EAT1_WICAA
ID EAT1_WICAA Reviewed; 391 AA.
AC A0A1E3P8S6;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Ethanol acetyltransferase 1;
DE EC=2.3.1.268 {ECO:0000269|PubMed:28356220};
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=WICANDRAFT_27004;
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8;
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 8168 / CBS 5759 / DSM 6766 / JCM 3585 / NCYC 432 / NBRC 10213 /
RC NRRL Y-366;
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. Can also function as a
CC thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as
CC well as esterase hydrolyzing ethyl acetate.
CC {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:0000269|PubMed:28356220};
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:0000269|PubMed:28356220};
CC -!- ACTIVITY REGULATION: By ethanol. Thioesterase and esterase reactions
CC are highly repressed in the presence of high ethanol concentrations.
CC {ECO:0000269|PubMed:28356220}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.12 mM for acetyl-CoA (for acetyl-CoA hydrolase reaction)
CC {ECO:0000269|PubMed:28356220};
CC KM=2.43 mM for ethanol (for alcohol acetyltransferase reaction)
CC {ECO:0000269|PubMed:28356220};
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- BIOTECHNOLOGY: In contrast to S.cerevisiae, W.anomalous is a better
CC ethyl acetate producing yeast. Ethyl acetate is an important industrial
CC compound, used as a chemical solvent applied in the synthesis of
CC biodiesels, paints, adhesives, herbicides and resins. It is also
CC popular because it is relatively non-toxic and fully biodegradable.
CC However, the sustainability of the ethyl acetate industry is severly
CC hampered by the current energy intensive production processes that are
CC based exclusively on petrochemical resources. Ethanol acetyltransferase
CC may be a target for an efficient biobased alternative production
CC process. {ECO:0000305|PubMed:28356220}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; KV454208; ODQ61813.1; -; Genomic_DNA.
DR RefSeq; XP_019041020.1; XM_019181327.1.
DR AlphaFoldDB; A0A1E3P8S6; -.
DR SMR; A0A1E3P8S6; -.
DR STRING; 683960.A0A1E3P8S6; -.
DR ESTHER; wicao-a0a1e3p8s6; ABHD11-Acetyl_transferase.
DR EnsemblFungi; ODQ61813; ODQ61813; WICANDRAFT_27004.
DR GeneID; 30198573; -.
DR OrthoDB; 1268438at2759; -.
DR BioCyc; MetaCyc:MON-20221; -.
DR BRENDA; 2.3.1.268; 1135.
DR Proteomes; UP000094112; 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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..391
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446182"
FT DOMAIN 48..154
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:28356220"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:28356220"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:28356220"
SQ SEQUENCE 391 AA; 45069 MW; 9AAFAF5204824413 CRC64;
MFFTKVLNNQ VANGLKQLPV HKRVQMAYDL HIPNKTVNPN LNIRSHEPIV FVHGIFGSKK
NYRHDCQKIA NVTHTPVYTI DLRNHGQSMH ALPFDYETLA QDVTDFCEDH GLKKVNLIGY
SLGAKICMLT MLQNPDLVRS GVIIDNSPIE QPHIEIFLTQ FIKSMLHVLN STKIRADDKD
WKSKANQAMR RYIPNGGIRD YLLANLINKV PKGYKSPVIN YDDGYIHFQN PVRHMTEVAV
KNVSAWPTEH VKGLKFEGQV RFLKGTKSAF IDEKGLEAIK EYFPNYSLSE LNATHFILNE
RPQEYVKLIC DFIKVNRYKS LQEHIRHVEN FSSAELEARH NAEHERQMEE LRQLTQTTPT
AEQVKTIDNL ASKVDLSATE RQQQQNKEIT V
