IED ID IndEnz0010000045
Enzyme Type ID esterase000045
Protein Name Cytosolic acyl coenzyme A thioester hydrolase
EC 3.1.2.2
Acyl-CoA thioesterase 7
Brain acyl-CoA hydrolase
BACH
hBACH
CTE-IIa
CTE-II
Long chain acyl-CoA thioester hydrolase
Gene Name ACOT7 BACH
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 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP
Enzyme Length 380
Uniprot Accession Number O00154
Absorption
Active Site ACT_SITE 66; /evidence=ECO:0000250; ACT_SITE 255; /evidence=ECO:0000250
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:10578051};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:10578051}; 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:0000305|PubMed:10578051};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000305|PubMed:10578051}; 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:0000305|PubMed:10578051};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:10578051}; 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:0000305|PubMed:10578051};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:10578051}; 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 + 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};
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 (PubMed:10578051). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (PubMed:10578051). May play an important physiological function in brain (PubMed:10578051). {ECO:0000269|PubMed:10578051}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:10578051}.
nucleotide Binding
Features Active site (2); Alternative sequence (7); Beta strand (6); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Helix (4); Modified residue (3); Region (1); Sequence conflict (3)
Keywords 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Mitochondrion;Reference proteome;Repeat;Serine esterase
Interact With Q01484; Q13554; Q9HCK8; Q13618; Q06787; V9HW27; P43360; Q9NVV9; Q9UMX0; Q9UMX0-2; Q8WYK0; O95429; Q13554-3; Q15038; P32321; Q9H0I2; P43357; P43360; Q14863; Q9H0A9-2; Q9NVV9; Q9UMX0; Q9UHD9; Q04323-2; Q7Z4V0
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion {ECO:0000269|PubMed:12435388}.
Modified Residue MOD_RES 168; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 198; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 283; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2QQ2;
Mapped Pubmed ID 11696000; 15638818; 16423998; 16713569; 16934754; 16940157; 19170545; 19305408; 19851296; 20338778; 20470824; 20711500; 21044950; 22465940; 23700546; 23901139; 24412244; 24502978; 24732803; 25002576; 25416956; 25609649; 26752685;
Motif
Gene Encoded By
Mass 41,796
Kinetics
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:30143; RHEA:30144; RHEA:30135; RHEA:30136; RHEA:40139; RHEA:40140; RHEA:40119; RHEA:40120; RHEA:40059; RHEA:40060; RHEA:30139; RHEA:30140
Cross Reference Brenda 3.1.2.2;3.1.2.20;