EAT2_WICAA
ID EAT2_WICAA Reviewed; 341 AA.
AC A0A1E3P8S8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Probable alcohol acetyltransferase;
DE Short=AAT;
DE EC=2.3.1.-;
DE Flags: Precursor;
GN Name=EAT2; ORFNames=WICANDRAFT_48865;
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.
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: Probable alcohol acetyltransferase that uses acetyl-CoA to
CC synthesize acetate esters from various alcohols (Probable). Not
CC involved in the synthesis of ethyl acetate (PubMed:28356220).
CC {ECO:0000269|PubMed:28356220, ECO:0000305|PubMed:28356220}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; KV454208; ODQ61815.1; -; Genomic_DNA.
DR RefSeq; XP_019041022.1; XM_019182618.1.
DR AlphaFoldDB; A0A1E3P8S8; -.
DR SMR; A0A1E3P8S8; -.
DR STRING; 683960.A0A1E3P8S8; -.
DR ESTHER; wicao-a0a1e3p8s8; ABHD11-Acetyl_transferase.
DR EnsemblFungi; ODQ61815; ODQ61815; WICANDRAFT_48865.
DR GeneID; 30199864; -.
DR OrthoDB; 1268438at2759; -.
DR Proteomes; UP000094112; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Hydrolase; Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..341
FT /note="Probable alcohol acetyltransferase"
FT /id="PRO_0000446183"
FT DOMAIN 48..301
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 295
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 341 AA; 38883 MW; 5A152E9F244C0799 CRC64;
MFASRILRNS AQTLKTELPH KETIKMAYDL HKPRSTAIRH LNENPEEPIL FLHGIFGSKK
SYATDSKLIA SSTHTPVYTM DLRNHGETGH AQPFNYETLA QDVKEFCDEH KLDKVKLIGY
SLGAKVSMLT ALQFPNLVKS AVIIDNAPIP QPQIQLFMKQ YIKSMLHVLN ESKIRADDKD
WKNKASAAMK RFLPNGVIRK NLLVNLVNKP PKDFESPVID FEDGYIHFLN PIEQMEEMAV
KDVTDWPVET TKDLKFEGPV KFIKGLQSPF ITDEGMKAIQ THFPNNDFTD VNSNHDILDQ
RPSEYVKIIT DFFNKQRYQS APDDTILGNK TPTPKQTEVS A