ID   MCR1_PHANO              Reviewed;         336 AA.
AC   Q0U9W5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            EC=1.6.2.2;
DE   AltName: Full=Mitochondrial cytochrome b reductase;
GN   Name=MCR1; ORFNames=SNOG_11449;
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: May mediate the reduction of outer membrane cytochrome
CC       b5 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) +
CC       2 ferrocytochrome b5.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       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; CH445343; EAT81157.1; -; Genomic_DNA.
DR   RefSeq; XP_001801691.1; -.
DR   GeneID; 5978599; -.
DR   OMA; Q0U9W5; YANVSPD.
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; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; NAD; Oxidoreductase; Transmembrane.
FT   CHAIN         1    336       NADH-cytochrome b5 reductase 2.
FT                                /FTId=PRO_0000330187.
FT   TRANSMEM     28     50       Potential.
FT   DOMAIN       84    189       FAD-binding FR-type.
FT   NP_BIND     192    227       FAD (By similarity).
SQ   SEQUENCE   336 AA;  37024 MW;  D6BDA6CF8E11601B CRC64;
     MFARQVIRPA RQLQQHVRRY ASEAPQSGGS SNGALYVGIG AAGLAGAYIY MRGGKPAAPL
     SEEANKVAAK VGGASKKAFT GGDQGFISLL LDKSEVVNHN TKKLTFKLPE PDMESGLPVT
     SAVITKYKGP EMEKPVIRPY TPVSDVDQQG TVDFIVKKYE KGPMSSHMHN MEPGQRLDIK
     GPIPKYPWSP NKHEHIALIA GGTGITPMWQ TARAIFKNPE DKTKVTLVFG NISEEDILLK
     KEWEHLENTY PQRFRAFYVL DNPPESWQGG KGFITKELLK TVLPEPKEGE KVKIFVCGPP
     GMYKAISGGK KSPSDQGELD GYLKELGYSK DQVYKF
//