EAT1_WICCF
ID EAT1_WICCF Reviewed; 393 AA.
AC K0KPV8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=BN7_4634;
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10;
RX PubMed=23193139; DOI=10.1128/ec.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Rueckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puehler A., Schaffer S.,
RA Tauch A., Koehler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10;
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; CAIF01000179; CCH45056.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KPV8; -.
DR SMR; K0KPV8; -.
DR STRING; 1206466.K0KPV8; -.
DR ESTHER; wiccf-k0kpv8; ABHD11-Acetyl_transferase.
DR EnsemblFungi; CCH45056; CCH45056; BN7_4634.
DR eggNOG; KOG2382; Eukaryota.
DR HOGENOM; CLU_020336_53_0_1; -.
DR InParanoid; K0KPV8; -.
DR Proteomes; UP000009328; 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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..393
FT /note="Ethanol acetyltransferase 1"
FT /id="PRO_0000446184"
FT DOMAIN 49..151
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 343..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 393 AA; 44775 MW; F9C3DD9FA054D17E CRC64;
MHFTRTLFNQ VASKASRQLP VQKRVQMAYD LHIPNKTVNP NLNIRSHEPI VFVHGIFGSK
KNYRFDCQKI ANVTHTPVYT VDLRNHGQSI HALPFDYETL AQDVADFCED HGLKKVNLIG
YSLGAKICML TMLQNPDLIR SGVIIDNSPI EQPHIEIFLQ MFVKSMIHVL NSTKIEANDS
DWKRKADDAM KRYIPDGGIR KYLLANLINK VPKGYKSPVI DYDDGFIHFQ NPVKHMTEVA
VKNVSAWPTE KVAGKTFEGP IRFIKGTKSA FIDDAGKKAI AGYFPNHSIS EINATHFILN
ERPLEYVRVI CDFIKTERFR SLQEHLRNVE HFSPSEIEAK QAAKHAQQIE ELRKVTSTSE
SSIPHSTQSS EQAFTENIDL ARQEREHQKS VSA
