| IED ID | IndEnz0010001383 |
| Enzyme Type ID | esterase001383 |
| Protein Name |
Peroxisomal acyl-coenzyme A thioester hydrolase 1 EC 3.1.2.2 Peroxisomal long-chain acyl-CoA thioesterase 1 |
| Gene Name | TES1 PTE1 YJR019C J1456 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSASKMAMSNLEKILELVPLSPTSFVTKYLPAAPVGSKGTFGGTLVSQSLLASLHTVPLNFFPTSLHSYFIKGGDPRTKITYHVQNLRNGRNFIHKQVSAYQHDKLIFTSMILFAVQRSKEHDSLQHWETIPGLQGKQPDPHRYEEATSLFQKEVLDPQKLSRYASLSDRFQDATSMSKYVDAFQYGVMEYQFPKDMFYSARHTDELDYFVKVRPPITTVEHAGDESSLHKHHPYRIPKSITPENDARYNYVAFAYLSDSYLLLTIPYFHNLPLYCHSFSVSLDHTIYFHQLPHVNNWIYLKISNPRSHWDKHLVQGKYFDTQSGRIMASVSQEGYVVYGSERDIRAKF |
| Enzyme Length | 349 |
| Uniprot Accession Number | P41903 |
| Absorption | |
| Active Site | ACT_SITE 259; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 282; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 333; /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:10092594}; |
| DNA Binding | |
| EC Number | 3.1.2.2 |
| Enzyme Function | FUNCTION: Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Contributes to growth on fatty acids. {ECO:0000269|PubMed:10092594}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (6); Chain (1); Helix (1); Motif (1) |
| Keywords | 3D-structure;Hydrolase;Peroxisome;Reference proteome;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Up-regulated by oleic acid. {ECO:0000269|PubMed:10092594}. |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10092594}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TBU; |
| Mapped Pubmed ID | 11283351; 12697341; 14690591; 16490786; 16606443; 17028011; 17107617; 18671944; 19536198; 19830908; 20124343; 20489023; 22206997; 23275493; 24997118; |
| Motif | MOTIF 347..349; /note=Microbody targeting signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 40,260 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16645 |
| Cross Reference Brenda | 3.1.2.2;3.1.2.20; |