IED ID | IndEnz0010001607 |
Enzyme Type ID | esterase001607 |
Protein Name |
Alcohol O-acetyltransferase 2 AATase 2 EC 2.3.1.84 Acetyl-CoA:pregnenolone acetyltransferase APAT |
Gene Name | ATF2 YGR177C G7135 |
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 | MEDIEGYEPHITQELIDRGHARRMGHLENYFAVLSRQKMYSNFTVYAELNKGVNKRQLMLVLKVLLQKYSTLAHTIIPKHYPHHEAYYSSEEYLSKPFPQHDFIKVISHLEFDDLIMNNQPEYREVMEKISEQFKKDDFKVTNRLIELISPVIIPLGNPKRPNWRLICLPGKDTDGFETWKNFVYVTNHCGSDGVSGSNFFKDLALLFCKIEEKGFDYDEEFIEDQVIIDYDRDYTEISKLPKPITDRIDYKPALTSLPKFFLTTFIYEHCNFKTSSESTLTARYSPSSNANASYNYLLHFSTKQVEQIRAQIKKNVHDGCTLTPFIQACFLVALYRLDKLFTKSLLEYGFDVAIPSNARRFLPNDEELRDSYKYGSNVGGSHYAYLISSFDIPEGDNDKFWSLVEYYYDRFLESYDNGDHLIGLGVLQLDFIVENKNIDSLLANSYLHQQRGGAIISNTGLVSQDTTKPYYVRDLIFSQSAGALRFAFGLNVCSTNVNGMNMDMSVVQGTLRDRGEWESFCKLFYQTIGEFASL |
Enzyme Length | 535 |
Uniprot Accession Number | P53296 |
Absorption | |
Active Site | ACT_SITE 189; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P40353; ACT_SITE 193; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P40353 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an aliphatic alcohol = an acetyl ester + CoA; Xref=Rhea:RHEA:17229, ChEBI:CHEBI:2571, ChEBI:CHEBI:47622, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.84; Evidence={ECO:0000269|PubMed:10103065}; |
DNA Binding | |
EC Number | 2.3.1.84 |
Enzyme Function | FUNCTION: Can use acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate (PubMed:12957907, PubMed:12937998, PubMed:16845703, PubMed:17891501). ATF2 seems to play only a minor role in the acetate ester synthesis, compared to ATF1 (PubMed:12957907). Plays an active role in the detoxification hydroxysteroids and possibly certain phytochemicals, in association with the efflux pumps PDR5 and SNQ2 (PubMed:10103065). {ECO:0000269|PubMed:10103065, ECO:0000269|PubMed:12937998, ECO:0000269|PubMed:12957907, ECO:0000269|PubMed:16845703, ECO:0000269|PubMed:17891501}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Region (2); Sequence conflict (1) |
Keywords | Acyltransferase;Direct protein sequencing;Endoplasmic reticulum;Lipid droplet;Membrane;Reference proteome;Transferase |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25093817}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25093817}; Peripheral membrane protein {ECO:0000269|PubMed:25093817}. Note=Traffics to lipid droplets during the stationary phase (PubMed:25093817). {ECO:0000269|PubMed:25093817}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10219999; 11015726; 11283351; 16002012; 16233495; 16233541; 16554755; 18034159; 18309479; 18719252; 19536198; 19804856; 21255318; 21811398; 22940803; 23464572; 24384752; 24520995; 24597968; 25267117; 25880435; 7764365; 9836419; |
Motif | |
Gene Encoded By | |
Mass | 61,898 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.52 uM for pregnenolone {ECO:0000269|PubMed:10103065}; KM=1.1 uM for acetyl-CoA {ECO:0000269|PubMed:10103065}; |
Metal Binding | |
Rhea ID | RHEA:17229 |
Cross Reference Brenda | 2.3.1.84; |