ID OYEC_SCHPO Reviewed; 395 AA. AC O94467; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 16-JUN-2009, entry version 38. DE RecName: Full=Putative NADPH dehydrogenase C23G7.10c; DE EC=1.6.99.1; DE AltName: Full=Old yellow enzyme homolog 3; GN ORFNames=SPBC23G7.10c; 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). CC -!- CATALYTIC ACTIVITY: NADPH + acceptor = NADP(+) + reduced acceptor. CC -!- COFACTOR: FMN (By similarity). CC -!- SUBUNIT: Homodimer or heterodimer (By similarity). CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase CC family. 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; CU329671; CAA22626.1; -; Genomic_DNA. DR PIR; T39956; T39956. DR RefSeq; NP_595868.1; -. DR GeneID; 2540490; -. DR KEGG; spo:SPBC23G7.10c; -. DR NMPDR; fig|4896.1.peg.1734; -. DR GeneDB_Spombe; SPBC23G7.10c; -. DR OMA; O94467; STVAPWL. DR BRENDA; 1.6.99.1; 653. DR ArrayExpress; O94467; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:EC. DR GO; GO:0033554; P:cellular response to stress; IEP:GeneDB_SPombe. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001155; OxRdtase_FMN_N. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00724; Oxidored_FMN; 1. PE 2: Evidence at transcript level; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase. FT CHAIN 1 395 Putative NADPH dehydrogenase C23G7.10c. FT /FTId=PRO_0000314118. FT ACT_SITE 213 213 Proton donor (By similarity). FT BINDING 208 208 FMN (By similarity). FT BINDING 208 208 Substrate (By similarity). FT BINDING 358 358 FMN (By similarity). FT BINDING 386 386 Substrate (By similarity). SQ SEQUENCE 395 AA; 43684 MW; EF4687841D9FDA06 CRC64; MTIVNEGAEN VGYFTPAQKI PAGAAIGVPQ TKLFTPLKIR GVEFHNRMFV SPMCTYSADQ EGHLTDFHLV HLGAMGMRGP GLVMVEATAV SPEGRISPND SGLWMESQMK PLRRIVEFAH SQNQKIGIQL AHAGRKASTT APYRGYTVAT EAQGGWENDV YGPNEDRWDE NHAQPHKLTE KQYDELVDKF VVAAKRAVEI GFDVIEIHGA HGYLISSTVS PATNDRNDKY GGTFEKRILF PMEVVHSVRK AIPDSMPLFY RVTATDWLPK GQGWEIEDTV ALAARLRDGG VDLIDVSSGG NHKDQRIEVK DCYQVPFAEK IKDQVNGILL GAVGMIRDGL TANEILESGK ADVTFVAREF LRNPSLVLDS ANQLGENVAW PVQYDYAVKG HRKLR //