ID   OYEA_SCHPO              Reviewed;         382 AA.
AC   Q09670;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Putative NADPH dehydrogenase C5H10.04;
DE            EC=1.6.99.1;
DE   AltName: Full=Old yellow enzyme homolog 1;
GN   ORFNames=SPAC5H10.04;
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; CAA89954.1; -; Genomic_DNA.
DR   PIR; S55482; S55482.
DR   RefSeq; NP_592817.1; -.
DR   HSSP; Q9XG54; 1ICP.
DR   GeneID; 2541543; -.
DR   KEGG; spo:SPAC5H10.04; -.
DR   NMPDR; fig|4896.1.peg.2787; -.
DR   GeneDB_Spombe; SPAC5H10.04; -.
DR   OMA; Q09670; NIYLMSE.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000562-MON; -.
DR   BRENDA; 1.6.99.1; 653.
DR   ArrayExpress; Q09670; -.
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    382       Putative NADPH dehydrogenase C5H10.04.
FT                                /FTId=PRO_0000194477.
FT   BINDING      28     28       FMN (By similarity).
FT   BINDING     189    189       FMN (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   BINDING     192    192       Substrate (By similarity).
FT   BINDING     242    242       FMN (By similarity).
FT   BINDING     334    334       FMN (By similarity).
FT   BINDING     361    361       Substrate (By similarity).
SQ   SEQUENCE   382 AA;  43813 MW;  3F7939599CA167D1 CRC64;
     MNDRGELFKP IKVGNMLLQH RIVHAPMTRL RATDYGKITG LMVEYYSQRS MIPGTLLIAD
     ATFVGEKSGG FPNNPRCFTK EQAESWIPLV EAVHKNKSFL FIQFWPLPGD LKDEYRNDLE
     KMQKITYSDC PQDPGGLPAG IHSFDAVQGV EVYKKKYMSK RDIQEHIQDF VNAADLAVNI
     AKADGVEIHQ VNGFLLDRFV LGGFGDQCDP EYRGSIENRC RFPLEVLEAV TRKIGQERVG
     YRISPFSGWM QKIDFMEVNI YLMSEIAKRF PKLAYIHAIE PRKYWSGHKL VSSEQNTSFL
     QKYWKGPFIT AGGYDPETAV QAANERGVLV AFGRNFIANP DLVFRIKHHI PLNKWDRSSF
     YLPKTEKGYT DYPFSKEFLQ SK
//