EAT1_ERECY
ID EAT1_ERECY Reviewed; 358 AA.
AC G8JVR4;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Ethanol acetyltransferase 1;
DE EC=2.3.1.268;
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; OrderedLocusNames=Ecym_7076;
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582;
RX PubMed=22384365; DOI=10.1534/g3.111.001032;
RA Wendland J., Walther A.;
RT "Genome evolution in the Eremothecium clade of the Saccharomyces complex
RT revealed by comparative genomics.";
RL G3 (Bethesda) 1:539-548(2011).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582;
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:0000250|UniProtKB:A0A1E3P8S6}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; CP002503; AET40929.1; -; Genomic_DNA.
DR RefSeq; XP_003647746.1; XM_003647698.1.
DR AlphaFoldDB; G8JVR4; -.
DR SMR; G8JVR4; -.
DR STRING; 931890.G8JVR4; -.
DR ESTHER; erecy-g8jvr4; ABHD11-Acetyl_transferase.
DR EnsemblFungi; AET40929; AET40929; Ecym_7076.
DR GeneID; 11469347; -.
DR KEGG; erc:Ecym_7076; -.
DR eggNOG; KOG2382; Eukaryota.
DR HOGENOM; CLU_020336_53_0_1; -.
DR InParanoid; G8JVR4; -.
DR OMA; ACIIDNA; -.
DR OrthoDB; 1268438at2759; -.
DR Proteomes; UP000006790; Chromosome 7.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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..358
FT /note="Ethanol acetyltransferase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446177"
FT DOMAIN 59..166
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 358 AA; 40864 MW; 3E35975A7B9CADAF CRC64;
MKMLQGVRAF QKLKKSCAYS TAAKELKPLP VKETVNMAYD LHLPERSVIG KMPYHSPEPI
VFIHGLFGWK RFYRNDCKTL ATALQTPVYA VDMRNHGDTE HAMPFDYNTL MDDLVLLLRK
LDIKKVNLIG YSMGGKMSML TALNYPELVS SACIIDNAPI NQPHISPFLK VFSKSCQHVE
NMKIRATDKE WRSKVAVGLK RYIPNPGIRS YLLQNVSGTP PKKYRSPVID WNDGNVHFVN
PVNHLFQCVV KDASAWPVEQ VAGKQFLGPV NFIRGTKSEF VNADGEKAIA EYFPYHKIQS
INTTHNVLHE RPQEYLRSVI DFFKTTRYVL ERKRDSERVT MIAKPKPLTS SQNAAEYS
