Detail Information for IndEnz0010000328
IED ID IndEnz0010000328
Enzyme Type ID esterase000328
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
mCACH-1
Gene Name Acot12 Cach Cach1
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 MESMVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKPVGKEKVHLKPVLLQTEQEQVEHNLASERRKVRLQHENTFNNIMKESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATPDGLKSVL
Enzyme Length 556
Uniprot Accession Number Q9DBK0
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Allosterically regulated by ATP (activator) and ADP (inhibitor) (By similarity). Cold labile, it dissociates into inactive monomers at low temperature (By similarity). {ECO:0000250|UniProtKB:Q8WYK0, ECO:0000250|UniProtKB:Q99NB7}.
Binding Site BINDING 145; /note=Coenzyme A; /evidence=ECO:0000250
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:0000250|UniProtKB:Q8WYK0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290; Evidence={ECO:0000250|UniProtKB:Q8WYK0}; 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. Preferentially hydrolyzes acetyl-CoA. {ECO:0000250|UniProtKB:Q8WYK0}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q8WYK0}.
nucleotide Binding
Features Binding site (1); Chain (1); Domain (3); Modified residue (4); Region (3)
Keywords Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WYK0}.
Modified Residue MOD_RES 34; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 97; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 160; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 229; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14681479; 16103133; 21267068; 21677750;
Motif
Gene Encoded By
Mass 61,762
Kinetics
Metal Binding
Rhea ID RHEA:20289; RHEA:20290; RHEA:40111; RHEA:40112; RHEA:40115; RHEA:40116
Cross Reference Brenda 3.1.2.1;