ID   MCR1_PICGU              Reviewed;         294 AA.
AC   A5DQE4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   16-JUN-2009, entry version 18.
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=PGUG_05495;
OS   Pichia guilliermondii (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K.,
RA   Cuomo C., Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D.B.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Zeng Q., Kodira C.D., Yandava C., Alvarado L., O'Leary S.,
RA   Reedy J., Heitman J.;
RT   "The genome sequence of Pichia guilliermondii ATCC 6260.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408161; EDK41397.2; -; Genomic_DNA.
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    294       NADH-cytochrome b5 reductase 2.
FT                                /FTId=PRO_0000330188.
FT   TRANSMEM     11     27       Potential.
FT   DOMAIN       45    149       FAD-binding FR-type.
FT   NP_BIND     152    187       FAD (By similarity).
SQ   SEQUENCE   294 AA;  32570 MW;  83D98BB5338749AE CRC64;
     MSLARFTQPR VLLPVVAAAT SIGLVYHYSS LSIQNDTAKT FKGGDEWIDL KLKKSWDVSS
     NTRHFVFELK SPEDVSGLVT ASCLMTKFVT AKGNNVIRPY TPVSDVDQKG TIDFVIKKYD
     GGKMSTHFHG LKEGDTVSFK GPIVKWKWEP NQFQSIALIG GGTGITPLYQ LLHEITKNPE
     DKTKVKLFYG NLTEEDILIK KELDDIAEKH KDQVSITYFV DKASANWKGE TGHIDKEFLQ
     SNLPGPSKDS KVFVCGPPGL YKALSGVKVS PTDQGEVTGV LAELGYTKEN VYKF
//