ID   NCB5R_SCHPO             Reviewed;         301 AA.
AC   O74557;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=NADH-cytochrome b5 reductase 1;
DE            EC=1.6.2.2;
DE   AltName: Full=Microsomal cytochrome b reductase;
GN   Name=cbr1; ORFNames=SPCC970.03;
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).
CC   -!- FUNCTION: Electron donor reductase for cytochrome b5. The
CC       cytochrome b5/NADH cytochrome b5 reductase electron transfer
CC       system supports the catalytic activity of several sterol
CC       biosynthetic enzymes (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) +
CC       2 ferrocytochrome b5.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (Potential). Mitochondrion outer membrane; Multi-
CC       pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide
CC       cytochrome reductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; CU329672; CAA20696.1; -; Genomic_DNA.
DR   PIR; T41677; T41677.
DR   RefSeq; NP_587852.1; -.
DR   HSSP; P20070; 1I7P.
DR   GeneID; 2539526; -.
DR   KEGG; spo:SPCC970.03; -.
DR   NMPDR; fig|4896.1.peg.190; -.
DR   GeneDB_Spombe; SPCC970.03; -.
DR   OMA; O74557; ARFKFAL.
DR   BRENDA; 1.6.2.2; 653.
DR   ArrayExpress; O74557; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:GeneDB_SPombe.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IC:GeneDB_SPombe.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR001834; NADH-Cyt_B5_reductase.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase;
KW   Transmembrane.
FT   CHAIN         1    301       NADH-cytochrome b5 reductase 1.
FT                                /FTId=PRO_0000310844.
FT   TRANSMEM      8     28       Potential.
FT   TRANSMEM     32     49       Potential.
FT   DOMAIN       59    162       FAD-binding FR-type.
FT   NP_BIND     142    157       FAD (By similarity).
FT   NP_BIND     168    199       FAD (By similarity).
SQ   SEQUENCE   301 AA;  33723 MW;  455412A9AB47AA6B CRC64;
     MAKQTLLSTP LHGVYIPVFL IIFGTYIVKR EWVGYAIVVA FSLGFHKFWR GRVRKVLSDK
     IQQFELSDKA VLNHNTAIYR FRLPRANDVL GLPIGQHLKV FVDVDGKEYS RSYTPLSSDA
     DKGYFDLLVK SYPNGKVSKK FSELKIGDTI GVRGPKGNWK HRTGLARHFG MIAGGTGITP
     MLQIIRAVLS NFEDPTEITL LYANVSEGDI VLRDEIDALA KKDPRFTVHY VLNNPPENWK
     GSVGFVTQEL IKAHFPAPSP ETKVLICGPT PMVNSLREAT VALGYEKSRA ISKLEDQVFV
     F
//