EAT1_YEAST
ID EAT1_YEAST Reviewed; 328 AA.
AC P53208; D6VUF1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ethanol acetyltransferase 1;
DE EC=2.3.1.268 {ECO:0000269|PubMed:28356220};
DE AltName: Full=Acetyl-CoA hydrolase;
DE EC=3.1.2.1;
DE AltName: Full=Acetyl-CoA thioesterase;
DE AltName: Full=Alcohol acetyltransferase;
DE Short=AAT;
DE AltName: Full=Ethyl acetate esterase;
DE EC=3.1.1.-;
GN Name=EAT1 {ECO:0000303|PubMed:28356220};
GN OrderedLocusNames=YGR015C {ECO:0000312|SGD:S000003247};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=CEN.PK2-1D;
RX PubMed=28356220; DOI=10.1016/j.ymben.2017.03.004;
RA Kruis A.J., Levisson M., Mars A.E., van der Ploeg M., Garces Daza F.,
RA Ellena V., Kengen S.W.M., van der Oost J., Weusthuis R.A.;
RT "Ethyl acetate production by the elusive alcohol acetyltransferase from
RT yeast.";
RL Metab. Eng. 41:92-101(2017).
CC -!- FUNCTION: Alcohol acetyltransferase that catalyzes the synthesis of
CC ethyl acetate from ethanol and acetyl-CoA (PubMed:28356220). Can also
CC function as a thioesterase by hydrolyzing acetyl-CoA in the absence of
CC ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity).
CC {ECO:0000250|UniProtKB:A0A1E3P8S6, ECO:0000269|PubMed:28356220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ethanol = CoA + ethyl acetate;
CC Xref=Rhea:RHEA:55972, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.268;
CC Evidence={ECO:0000269|PubMed:28356220};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC Evidence={ECO:0000250|UniProtKB:A0A1E3P8S6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethyl acetate + H2O = acetate + ethanol + H(+);
CC Xref=Rhea:RHEA:58148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:27750, ChEBI:CHEBI:30089;
CC Evidence={ECO:0000250|UniProtKB:A0A1E3P8S6};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Reduces ethyl acetate production by at least 50%.
CC {ECO:0000269|PubMed:28356220}.
CC -!- BIOTECHNOLOGY: S.cerevisiae produces only trace amounts of ethyl
CC acetate. These traces help S.cerevisiae disseminate in the environment
CC by attracting fruit flies. However, as ethyl acetate is a key flavor
CC compound and the most abundant ester in wine and beer, ethyl acetate-
CC producting genes such as ethanol acetyltransferase are relevant for the
CC fermented foods and beverages industry. {ECO:0000305|PubMed:28356220}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Z72800; CAA96998.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08112.1; -; Genomic_DNA.
DR PIR; S64306; S64306.
DR RefSeq; NP_011529.1; NM_001181144.1.
DR AlphaFoldDB; P53208; -.
DR SMR; P53208; -.
DR BioGRID; 33258; 22.
DR IntAct; P53208; 1.
DR MINT; P53208; -.
DR STRING; 4932.YGR015C; -.
DR ESTHER; yeast-yg19; ABHD11-Acetyl_transferase.
DR PaxDb; P53208; -.
DR PRIDE; P53208; -.
DR EnsemblFungi; YGR015C_mRNA; YGR015C; YGR015C.
DR GeneID; 852898; -.
DR KEGG; sce:YGR015C; -.
DR SGD; S000003247; EAT1.
DR VEuPathDB; FungiDB:YGR015C; -.
DR eggNOG; KOG2382; Eukaryota.
DR HOGENOM; CLU_020336_53_0_1; -.
DR InParanoid; P53208; -.
DR OMA; KPYDYIT; -.
DR BioCyc; YEAST:G3O-30742-MON; -.
DR BRENDA; 2.3.1.268; 984.
DR Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR PRO; PR:P53208; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53208; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016453; F:C-acetyltransferase activity; IDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..328
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000202782"
FT DOMAIN 39..309
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 115
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 328 AA; 37937 MW; C409FA9444671CF2 CRC64;
MSRLAHNKAL PYKIIVDLSF HRTRLPSDVS SLIKFEQRPA IINIHGLLGS HVMFHSLNKL
LSRKLDADIF SVDVRNHGIS PKAIPYDYTT LTNDLIYFIE THIGLERPIY LLGFSMGGKI
ALLTTLYKNI NIRKCISIDL PPYETPELDP MILQNYDLIM RIIRRDVKIL RGSPSWQKKV
LELFKSLECN KRKCGGAVAL YFANGFLSVK SNNVHQAQLH YEQQQHDPYI NYSMPLSSMP
NLLDEVKKWP DLSNQRDFFQ KGTASRKVLF MKGLQSNFIN NDYSLLRYNF PCADVREFNT
GHNLLLENPE DSFKCILNFF AEETLDFE
