EAT1_HANUV
ID EAT1_HANUV Reviewed; 334 AA.
AC A0A1E5RUL9;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 19.
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.-;
DE Flags: Precursor;
GN Name=EAT1; ORFNames=AWRI3580_g1230;
OS Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=29833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3580;
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CECT 11105;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPNN01000003; OEJ90549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5RUL9; -.
DR SMR; A0A1E5RUL9; -.
DR STRING; 29833.A0A1E5RUL9; -.
DR ESTHER; hanuv-a0a1e5rul9; ABHD11-Acetyl_transferase.
DR VEuPathDB; FungiDB:AWRI3580_g1230; -.
DR OrthoDB; 1268438at2759; -.
DR Proteomes; UP000095358; Unassembled WGS sequence.
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; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..334
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446178"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 334 AA; 37862 MW; 00D6CFBB3805703C CRC64;
MFASNVVVLN KRSIRFIQTQ LPVKATVDMK FDLHLPKRSV IGKLPYHVEE PIVFVHGLFG
SKKNYFNDCE KLSNLLQTPI YTIDFRNHGE TEHAMPFDYE TLTNDLIHFV EKHNLKNPSL
IGYSLGAKVS MLALLKQPSL FKSAMIIDNS PVVQPEIVPF LKVFRKACVE TVNKAGIRAD
DKDYRAKANQ YMSKFIPNAG IKGYLLQNCI NKPPKNPSPV INYNDGMIHW KNPVNHMANV
SEENVADWPT IPEGIKFNGP VGFLRGTKSD FVLQKGRDAI AKLFPNNRIF DINATHFILN
ERPSEYVGIV ADWFKTGRHD VEKLAAKKAK NAQL
