ID   NCB5R_USTMA             Reviewed;         324 AA.
AC   Q4PGW7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=UM00646;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(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; Single-pass
CC       membrane protein (By similarity). Mitochondrion outer membrane;
CC       Single-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; AACP01000015; EAK81075.1; -; Genomic_DNA.
DR   RefSeq; XP_756793.1; -.
DR   GeneID; 3628702; -.
DR   KEGG; uma:UM00646.1; -.
DR   OMA; Q4PGW7; GNISRHV.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   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   3: Inferred from homology;
KW   Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase;
KW   Transmembrane.
FT   CHAIN         1    324       NADH-cytochrome b5 reductase 1.
FT                                /FTId=PRO_0000330164.
FT   TRANSMEM     49     69       Potential.
FT   DOMAIN       81    184       FAD-binding FR-type.
FT   NP_BIND     164    179       FAD (By similarity).
FT   NP_BIND     190    222       FAD (By similarity).
SQ   SEQUENCE   324 AA;  36028 MW;  5DAE5856673654C9 CRC64;
     MVLIEQVVLV ASILITFGTC LAATKYAARL FPHFEPLQFY DEATNPMELN IVLAFVVGLI
     GSVVVLLYFD SQKIKPVLNP TQWQQYRLME KQKLSDNTAL YRFKLPRSNN ILGLPIGQHI
     SVQANMGGKT VVRSYTPTSS DDDHGFFDLV VKSYEQGNVS KYIGSMKIGD LLSVKGPKGQ
     MRYAPGLSRH IGMIAGGTGL TPCLQIIRAA LKNPADKTQI DFIYANVKET DILLKDELDE
     LALKHKDQFR ISYFLNEAPE GWKGGVGFVT KEALEKNLPK PANDIKVLMC GPPPMIKAMT
     GHLEALGYEK PRTVSKLEDQ VFCF
//