QOR_YEAST
ID QOR_YEAST Reviewed; 334 AA.
AC P38230; D6VQ46;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable quinone oxidoreductase;
DE EC=1.6.5.5;
DE AltName: Full=NADPH:quinone reductase;
GN Name=ZTA1; OrderedLocusNames=YBR046C; ORFNames=YBR0421;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone +
CC NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC EC=1.6.5.5;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; Z35915; CAA84988.1; -; Genomic_DNA.
DR EMBL; AY557866; AAS56192.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07166.1; -; Genomic_DNA.
DR PIR; S45904; S45904.
DR RefSeq; NP_009602.1; NM_001178394.1.
DR PDB; 3QWA; X-ray; 2.00 A; A/B=1-334.
DR PDB; 3QWB; X-ray; 1.59 A; A/B/C/D=1-334.
DR PDBsum; 3QWA; -.
DR PDBsum; 3QWB; -.
DR AlphaFoldDB; P38230; -.
DR SMR; P38230; -.
DR BioGRID; 32748; 57.
DR IntAct; P38230; 1.
DR STRING; 4932.YBR046C; -.
DR MaxQB; P38230; -.
DR PaxDb; P38230; -.
DR PRIDE; P38230; -.
DR EnsemblFungi; YBR046C_mRNA; YBR046C; YBR046C.
DR GeneID; 852335; -.
DR KEGG; sce:YBR046C; -.
DR SGD; S000000250; ZTA1.
DR VEuPathDB; FungiDB:YBR046C; -.
DR eggNOG; KOG1197; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; P38230; -.
DR OMA; THIATRE; -.
DR BioCyc; YEAST:YBR046C-MON; -.
DR BRENDA; 1.6.5.5; 984.
DR PRO; PR:P38230; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38230; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IDA:SGD.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:SGD.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:SGD.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Probable quinone oxidoreductase"
FT /id="PRO_0000160912"
FT STRAND 7..19
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 120..141
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3QWB"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:3QWB"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:3QWA"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3QWB"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3QWB"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:3QWB"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:3QWB"
SQ SEQUENCE 334 AA; 37019 MW; 8E9D2D85D9AC518E CRC64;
MKCTIPEQQK VILIDEIGGY DVIKYEDYPV PSISEEELLI KNKYTGVNYI ESYFRKGIYP
CEKPYVLGRE ASGTVVAKGK GVTNFEVGDQ VAYISNSTFA QYSKISSQGP VMKLPKGTSD
EELKLYAAGL LQVLTALSFT NEAYHVKKGD YVLLFAAAGG VGLILNQLLK MKGAHTIAVA
STDEKLKIAK EYGAEYLINA SKEDILRQVL KFTNGKGVDA SFDSVGKDTF EISLAALKRK
GVFVSFGNAS GLIPPFSITR LSPKNITLVR PQLYGYIADP EEWKYYSDEF FGLVNSKKLN
IKIYKTYPLR DYRTAAADIE SRKTVGKLVL EIPQ
