ID   MCR1_NEOFI              Reviewed;         323 AA.
AC   A1D4H0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=NFIA_020210;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL
OS   181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW23313.1; -; Genomic_DNA.
DR   RefSeq; XP_001265210.1; -.
DR   GeneID; 4591841; -.
DR   KEGG; nfi:NFIA_020210; -.
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    323       NADH-cytochrome b5 reductase 2.
FT                                /FTId=PRO_0000330185.
FT   TRANSMEM     32     48       Potential.
FT   DOMAIN       72    177       FAD-binding FR-type.
FT   NP_BIND     180    215       FAD (By similarity).
SQ   SEQUENCE   323 AA;  36231 MW;  A99290424B1703E9 CRC64;
     MFARQSLRFA QPLKQGFRKY STEAPSKGKS SLAPIYVAVG LTGLGVGLYR YNSASAEAPP
     AERPKVFTGG DQGWVDLKLA QIENLSPNTK RLRFEFPDKE AVSGLHVASA LLTKFKPHGA
     EKPVIRPYTP VSDEEQPGYL DLVVKVYPNG PMSEHLHSMN VDQRLEFKGP IPKYPWEANK
     HKHICLIAGG TGITPMYQLA RKIFKDPEDQ TKVTLVFGNV REEDILLKKE LQELENTYPR
     RFRAFYVLDH PPKEWTGGKG YITKELLKTV LPEPKEENIK IFVCGPPGMY KSISGPKVSP
     KDQGELTGIL AELGYSKDQV FKF
//