ID   OYEB_SCHPO              Reviewed;         392 AA.
AC   Q09671;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 54.
DE   RecName: Full=Putative NADPH dehydrogenase C5H10.10;
DE            EC=1.6.99.1;
DE   AltName: Full=Old yellow enzyme homolog 2;
GN   ORFNames=SPAC5H10.10;
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.
CC   -!- SUBUNIT: Homodimer or heterodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family.
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DR   EMBL; CU329670; CAA89960.1; -; Genomic_DNA.
DR   PIR; S55488; S55488.
DR   RefSeq; NP_592823.1; -.
DR   HSSP; Q9XG54; 1ICP.
DR   GeneID; 2541553; -.
DR   KEGG; spo:SPAC5H10.10; -.
DR   NMPDR; fig|4896.1.peg.2793; -.
DR   GeneDB_Spombe; SPAC5H10.10; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000568-MON; -.
DR   ArrayExpress; Q09671; -.
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: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    392       Putative NADPH dehydrogenase C5H10.10.
FT                                /FTId=PRO_0000194478.
FT   BINDING      34     34       FMN (By similarity).
FT   BINDING     196    196       FMN (By similarity).
FT   BINDING     196    196       Substrate (By similarity).
FT   BINDING     199    199       Substrate (By similarity).
FT   BINDING     249    249       FMN (By similarity).
FT   BINDING     341    341       FMN (By similarity).
FT   BINDING     368    368       Substrate (By similarity).
SQ   SEQUENCE   392 AA;  44983 MW;  EE41AD26E3514C4F CRC64;
     MAVQKLYESQ SKLFQPIKVG NMQLQHRMVH APATRLRCLD NGLVMTDLVK EYYKQRSSIP
     GTLLITESLF SGAKSGGFSN IPCLYNDEHV EAWKPIVQAI HDNDCFVFIQ FWNLPGELKV
     DYLEDQERLE KVTQGECPMD PTGLPAALGS AYSICGEELY VDKFMTKQDI QEHITTYTEA
     AKRAVFGCGA DGVEVHQVNG FLLDKFVLNG YGDKCDPEYC GSLENRARFC LELLESVVNA
     IGQERVGYRI SPFSDIWKDK DSFEAHVFMI KKIKERFPNL AYLHAIEPRQ YWNGHVHITQ
     EKNTLIYKNL WGDPFITAGG HDRDSAIQMA EQENTLVAFG RYFLSNPDLP FRLKYNLPLN
     KWDRATFYTK MSPKGYIDYP FSKEFLDTKK VE
//