Detail Information for IndEnz0010000341
IED ID IndEnz0010000341
Enzyme Type ID esterase000341
Protein Name Acyl-coenzyme A thioesterase 6
Acyl-CoA thioesterase 6
EC 3.1.2.-
Gene Name ACOT6 C14orf42
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 MAATLILEPAGRCCWDEPLRIAVRGLAPEQPVTLRTSLRDEEGALFRAHARYRADARDELDLERAPALGGSFAGLQPMGLLWALEPEKALVRLVKRDVRTPFAVELEVLDGHDTEPGRLLCLAQNKRDFLRPGVRREPVRAGPVRAALFLPPDEGPFPGIIDLFGSSRGLCEYRASLLAGHGFAVLALAYFRFEDLPEDLNDVHLEYFEEAVDFMLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANTVAPLHYKDMIIPKLVDDLGKVKITKSGFLTFMDTWSNPLEEHNHQSLVPLEKAQVPFLFIVGMDDQSWKSEFYAQIASERLQAHGKERPQIICYPETGHCIDPPYFPPSRASVHAVLGEAIFYGGEPKAHSKAQVDAWQQIQTFFHKHLNGKKSVKHSKI
Enzyme Length 421
Uniprot Accession Number Q3I5F7
Absorption
Active Site ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137; ACT_SITE 360; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + pristanoyl-CoA = 2,6,10,14-tetramethylpentadecanoate + CoA + H(+); Xref=Rhea:RHEA:40415, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250, ChEBI:CHEBI:77268; Evidence={ECO:0000250|UniProtKB:Q32Q92};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40416; Evidence={ECO:0000250|UniProtKB:Q32Q92}; CATALYTIC ACTIVITY: Reaction=H2O + phytanoyl-CoA = 3,7,11,15-tetramethylhexadecanoate + CoA + H(+); Xref=Rhea:RHEA:40419, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57391; Evidence={ECO:0000250|UniProtKB:Q32Q92};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40420; Evidence={ECO:0000250|UniProtKB:Q32Q92};
DNA Binding
EC Number 3.1.2.-
Enzyme Function FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Catalyzes the hydrolysis of phytanoyl-CoA and pristanoyl-CoA, two methyl-branched fatty acids derived from phytol, that enter the body via the diet. {ECO:0000250|UniProtKB:Q32Q92}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q32Q92}.
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Motif (1); Natural variant (1)
Keywords Alternative splicing;Cytoplasm;Hydrolase;Peroxisome;Reference proteome;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Peroxisome {ECO:0000305|PubMed:16940157}. Note=Localization to the peroxisome is uncertain since the potential C-terminal peroxisome targeting signal found in the mouse ortholog is not perfectly conserved. {ECO:0000305|PubMed:16940157}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305|PubMed:16940157}. Note=Recombinant N-terminally GFP-tagged protein localizes to the cytosol. {ECO:0000305|PubMed:16940157}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11673457;
Motif MOTIF 419..421; /note=Peroxisome targeting signal; /evidence=ECO:0000305
Gene Encoded By
Mass 46,789
Kinetics
Metal Binding
Rhea ID RHEA:40415; RHEA:40416; RHEA:40419; RHEA:40420
Cross Reference Brenda 3.1.2.20;