ID   YGD9_YEAST              Reviewed;         348 AA.
AC   P53183; D6VUA0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Putative uncharacterized oxidoreductase YGL039W;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=YGL039W;
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 [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   [2]
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   [3]
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   [4]
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).
CC   -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR   EMBL; Z72561; CAA96741.1; -; Genomic_DNA.
DR   EMBL; AY692765; AAT92784.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08061.1; -; Genomic_DNA.
DR   PIR; S64041; S64041.
DR   RefSeq; NP_011476.1; NM_001180904.1.
DR   AlphaFoldDB; P53183; -.
DR   SMR; P53183; -.
DR   BioGRID; 33208; 40.
DR   DIP; DIP-5378N; -.
DR   IntAct; P53183; 9.
DR   MINT; P53183; -.
DR   STRING; 4932.YGL039W; -.
DR   iPTMnet; P53183; -.
DR   MaxQB; P53183; -.
DR   PaxDb; 4932-YGL039W; -.
DR   PeptideAtlas; P53183; -.
DR   TopDownProteomics; P53183; -.
DR   EnsemblFungi; YGL039W_mRNA; YGL039W; YGL039W.
DR   GeneID; 852844; -.
DR   KEGG; sce:YGL039W; -.
DR   AGR; SGD:S000003007; -.
DR   SGD; S000003007; YGL039W.
DR   VEuPathDB; FungiDB:YGL039W; -.
DR   eggNOG; KOG1502; Eukaryota.
DR   GeneTree; ENSGT00940000176317; -.
DR   HOGENOM; CLU_007383_9_2_1; -.
DR   InParanoid; P53183; -.
DR   OMA; KNEECWA; -.
DR   OrthoDB; 1200131at2759; -.
DR   BioCyc; YEAST:G3O-30553-MONOMER; -.
DR   BioGRID-ORCS; 852844; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53183; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53183; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:SGD.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:SGD.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IDA:SGD.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IDA:SGD.
DR   GO; GO:0042180; P:cellular ketone metabolic process; IDA:SGD.
DR   GO; GO:1901426; P:response to furfural; IMP:SGD.
DR   CDD; cd05227; AR_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   PANTHER; PTHR10366:SF853; NADPH-DEPENDENT ALDEHYDE REDUCTASE ARI1-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..348
FT                   /note="Putative uncharacterized oxidoreductase YGL039W"
FT                   /id="PRO_0000215577"
FT   BINDING         41
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
SQ   SEQUENCE   348 AA;  38259 MW;  B3978DCF7DD16CB4 CRC64;
     MTTEKTVVFV SGATGFIALH VVDDLLKTGY KVIGSGRSQE KNDGLLKKFK SNPNLSMEIV
     EDIAAPNAFD KVFQKHGKEI KVVLHIASPV HFNTTDFEKD LLIPAVNGTK SILEAIKNYA
     ADTVEKVVIT SSVAALASPG DMKDTSFVVN EESWNKDTWE SCQANAVSAY CGSKKFAEKT
     AWDFLEENQS SIKFTLSTIN PGFVFGPQLF ADSLRNGINS SSAIIANLVS YKLGDNFYNY
     SGPFIDVRDV SKAHLLAFEK PECAGQRLFL CEDMFCSQEA LDILNEEFPQ LKGKIATGEP
     GSGSTFLTKN CCKCDNRKTK NLLGFQFNKF RDCIVDTASQ LLEVQSKS
//