Detail Information for IndEnz0010000125
IED ID IndEnz0010000125
Enzyme Type ID esterase000125
Protein Name Acyl-coenzyme A thioesterase 1
Acyl-CoA thioesterase 1
EC 3.1.2.-
CTE-I
Inducible cytosolic acyl-coenzyme A thioester hydrolase
LACH2
ACH2
Long chain acyl-CoA thioester hydrolase
Long chain acyl-CoA hydrolase
Palmitoyl-coenzyme A thioesterase
EC 3.1.2.2
Gene Name Acot1 Cte1
Organism Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MEATLSLEPAGRSCWDEPLSITVRGLVPEQPVTLRAALRDEKGALFRARALYRADAHGELDLARAPALGGSFTGLEPMGLIWAMEPERPFWRLVKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTICYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVEQKSFIPVERSDTTFLFLVGQDDHNWKSEFYANEISKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLGGKSHGVSPKI
Enzyme Length 419
Uniprot Accession Number O88267
Absorption
Active Site ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 324; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 358; /note=Charge relay system; /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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:7906114}; 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:0000269|PubMed:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:7906114}; 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:0000269|PubMed:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:7906114}; 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:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:Q86TX2}; 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:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000250|UniProtKB:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000250|UniProtKB:Q86TX2}; 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:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:Q86TX2}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000250|UniProtKB:Q86TX2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000250|UniProtKB:Q86TX2};
DNA Binding
EC Number 3.1.2.-; 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. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:7906114}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:7906114}.
nucleotide Binding
Features Active site (3); Chain (1); Modified residue (1); Sequence conflict (8)
Keywords Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Phosphoprotein;Reference proteome;Serine esterase
Interact With
Induction INDUCTION: In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9490035}.
Modified Residue MOD_RES 416; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 23226270; 23994635;
Motif
Gene Encoded By
Mass 46,013
Kinetics
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:40059; RHEA:40060; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148; RHEA:40139; RHEA:40140; RHEA:40131; RHEA:40132; RHEA:40723; RHEA:40724
Cross Reference Brenda 3.1.2.2;3.1.2.20;