ID   MCR1_LODEL              Reviewed;         300 AA.
AC   A5E5C5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=LELG_04814;
OS   Lodderomyces elongisporus (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239;
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   Kurtzman C., Reedy J., Heitman J.;
RT   "The genome sequence of Lodderomyces elongisporus.";
RL   Submitted (JUL-2006) 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; CH981530; EDK46633.1; -; Genomic_DNA.
DR   RefSeq; XP_001524001.1; -.
DR   GeneID; 5231247; -.
DR   OMA; A5E5C5; VVKWKWE.
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    300       NADH-cytochrome b5 reductase 2.
FT                                /FTId=PRO_0000330183.
FT   TRANSMEM     12     29       Potential.
FT   DOMAIN       49    153       FAD-binding FR-type.
FT   NP_BIND     156    191       FAD (By similarity).
SQ   SEQUENCE   300 AA;  33537 MW;  360834C12407A8C6 CRC64;
     MSVSRLFSNP KFVYPLVGAT IGSIGLAYYS TQAQFYIANE TGKTFTGGDQ WIDLKLKKSE
     DLTHNTKHLT FELLNPDDVS GLITASMLMT KYVTPKGNNV IRPYTPVSDP DQKGTLDFVI
     KRYENGKMSN HIHNLKEGET LSFKGPVVKW KWEPNQFKSI ALIGGGTGIT PLYQLLREIT
     SNPEDKTKVS LIYGNTSPED VLIKDRIDDI AAKHKDQVKV TYFVDENKAT KDWEGEVGFI
     TKEFLEKELD KPSPDFKIFV CGPPGLYKAI SGVKVSPTDQ GEVEGALKDL GFSKEHVFKF
//