ID QOR_SCHPO Reviewed; 329 AA. AC O74489; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1999, sequence version 2. DT 16-JUN-2009, entry version 50. DE RecName: Full=Probable quinone oxidoreductase; DE EC=1.6.5.5; DE AltName: Full=NADPH:quinone reductase; GN Name=zta1; ORFNames=SPCC1442.16c, SPCC285.01c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND MASS RP SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- CATALYTIC ACTIVITY: NADPH + 2 quinone = NADP(+) + 2 semiquinone. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329672; CAA21450.1; -; Genomic_DNA. DR PIR; T40981; T40981. DR PIR; T41247; T41247. DR RefSeq; NP_588330.1; -. DR HSSP; P28304; 1QOR. DR GeneID; 2538826; -. DR KEGG; spo:SPCC1442.16c; -. DR NMPDR; fig|4896.1.peg.668; -. DR GeneDB_Spombe; SPCC1442.16c; -. DR OMA; O74489; GTEVCGT. DR ArrayExpress; O74489; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NADP; Nucleus; Oxidoreductase; KW Phosphoprotein. FT CHAIN 1 329 Probable quinone oxidoreductase. FT /FTId=PRO_0000339115. FT MOD_RES 191 191 Phosphoserine. SQ SEQUENCE 329 AA; 34947 MW; 534A8ED20C98C0AB CRC64; MSNLLVQVSK TGPSSVLQVI TKEIPKPAPN GLVIKNAYAG LNYIDTYLRT GLYTAPLPYI PGKEAAGVVA AVGDKVEADF KVGDRVVYLT PFGAYAQYTN VPTTLVSKVS EKIPLKIASA ALLQGLTAYT LIEEAYPVKT GDTVVVHAAA GGVGLLLCQM LRARNVHVIA TASTAAKRRI AIKNGAEIAC SYEDLTKVVA DYTNGKGVDA AYDSVGIDTL SSSLDALRNG GTMVSFGNAS GAIDAIPLKF LSARCLKFVR PSLFGYITGH AVFEGYVSRL WKEILDNNLN IAIHHIFKLS EAKEAHDAIE SRATTGKLLL LCNEDLADA //