ID   NCB5R_PHANO             Reviewed;         282 AA.
AC   Q0UEY4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   16-JUN-2009, entry version 24.
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=SNOG_09680;
OS   Phaeosphaeria nodorum (Septoria nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Phaeosphaeriaceae;
OC   Phaeosphaeria.
OX   NCBI_TaxID=13684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445339; EAT82945.2; -; Genomic_DNA.
DR   RefSeq; XP_001799967.1; -.
DR   GeneID; 5976872; -.
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    282       NADH-cytochrome b5 reductase 1.
FT                                /FTId=PRO_0000330161.
FT   TRANSMEM      2     22       Potential.
FT   DOMAIN       36    141       FAD-binding FR-type.
FT   NP_BIND     121    136       FAD (By similarity).
FT   NP_BIND     147    181       FAD (By similarity).
SQ   SEQUENCE   282 AA;  30777 MW;  42BC818575EBE25E CRC64;
     MAFSPQALLP YVVLFVAAVG GWKVYSSGSK KVLKPNEFQE FELEEKTVLS HNTAIYRFKL
     PRKTDILGLP IGQHISLGAT IEGQPKEVVR SYTPISSDED KGHFDLLIKS YPTGNISKYV
     ANLKVGEKMR VKGPKGAMVY TPNMVRHFGM ISGGTGITPM LQVVKAIIRG RGQGDTTEVD
     LIFANVNPED ILLKEDLDAL AAKDPKFRVH YVLNNPPEGW TGGVGFVTAD MIKEKLPAPA
     SDVKILVCGP PPMVAAMKKA TESLGYAKAK PVSKLEDQVF CF
//