ID   EAT1_KLUMD              Reviewed;         363 AA.
AC   W0T4A7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 25.
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=KLMA_10805;
OS   Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS   (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1003335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX   PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA   Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA   Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA   Limtong S., Fujita N., Yamada M.;
RT   "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT   complete genome sequence and transcriptome analyses.";
RL   Biotechnol. Biofuels 8:47-47(2015).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 5422;
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; AP012213; BAO38427.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0T4A7; -.
DR   SMR; W0T4A7; -.
DR   ESTHER; kluma-w0t4a7; ABHD11-Acetyl_transferase.
DR   EnsemblFungi; BAO38427; BAO38427; KLMA_10805.
DR   OrthoDB; 1268438at2759; -.
DR   BRENDA; 2.3.1.268; 1120.
DR   Proteomes; UP000065495; Chromosome 1.
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; Transferase; Transit peptide.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..363
FT                   /note="Ethanol acetyltransferase 1"
FT                   /id="PRO_0000446181"
FT   DOMAIN          65..164
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT   ACT_SITE        313
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ   SEQUENCE   363 AA;  41758 MW;  9A26ECA8D76EB9E9 CRC64;
     MLLAYTVRPS NWSFTRRAYS ATARAFNQQK GLLPLPIKET VDMAYDLHLP ERSVIGKMPY
     HSPEPIIFYH GLLGSKRNYR HDCKKLATAL QTPVYTVDIR NHGSSEHALP FDYNTLVNDL
     VHFAETHSLG KVNLVGYSLG AKVAMLACLK HPERFSAACI IDNSPEEQPH IKPLLTALVK
     SCVKLLDHHN VRADDKLWRH KASEALKKYI PDAGIRYYLL SNIINNPRVV EYRSPVINYD
     DGMLHFKNPV RHMMDFVTKE VAAWPTQELE GKQFLGPVNF IKATRSDFIN PKSLQAINQY
     FPYHNIDEIN ATHFILNERP QEYLRAVTDF FKVTRYQLEK KREQDLAKID QLNASESLKS
     ARD