MCFS1_YEAST
ID MCFS1_YEAST Reviewed; 456 AA.
AC Q02891; D6W3S2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Medium-chain fatty acid ethyl ester synthase/esterase 1;
DE AltName: Full=Alcohol O-acetyltransferase;
DE EC=2.3.1.84;
DE EC=3.1.1.-;
DE AltName: Full=Ethyl ester biosynthesis protein 1;
GN Name=EEB1; OrderedLocusNames=YPL095C; ORFNames=LPG13C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
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).
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 573 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; U43281; AAB68204.1; -; Genomic_DNA.
DR EMBL; AY692561; AAT92580.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11338.1; -; Genomic_DNA.
DR PIR; S61971; S61971.
DR RefSeq; NP_015230.1; NM_001183909.1.
DR AlphaFoldDB; Q02891; -.
DR BioGRID; 36086; 76.
DR DIP; DIP-2691N; -.
DR IntAct; Q02891; 2.
DR MINT; Q02891; -.
DR STRING; 4932.YPL095C; -.
DR ESTHER; yeast-MCFS1; abh_upf0017.
DR iPTMnet; Q02891; -.
DR PaxDb; Q02891; -.
DR PRIDE; Q02891; -.
DR EnsemblFungi; YPL095C_mRNA; YPL095C; YPL095C.
DR GeneID; 856010; -.
DR KEGG; sce:YPL095C; -.
DR SGD; S000006016; EEB1.
DR VEuPathDB; FungiDB:YPL095C; -.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR HOGENOM; CLU_032487_1_0_1; -.
DR InParanoid; Q02891; -.
DR OMA; GCCRTKI; -.
DR BioCyc; MetaCyc:G3O-33999-MON; -.
DR BioCyc; YEAST:G3O-33999-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR PRO; PR:Q02891; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02891; protein.
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:0034321; F:alcohol O-octanoyltransferase activity; IDA:SGD.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Hydrolase; Reference proteome; Serine esterase;
KW Transferase.
FT CHAIN 1..456
FT /note="Medium-chain fatty acid ethyl ester
FT synthase/esterase 1"
FT /id="PRO_0000212456"
FT DOMAIN 168..434
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 51724 MW; CABC660FF44A287E CRC64;
MFRSGYYPTV TPSHWGYNGT VKHVLGEKGT KSLAFRDSKR QIPLHEFVTK HVPTLKDGAN
FRLNSLLFTG YLQTLYLSAG DFSKKFQVFY GREIIKFSDG GVCTADWVMP EWEQTYSLNA
EKASFNEKQF SNDEKATHPK GWPRLHPRTR YLSSEELEKC HSKGYSYPLV VVLHGLAGGS
HEPLIRALSE DLSKVGDGKF QVVVLNARGC SRSKVTTRRI FTALHTGDVR EFLNHQKALF
PQRKIYAVGT SFGAAMLTNY LGEEGDNCPL NAAVALSNPW DFVHTWDKLA HDWWSNHIFS
RTLTQFLTRT VKVNMNELQV PENFEVSHKP TVEKPVFYTY TRENLEKAEK FTDILEFDNL
FTAPSMGLPD GLTYYRKASS INRLPNIKIP TLIINATDDP VTGENVIPYK QARENPCVLL
CETDLGGHLA YLDNESNSWL TKQAAEFLGS FDELVL
