EAT1_KLULA
ID EAT1_KLULA Reviewed; 368 AA.
AC Q6CLY8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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; OrderedLocusNames=KLLA0_E24421g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=30054364; DOI=10.1128/aem.01640-18;
RA Kruis A.J., Mars A.E., Kengen S.W.M., Borst J.W., van der Oost J.,
RA Weusthuis R.A.;
RT "Alcohol acetyltransferase Eat1 is located in yeast mitochondria.";
RL Appl. Environ. Microbiol. 84:E01640.1-E01640.11(2018).
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:0000269|PubMed:30054364}.
CC -!- DISRUPTION PHENOTYPE: Reduces ethyl acetate production by at least 80%.
CC {ECO:0000269|PubMed:28356220}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; CR382125; CAH00138.1; -; Genomic_DNA.
DR RefSeq; XP_455051.1; XM_455051.1.
DR AlphaFoldDB; Q6CLY8; -.
DR SMR; Q6CLY8; -.
DR STRING; 28985.XP_455051.1; -.
DR ESTHER; klula-q6cly8; ABHD11-Acetyl_transferase.
DR EnsemblFungi; CAH00138; CAH00138; KLLA0_E24421g.
DR GeneID; 2894336; -.
DR KEGG; kla:KLLA0_E24421g; -.
DR eggNOG; KOG2382; Eukaryota.
DR HOGENOM; CLU_020336_53_0_1; -.
DR InParanoid; Q6CLY8; -.
DR OMA; ACIIDNA; -.
DR BRENDA; 2.3.1.268; 2825.
DR Proteomes; UP000000598; Chromosome E.
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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..368
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446180"
FT DOMAIN 67..171
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 344..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 368 AA; 41851 MW; 8FCEA1F8FCAF6B2F CRC64;
MFLSLRPSLS VSRLAVVRRA YSSPASKKQI NDGLVPLPHK EVIDMAFDLH LPERSVIGKL
PYHSPEPIIF FHGLLGSKRN YKHDCKKLAT ALQTPVYTVD VRNHGSSEHA LPFNYGTLVN
DLVHFIHQHK LGKVNIIGYS LGAKVGMLAC LKHPELFSAA CIIDNAPEPQ PHIKAFLSTL
IKSCVKLLDQ GKVRVDDKLW RHKASESLKR YLPNAGVRNY VLNNIVHNPR VVEYRSPVIN
YDDGLIHFKN PVRHMLDCGV KDVADWPTEE VKDKKFLGPV NFIRATKSAF INPDSLKAIN
SFFPFNNIHE INATHFVLNE RPQEYLRAVI DFFKVTRYQL ENKRNKDPNN YMQTQNSISN
SDTMGQSL
