ID   MCFS2_YEAST             Reviewed;         451 AA.
AC   P38295; D6VQH2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Medium-chain fatty acid ethyl ester synthase/esterase 2;
DE   AltName: Full=Alcohol O-acetyltransferase;
DE            EC=2.3.1.84;
DE            EC=3.1.1.-;
DE   AltName: Full=Ethanol hexanoyl transferase 1;
GN   Name=EHT1; OrderedLocusNames=YBR177C; ORFNames=YBR1239;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
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   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=16361250; DOI=10.1074/jbc.m512028200;
RA   Saerens S.M.G., Verstrepen K.J., Van Laere S.D., Voet A.R., Van Dijck P.,
RA   Delvaux F.R., Thevelein J.M.;
RT   "The Saccharomyces cerevisiae EHT1 and EEB1 genes encode novel enzymes with
RT   medium-chain fatty acid ethyl ester synthesis and hydrolysis capacity.";
RL   J. Biol. Chem. 281:4446-4456(2006).
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-114, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Displays enzymatic activity both for medium-chain fatty acid
CC       (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA
CC       are toxic for yeast and this enzyme could thus be involved in their
CC       detoxification by esterification. {ECO:0000269|PubMed:16361250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an aliphatic alcohol = an acetyl ester + CoA;
CC         Xref=Rhea:RHEA:17229, ChEBI:CHEBI:2571, ChEBI:CHEBI:47622,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.84;
CC   -!- MISCELLANEOUS: Present with 2550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC       family. {ECO:0000305}.
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DR   EMBL; Z36046; CAA85138.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07292.1; -; Genomic_DNA.
DR   PIR; S46048; S46048.
DR   RefSeq; NP_009736.3; NM_001178525.3.
DR   AlphaFoldDB; P38295; -.
DR   BioGRID; 32876; 149.
DR   IntAct; P38295; 23.
DR   MINT; P38295; -.
DR   STRING; 4932.YBR177C; -.
DR   ESTHER; yeast-MCFS2; abh_upf0017.
DR   iPTMnet; P38295; -.
DR   MaxQB; P38295; -.
DR   PaxDb; 4932-YBR177C; -.
DR   PeptideAtlas; P38295; -.
DR   EnsemblFungi; YBR177C_mRNA; YBR177C; YBR177C.
DR   GeneID; 852476; -.
DR   KEGG; sce:YBR177C; -.
DR   AGR; SGD:S000000381; -.
DR   SGD; S000000381; EHT1.
DR   VEuPathDB; FungiDB:YBR177C; -.
DR   eggNOG; KOG1838; Eukaryota.
DR   GeneTree; ENSGT00950000182902; -.
DR   HOGENOM; CLU_032487_1_0_1; -.
DR   InParanoid; P38295; -.
DR   OMA; HTMDIRE; -.
DR   OrthoDB; 1655372at2759; -.
DR   BioCyc; MetaCyc:YBR177C-MONOMER; -.
DR   BioCyc; YEAST:YBR177C-MONOMER; -.
DR   Reactome; R-SCE-1483191; Synthesis of PC.
DR   BioGRID-ORCS; 852476; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38295; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38295; Protein.
DR   GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR   GO; GO:0004026; F:alcohol O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034319; F:alcohol O-butanoyltransferase activity; IDA:SGD.
DR   GO; GO:0017171; F:serine hydrolase activity; HDA:SGD.
DR   GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:SGD.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR   GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IDA:SGD.
DR   GO; GO:0051793; P:medium-chain fatty acid catabolic process; IMP:SGD.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000952; AB_hydrolase_4_CS.
DR   InterPro; IPR012020; ABHD4.
DR   PANTHER; PTHR10794; ABHYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10794:SF44; MEDIUM-CHAIN FATTY ACID ETHYL ESTER SYNTHASE_ESTERASE 1-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01133; UPF0017; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Hydrolase; Isopeptide bond; Reference proteome;
KW   Serine esterase; Transferase; Ubl conjugation.
FT   CHAIN           1..451
FT                   /note="Medium-chain fatty acid ethyl ester
FT                   synthase/esterase 2"
FT                   /id="PRO_0000212454"
FT   DOMAIN          166..430
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        247
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        395
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        423
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        114
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   451 AA;  51255 MW;  48D48ABF4CC97029 CRC64;
     MSEVSKWPAI NPFHWGYNGT VSHIVGENGS IKLHLKDNKE QVDFDEFANK YVPTLKNGAQ
     FKLSPYLFTG ILQTLYLGAA DFSKKFPVFY GREIVKFSDG GVCTADWLID SWKKDYEFDQ
     STTSFDKKKF DKDEKATHPE GWPRLQPRTR YLKDNELEEL REVDLPLVVI LHGLAGGSHE
     PIIRSLAENL SRSGRFQVVV LNTRGCARSK ITTRNLFTAY HTMDIREFLQ REKQRHPDRK
     LYAVGCSFGA TMLANYLGEE GDKSPLSAAA TLCNPWDLLL SAIRMSQDWW SRTLFSKNIA
     QFLTRTVQVN MGELGVPNGS LPDHPPTVKN PSFYMFTPEN LIKAKSFKST REFDEVYTAP
     ALGFPNAMEY YKAASSINRV DTIRVPTLVI NSRDDPVVGP DQPYSIVEKN PRILYCRTDL
     GGHLAYLDKD NNSWATKAIA EFFTKFDELV V
//