OYE2_YEAST
ID OYE2_YEAST Reviewed; 400 AA.
AC Q03558; D3DLC8; E9P8V8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=NADPH dehydrogenase 2 {ECO:0000305|PubMed:7836424};
DE EC=1.6.99.1 {ECO:0000269|PubMed:7836424};
DE AltName: Full=Old yellow enzyme 2 {ECO:0000303|PubMed:8454584};
GN Name=OYE2 {ECO:0000303|PubMed:8454584}; OrderedLocusNames=YHR179W;
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], PROTEIN SEQUENCE OF 2-37, CLEAVAGE OF
RP INITIATOR METHIONINE, MASS SPECTROMETRY, SUBUNIT, AND COFACTOR.
RX PubMed=8454584; DOI=10.1016/s0021-9258(18)53224-5;
RA Stott K., Saito K., Thiels D.J., Massey V.;
RT "Old Yellow Enzyme. The discovery of multiple isozymes and a family of
RT related proteins.";
RL J. Biol. Chem. 268:6097-6106(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
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 [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC STRAIN=RZ49-1;
RX PubMed=7836424; DOI=10.1074/jbc.270.5.1983;
RA Niino Y.S., Chakraborty S., Brown B.J., Massey V.;
RT "A new old yellow enzyme of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:1983-1991(1995).
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 MASS SPECTROMETRY.
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17897954; DOI=10.1074/jbc.m704058200;
RA Odat O., Matta S., Khalil H., Kampranis S.C., Pfau R., Tsichlis P.N.,
RA Makris A.M.;
RT "Old yellow enzymes, highly homologous FMN oxidoreductases with modulating
RT roles in oxidative stress and programmed cell death in yeast.";
RL J. Biol. Chem. 282:36010-36023(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-379, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Flavin-dependent enoate reductase that catalyzes the
CC chemo- and stereoslective hydrogenation of electron-poor alkenes. The
CC enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-
CC unsaturated aldehydes and ketones can act as electron acceptors to
CC complete catalytic turnover. The physiological oxidant remains elusive
CC (By similarity). Has an antioxidant activity, reducing reactive oxygen
CC species (ROS) levels when overexpressed. Formation of OYE2-OYE3
CC heterodimers contribute to the induction of programmed cell death upon
CC oxidative stress (PubMed:17897954). {ECO:0000250|UniProtKB:Q02899,
CC ECO:0000269|PubMed:17897954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC Evidence={ECO:0000269|PubMed:7836424};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000305|PubMed:8454584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for cyclohexenone {ECO:0000269|PubMed:7836424};
CC KM=1.65 mM for oxygen {ECO:0000269|PubMed:7836424};
CC -!- SUBUNIT: Homodimer or heterodimer with OYE3.
CC {ECO:0000269|PubMed:8454584}.
CC -!- INTERACTION:
CC Q03558; P41816: OYE3; NbExp=2; IntAct=EBI-12729, EBI-12734;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Mitochondrion
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:17897954}.
CC -!- MASS SPECTROMETRY: Mass=44886; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8454584};
CC -!- MASS SPECTROMETRY: Mass=44865; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7836424};
CC -!- MISCELLANEOUS: Present with 15100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; L06124; AAA83386.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68024.1; -; Genomic_DNA.
DR EMBL; AY558286; AAS56612.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06872.1; -; Genomic_DNA.
DR PIR; A46009; A46009.
DR RefSeq; NP_012049.1; NM_001179310.1.
DR AlphaFoldDB; Q03558; -.
DR SMR; Q03558; -.
DR BioGRID; 36612; 116.
DR DIP; DIP-213N; -.
DR IntAct; Q03558; 29.
DR MINT; Q03558; -.
DR STRING; 4932.YHR179W; -.
DR iPTMnet; Q03558; -.
DR MaxQB; Q03558; -.
DR PaxDb; Q03558; -.
DR PRIDE; Q03558; -.
DR TopDownProteomics; Q03558; -.
DR EnsemblFungi; YHR179W_mRNA; YHR179W; YHR179W.
DR GeneID; 856584; -.
DR KEGG; sce:YHR179W; -.
DR SGD; S000001222; OYE2.
DR VEuPathDB; FungiDB:YHR179W; -.
DR eggNOG; KOG0134; Eukaryota.
DR GeneTree; ENSGT00940000176560; -.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; Q03558; -.
DR OMA; QPKGHVS; -.
DR BioCyc; MetaCyc:YHR179W-MON; -.
DR BioCyc; YEAST:YHR179W-MON; -.
DR PRO; PR:Q03558; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; Q03558; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Flavoprotein; FMN; Mitochondrion;
KW NADP; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8454584"
FT CHAIN 2..400
FT /note="NADPH dehydrogenase 2"
FT /id="PRO_0000194474"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 38
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 244
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 349
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 90
FT /note="W -> R (in Ref. 4; AAS56612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 45011 MW; 67D4FF141B40324E CRC64;
MPFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RAQHPGNIPN RDWAVEYYAQ
RAQRPGTLII TEGTFPSPQS GGYDNAPGIW SEEQIKEWTK IFKAIHENKS FAWVQLWVLG
WAAFPDTLAR DGLRYDSASD NVYMNAEQEE KAKKANNPQH SITKDEIKQY VKEYVQAAKN
SIAAGADGVE IHSANGYLLN QFLDPHSNNR TDEYGGSIEN RARFTLEVVD AVVDAIGPEK
VGLRLSPYGV FNSMSGGAET GIVAQYAYVL GELERRAKAG KRLAFVHLVE PRVTNPFLTE
GEGEYNGGSN KFAYSIWKGP IIRAGNFALH PEVVREEVKD PRTLIGYGRF FISNPDLVDR
LEKGLPLNKY DRDTFYKMSA EGYIDYPTYE EALKLGWDKN
