EAT1_CYBJN
ID EAT1_CYBJN Reviewed; 336 AA.
AC A0A1E4S2P1; A0A0H5CKZ6;
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=BN1211_6162, CYBJADRAFT_189656;
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 / NRRL
RC Y-1542;
RX PubMed=26150016; DOI=10.1016/j.jbiotec.2015.06.423;
RA Rupp O., Brinkrolf K., Buerth C., Kunigo M., Schneider J., Jaenicke S.,
RA Goesmann A., Puehler A., Jaeger K.-E., Ernst J.F.;
RT "The structure of the Cyberlindnera jadinii genome and its relation to
RT Candida utilis analyzed by the occurrence of single nucleotide
RT polymorphisms.";
RL J. Biotechnol. 211:20-30(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 / NRRL
RC Y-1542;
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 2361;
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; CDQK01000007; CEP25159.1; -; Genomic_DNA.
DR EMBL; KV453929; ODV73796.1; -; Genomic_DNA.
DR RefSeq; XP_020070835.1; XM_020217351.1.
DR AlphaFoldDB; A0A1E4S2P1; -.
DR SMR; A0A1E4S2P1; -.
DR STRING; 983966.A0A1E4S2P1; -.
DR ESTHER; cybja-a0a0h5ckz6; ABHD11-Acetyl_transferase.
DR EnsemblFungi; CEP25159; CEP25159; BN1211_6162.
DR EnsemblFungi; ODV73796; ODV73796; CYBJADRAFT_189656.
DR GeneID; 30991747; -.
DR OMA; ACIIDNA; -.
DR OrthoDB; 1268438at2759; -.
DR Proteomes; UP000038830; Unassembled WGS sequence.
DR Proteomes; UP000094389; 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; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..336
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446175"
FT DOMAIN 44..296
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 291
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 336 AA; 38427 MW; B69F8DB7E1A805AD CRC64;
MFPTRVLRST LQKLPHRETV PMAYDLHMPQ RSLFQNLNEK HTEPIVFLHG IFGSKKSYEL
DSKMIAHGTH TPVYTVDIRN HGQTSHAMPF NYDTLAQDVK EFCHVQGLKS VKLVGYSLGA
KISMLAALKY PELVKSAVII DNAPVKQPYI ELYMKQYVKS MLHVLEEAKI KTTDKDWKNK
ASDAMKKFLP NGVIRKNLLV NLVNKKPDGF ESPVVNFDEG LIQFLNPIRQ MEEAAVKDVT
DWPEESTEGL KYNGPVKFIK GLKSPFINEE GMTKIQDIFP NNEFANVNSS HDILDQRPTE
YVKIICDFFN AHRYESAPSN TIIGHKDFKT TIDMRV
