ID NCB5R_LODEL Reviewed; 300 AA. AC A5E7U2; 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 1; DE EC=1.6.2.2; DE AltName: Full=Microsomal cytochrome b reductase; GN Name=CBR1; ORFNames=LELG_05681; 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: 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH981534; EDK47500.1; -; Genomic_DNA. DR RefSeq; XP_001523135.1; -. DR GeneID; 5230252; -. DR OMA; A5E7U2; GNISRHV. 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 1 300 NADH-cytochrome b5 reductase 1. FT /FTId=PRO_0000330156. FT TRANSMEM 8 28 Potential. FT DOMAIN 57 160 FAD-binding FR-type. FT NP_BIND 140 155 FAD (By similarity). FT NP_BIND 166 198 FAD (By similarity). FT COMPBIAS 38 47 Poly-Ser. SQ SEQUENCE 300 AA; 32936 MW; CFB31BB114073312 CRC64; MAETETNPLV VFATVATIII SFVTLYFFKQ SAKSSTTSSS SSSSSKSKKG SPALIPDKFQ KFPLISKTQV SHNSAIYRFG LPNPTDTLNL PIGQHISIGT IIDGKEVVRS YTPISLGDQQ GHFDLLIKTY ENGNISRHVA EKQVGDFVEI RGPKGFFTYT PNMKKSLGLI AGGTGIAPMY QIITAIMNNP EDKTKVHLLY ANVTENDILL RDELEQYAKE HPDRLKIHHV LNEAPEGWQH LTGFVTPELI DKHLPKPSAD TNLLLCGPPP MISAMKKAAV SLGFDKAKPV SKLGDQVFVF //