Detail Information for IndEnz0010001572
IED ID IndEnz0010001572
Enzyme Type ID esterase001572
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 Thea
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 MIQNVGNHLRRGFASMFSNRTSRKSISHPESGDPPTMAEGEGYRNPTEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSEDLCSEKQWSVCKALATFVAHRELSKVKLKQVIPLTEEEKTEHGVAAERRRMRLVYADTIKDLLTHCVIQDDLDKDCSNMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETQRRHINSAFMTFVVLDKDDQPQKLPWIRPQPGEGERRYREASARKKIRLDRKYLVSCKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEDFLSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDNRNDLAPSLQTL
Enzyme Length 594
Uniprot Accession Number Q8VHQ9
Absorption
Active Site
Activity Regulation
Binding Site BINDING 183; /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:0000250|UniProtKB:Q8WXI4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000250|UniProtKB:Q8WXI4}; 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:Q8WXI4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:Q8WXI4}; 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:Q8WXI4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000250|UniProtKB:Q8WXI4}; 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:Q8WXI4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence={ECO:0000250|UniProtKB:Q8WXI4};
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:0000250|UniProtKB:Q8WXI4}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q8WXI4}.
nucleotide Binding
Features Binding site (1); Chain (1); Domain (3); Modified residue (2); Region (4); Transit peptide (1)
Keywords Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Mitochondrion;Phosphoprotein;Reference proteome;Repeat;Serine esterase;Transit peptide
Interact With
Induction INDUCTION: By cold exposure and repressed by heat exposure.
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8WXI4}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXI4}.
Modified Residue MOD_RES 15; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 12693553; 16103133; 16141072; 21677750; 22427358; 22993230; 27110486; 29208699; 29688375; 34108467;
Motif
Gene Encoded By
Mass 67,355
Kinetics
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:40119; RHEA:40120; RHEA:30135; RHEA:30136; RHEA:40111; RHEA:40112
Cross Reference Brenda 3.1.2.20;