ID   EAT2_HANUV              Reviewed;         348 AA.
AC   A0A1E5RIW9;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   23-FEB-2022, entry version 18.
DE   RecName: Full=Ethanol acetyltransferase 2;
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=EAT2; ORFNames=AWRI3580_g2626;
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}.
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DR   EMBL; LPNN01000005; OEJ86816.1; -; Genomic_DNA.
DR   STRING; 29833.A0A1E5RIW9; -.
DR   ESTHER; hanuv-a0a0f4x9n5; ABHD11-Acetyl_transferase.
DR   VEuPathDB; FungiDB:AWRI3580_g2626; -.
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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..348
FT                   /note="Ethanol acetyltransferase 2"
FT                   /id="PRO_0000446179"
FT   DOMAIN          49..305
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        121
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT   ACT_SITE        294
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT   UNSURE          89
FT                   /note="E or Q"
FT                   /evidence="ECO:0000312|EMBL:OEJ86816.1"
SQ   SEQUENCE   348 AA;  39163 MW;  955265417AC20993 CRC64;
     MIFNSLSIKR LSSTXTSLPF KKHAKLNFDL YSPQHSTYGK LPYHCQEPII FLHGIYGYSK
     SFNSDYQQLS NLLHTPIYSV DMRCHGETEN CLPFTYDALA GDLDNFVITH NIKKPSLIGF
     SLGAKLAMLA ILKSPHLYTS GVIVDNVPLK QPRIKPNLTA FGNALRDSVF KSGVKRNDPS
     WISKSFNVMK DVCSDMPANF YLLHNIQPKP SYLKKYSTEE SENSLFCKVP IRELSSHVVE
     NVPDWPEEDL AGVKTDVPIL VVKASTSGFV NEDGVAALXK HFSDFTIVEV AGTHLVMKER
     PQEYISAVGR WFYQQNCKKA AALTKAKKTN DQKITQQPIL SYKKIEIA