EAT1_CYBFA
ID EAT1_CYBFA Reviewed; 335 AA.
AC A0A061B0Q2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
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; ORFNames=BON22_2185, CYFA0S_05e01970g;
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJS4271;
RX PubMed=25103752; DOI=10.1128/genomea.00638-14;
RA Freel K.C., Sarilar V., Neuveglise C., Devillers H., Friedrich A.,
RA Schacherer J.;
RT "Genome sequence of the yeast Cyberlindnera fabianii (Hansenula
RT fabianii).";
RL Genome Announc. 2:E00638-E00638(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65;
RX PubMed=28385833; DOI=10.1128/genomea.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CBS 5640;
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; LK052890; CDR40570.1; -; Genomic_DNA.
DR EMBL; MPUK01000003; ONH67980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061B0Q2; -.
DR SMR; A0A061B0Q2; -.
DR STRING; 36022.A0A061B0Q2; -.
DR ESTHER; cybfa-a0a061b0q2; ABHD11-Acetyl_transferase.
DR EnsemblFungi; CDR40570; CDR40570; CYFA0S_05e01970g.
DR VEuPathDB; FungiDB:BON22_2185; -.
DR OMA; ACIIDNA; -.
DR OrthoDB; 1268438at2759; -.
DR PhylomeDB; A0A061B0Q2; -.
DR Proteomes; UP000189513; 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 Hydrolase; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..335
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446173"
FT DOMAIN 48..300
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"
SQ SEQUENCE 335 AA; 38016 MW; D901472DB2BA60DF CRC64;
MFKPTRVLKS SQPILNSLPH AETVKMAYDL HLPKKTLHQN MNITSDEPIV FVHGIFGSKK
SYATDSKLIA NGTHSPVYTI DLRNHGETGH AQPFNYDTLV QDIKEFCSTH NLSNIKLVGY
SLGAKVSMLA ALRLPELVKS AVIIDNAPIK QPYIESYMKQ YIKSMLHVDD AKISTTDKDW
KRKASEAMKR YMPNATVRKN LLVNLVNKKP EGFESPAIDF ENGNIQFLNP IKHMEEMAVK
DVSDWPVEST EGLKFDGPVK FIRGLKSPFI SPEGFKKINE HFPKNEFYDV NSAHDILDQR
PSEYVKVICD FFNLQRYNSA PAHTVLGHKA PEMRV
