OYE3_YEAST
ID OYE3_YEAST Reviewed; 400 AA.
AC P41816; D6W3J7; E9P937;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=NADPH dehydrogenase 3 {ECO:0000305|PubMed:7836424};
DE EC=1.6.99.1 {ECO:0000269|PubMed:7836424};
DE AltName: Full=Old yellow enzyme 3 {ECO:0000303|PubMed:7836424};
GN Name=OYE3 {ECO:0000303|PubMed:7836424}; OrderedLocusNames=YPL171C;
GN ORFNames=P2291;
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], CATALYTIC ACTIVITY, AND MASS
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [6]
RP PROTEIN SEQUENCE OF 2-31, CLEAVAGE OF INITIATOR METHIONINE, SUBUNIT, AND
RP COFACTOR.
RC STRAIN=RZ49-1;
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 [7]
RP PARTIAL PROTEIN SEQUENCE.
RA Brown B.J., Massey V.;
RL (In) Yagi K. (eds.);
RL Flavin and Flavoproteins 1993, pp.391-394, Walter de Gruyter, Berlin
RL (1994).
RN [8]
RP FUNCTION.
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 [9] {ECO:0007744|PDB:5V4P}
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE
RP ANALOG.
RA Stewart J., Powell R.W. III;
RT "Saccharomyces cerevisiae OYE 3 soaked with p-hydroxybenzaldehyde.";
RL Submitted (MAR-2017) to the PDB data bank.
RN [10] {ECO:0007744|PDB:5V4V}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FMN.
RA Stewart J.D.;
RT "Saccharomyces cerevisiae old yellow enzyme 3.";
RL Submitted (MAR-2017) to the PDB data bank.
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 a prooxidant activity, increasing 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=0.14 mM for cyclohexenone {ECO:0000269|PubMed:7836424};
CC KM=5.8 uM for NADPH {ECO:0000269|PubMed:7836424};
CC -!- SUBUNIT: Homodimer or heterodimer with OYE2.
CC {ECO:0000269|PubMed:8454584}.
CC -!- INTERACTION:
CC P41816; Q03558: OYE2; NbExp=2; IntAct=EBI-12734, EBI-12729;
CC -!- MASS SPECTROMETRY: Mass=44788; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7836424};
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L29279; AAA64522.1; -; Genomic_DNA.
DR EMBL; Z73526; CAA97877.1; -; Genomic_DNA.
DR EMBL; Z73527; CAA97878.1; -; Genomic_DNA.
DR EMBL; AY693226; AAT93245.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65573.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11263.1; -; Genomic_DNA.
DR PIR; A55569; A55569.
DR RefSeq; NP_015154.1; NM_001183985.1.
DR PDB; 5V4P; X-ray; 1.88 A; A/B=2-400.
DR PDB; 5V4V; X-ray; 1.80 A; A/B=2-400.
DR PDBsum; 5V4P; -.
DR PDBsum; 5V4V; -.
DR AlphaFoldDB; P41816; -.
DR SMR; P41816; -.
DR BioGRID; 36012; 110.
DR DIP; DIP-6338N; -.
DR IntAct; P41816; 7.
DR STRING; 4932.YPL171C; -.
DR PaxDb; P41816; -.
DR PRIDE; P41816; -.
DR EnsemblFungi; YPL171C_mRNA; YPL171C; YPL171C.
DR GeneID; 855932; -.
DR KEGG; sce:YPL171C; -.
DR SGD; S000006092; OYE3.
DR VEuPathDB; FungiDB:YPL171C; -.
DR eggNOG; KOG0134; Eukaryota.
DR GeneTree; ENSGT00940000176560; -.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; P41816; -.
DR OMA; MQIMHGG; -.
DR BioCyc; YEAST:YPL171C-MON; -.
DR PRO; PR:P41816; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P41816; protein.
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 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8454584"
FT CHAIN 2..400
FT /note="NADPH dehydrogenase 3"
FT /id="PRO_0000194475"
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:0000269|Ref.10, ECO:0000269|Ref.9"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.9"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 244
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.9"
FT BINDING 349
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.9"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.9"
FT CONFLICT 78
FT /note="P -> S (in Ref. 4; AAT93245)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5V4V"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5V4V"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:5V4V"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:5V4V"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5V4V"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:5V4V"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:5V4V"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:5V4V"
SQ SEQUENCE 400 AA; 44920 MW; CC66CAC4B0748FE1 CRC64;
MPFVKGFEPI SLRDTNLFEP IKIGNTQLAH RAVMPPLTRM RATHPGNIPN KEWAAVYYGQ
RAQRPGTMII TEGTFISPQA GGYDNAPGIW SDEQVAEWKN IFLAIHDCQS FAWVQLWSLG
WASFPDVLAR DGLRYDCASD RVYMNATLQE KAKDANNLEH SLTKDDIKQY IKDYIHAAKN
SIAAGADGVE IHSANGYLLN QFLDPHSNKR TDEYGGTIEN RARFTLEVVD ALIETIGPER
VGLRLSPYGT FNSMSGGAEP GIIAQYSYVL GELEKRAKAG KRLAFVHLVE PRVTDPSLVE
GEGEYSEGTN DFAYSIWKGP IIRAGNYALH PEVVREQVKD PRTLIGYGRF FISNPDLVYR
LEEGLPLNKY DRSTFYTMSA EGYTDYPTYE EAVDLGWNKN
