Detail Information for IndEnz0010000993
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;