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; |