| IED ID | IndEnz0010000993 |
| Enzyme Type ID | esterase000993 |
| Protein Name |
Alcohol O-acetyltransferase 1 AATase 1 EC 2.3.1.84 EC 3.1.2.20 |
| Gene Name | ATF1 YOR377W |
| 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 | MNEIDEKNQAPVQQECLKEMIQNGHARRMGSVEDLYVALNRQNLYRNFCTYGELSDYCTRDQLTLALREICLKNPTLLHIVLPTRWPNHENYYRSSEYYSRPHPVHDYISVLQELKLSGVVLNEQPEYSAVMKQILEEFKNSKGSYTAKIFKLTTTLTIPYFGPTGPSWRLICLPEEHTEKWKKFIFVSNHCMSDGRSSIHFFHDLRDELNNIKTPPKKLDYIFKYEEDYQLLRKLPEPIEKVIDFRPPYLFIPKSLLSGFIYNHLRFSSKGVCMRMDDVEKTDDVVTEIINISPTEFQAIKANIKSNIQGKCTITPFLHVCWFVSLHKWGKFFKPLNFEWLTDIFIPADCRSQLPDDDEMRQMYRYGANVGFIDFTPWISEFDMNDNKENFWPLIEHYHEVISEALRNKKHLHGLGFNIQGFVQKYVNIDKVMCDRAIGKRRGGTLLSNVGLFNQLEEPDAKYSICDLAFGQFQGSWHQAFSLGVCSTNVKGMNIVVASTKNVVGSQESLEELCSIYKALLLGP |
| Enzyme Length | 525 |
| Uniprot Accession Number | P40353 |
| Absorption | |
| Active Site | ACT_SITE 191; /note=Charge relay system; /evidence=ECO:0000305|PubMed:28160314; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000305|PubMed:28160314 |
| Activity Regulation | ACTIVITY REGULATION: Found to be inhibited by cadmium, copper, zinc and mercurium divalent cations and sulfhydryl reagents (PubMed:7764365). Inhibited by the addition of unsaturated fatty acids to the culture (PubMed:7764365). {ECO:0000269|PubMed:7764365}. |
| 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:28160314, ECO:0000269|PubMed:7764365}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20; Evidence={ECO:0000269|PubMed:28160314}; CATALYTIC ACTIVITY: Reaction=3-methylbutanol + acetyl-CoA = 3-methylbutyl acetate + CoA; Xref=Rhea:RHEA:65236, ChEBI:CHEBI:15837, ChEBI:CHEBI:31725, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:7764365};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65237; Evidence={ECO:0000269|PubMed:7764365}; |
| DNA Binding | |
| EC Number | 2.3.1.84; 3.1.2.20 |
| Enzyme Function | FUNCTION: Major alcohol O-acetyltransferase that uses 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:7764365, PubMed:9758847, PubMed:10653746, PubMed:12937998, PubMed:16845703, PubMed:18597084, PubMed:17891501, PubMed:25306884, PubMed:28160314). The alcohol acyltransferase activity is promiscuous with regard to alcohol but relatively specific for acetyl-CoA since ATF1 does not use any other acyl-CoAs (C3, C4, C5, C6, C8, C10, C12) (PubMed:28160314). Acts also as an efficient thioesterase in vitro with specificity towards medium-chain-length acyl-CoAs (PubMed:28160314). In natural environments, the production of aromatic volatile metabolites promotes dispersal through insect vectors (PubMed:25310977). {ECO:0000269|PubMed:10653746, ECO:0000269|PubMed:12937998, ECO:0000269|PubMed:16845703, ECO:0000269|PubMed:17891501, ECO:0000269|PubMed:18597084, ECO:0000269|PubMed:25306884, ECO:0000269|PubMed:25310977, ECO:0000269|PubMed:28160314, ECO:0000269|PubMed:7764365, ECO:0000269|PubMed:9758847}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:7764365}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:7764365}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Mutagenesis (1); Region (2); Sequence conflict (2) |
| Keywords | Acyltransferase;Direct protein sequencing;Endoplasmic reticulum;Hydrolase;Lipid droplet;Membrane;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Expression is repressed both by aeration and by unsaturated fatty acids (PubMed:9055409, PubMed:9675816). Also repressed by heat and ethanol stress (PubMed:14654433). Rapid induction by glucose depends on the cAMP/PKA signaling pathway (PubMed:14654433). Long-term expression requires both carbon and nitrogen sources (PubMed:14654433). The activation of transcription is dependent on RAP1, and the ROX1-TUP1p-SSN6 hypoxic repressor complex is responsible for repression by oxygen (PubMed:10487921). The putative ROX1-binding sequence in the ATF1 promoter is 5'-CCTATTGTTTT-3' and the RAP1-binding sequence is 5'-AACCCAACAAA-3' (PubMed:10487921). {ECO:0000269|PubMed:10487921, ECO:0000269|PubMed:14654433, ECO:0000269|PubMed:9055409, ECO:0000269|PubMed:9675816}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15042596, ECO:0000269|PubMed:25093817, ECO:0000269|PubMed:28497697}. 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 | 11015726; 11133970; 11283351; 12172617; 15766533; 15856224; 16002012; 16233495; 16233541; 17605133; 18034159; 18309479; 18719252; 19536198; 21255318; 22576669; 22940803; 23200656; 23275493; 23464572; 24021962; 24384752; 25267117; 25880435; 27746307; 9787121; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,036 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 mM for acetyl-CoA (for acetyltransferase activity) {ECO:0000269|PubMed:7764365}; KM=29.8 mM for isoamyl alcohol (for acetyltransferase activity) {ECO:0000269|PubMed:7764365}; KM=61 uM for acetyl-CoA (for thioesterase activity) {ECO:0000269|PubMed:28160314}; KM=25 uM for butyryl-CoA (for thioesterase activity) {ECO:0000269|PubMed:28160314}; KM=12 uM for hexanoyl-CoA (for thioesterase activity) {ECO:0000269|PubMed:28160314}; KM=3 uM for octanoyl-CoA (for thioesterase activity) {ECO:0000269|PubMed:28160314}; |
| Metal Binding | |
| Rhea ID | RHEA:17229; RHEA:16781; RHEA:65236; RHEA:65237 |
| Cross Reference Brenda | 2.3.1.84; |