IMO32_YEAST
ID IMO32_YEAST Reviewed; 342 AA.
AC P53219; D6VUG6; Q45U54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable alcohol acetyltransferase;
DE Short=AAT;
DE EC=2.3.1.-;
DE AltName: Full=Intermediate cleaved by mitochondrial octapeptidyl aminopeptidase protein 32;
DE Flags: Precursor;
GN Name=IMO32; OrderedLocusNames=YGR031W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [9]
RP PROCESSING OF N-TERMINUS.
RX PubMed=21525245; DOI=10.1091/mbc.e11-02-0169;
RA Vogtle F.N., Prinz C., Kellermann J., Lottspeich F., Pfanner N.,
RA Meisinger C.;
RT "Mitochondrial protein turnover: role of the precursor intermediate
RT peptidase Oct1 in protein stabilization.";
RL Mol. Biol. Cell 22:2135-2143(2011).
RN [10]
RP FUNCTION.
RC STRAIN=CEN.PK2-1D;
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:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- PTM: Processed by both the mitochondrial processing peptidase (MPP) and
CC the mitochondrial octapeptidyl aminopeptidase (OCT1).
CC -!- MISCELLANEOUS: Present with 7400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: The gene contains the nested antisense gene NAG1.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; DQ115390; AAZ22445.1; -; Genomic_DNA.
DR EMBL; Z72816; CAA97019.1; -; Genomic_DNA.
DR EMBL; AY557770; AAS56096.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08127.1; -; Genomic_DNA.
DR PIR; S64322; S64322.
DR RefSeq; NP_011545.1; NM_001181160.1.
DR AlphaFoldDB; P53219; -.
DR SMR; P53219; -.
DR BioGRID; 33276; 43.
DR DIP; DIP-5604N; -.
DR IntAct; P53219; 3.
DR MINT; P53219; -.
DR STRING; 4932.YGR031W; -.
DR ESTHER; yeast-yg1l; ABHD11-Acetyl_transferase.
DR MaxQB; P53219; -.
DR PaxDb; P53219; -.
DR PRIDE; P53219; -.
DR EnsemblFungi; YGR031W_mRNA; YGR031W; YGR031W.
DR GeneID; 852919; -.
DR KEGG; sce:YGR031W; -.
DR SGD; S000003263; IMO32.
DR VEuPathDB; FungiDB:YGR031W; -.
DR eggNOG; KOG2382; Eukaryota.
DR GeneTree; ENSGT00390000015880; -.
DR HOGENOM; CLU_020336_53_0_1; -.
DR InParanoid; P53219; -.
DR OMA; MMYFARK; -.
DR BioCyc; YEAST:G3O-30754-MON; -.
DR PRO; PR:P53219; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53219; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
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..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:21525245"
FT PROPEP 39..46
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:21525245"
FT /id="PRO_0000410798"
FT CHAIN 47..342
FT /note="Probable alcohol acetyltransferase"
FT /id="PRO_0000202791"
FT DOMAIN 75..326
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
FT ACT_SITE 319
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:A0A1E3P8S6"
SQ SEQUENCE 342 AA; 38511 MW; C6F588A8DDDCA351 CRC64;
MMILGKAGIL AQYGTIYVRQ NTIRNNLSSC IFKQSLCAFH SLAKVLQQKQ VPLDLSYDII
KRDAVKTGDE GKPRPPIIIL HGLFGNKLNN RSIGRNLNKK LGRDVYLLDL RNHGSSPHSS
VHNYEVMSED VKHFITKHEL NTNGGPIIIG HSMGGKVAMM LVLKNPQLCS MLVCIENAPV
SLRPNAEFVE YIKALMEIVN DKGKTIRTLK QADEHLAERI GGNELVRRFL LTALKKVKMD
NSSSVSSYTF EERIPLATLK DAIVKGEIAA WPLDPARERW TRPALFIRAT QSHYVVDEYL
PIIGAFFPRF ETRDIDAGHW VNAEKPGECA ESIVDFVERH ED
