ID NCB5R_ASPCL Reviewed; 309 AA. AC A1C7E9; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-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=ACLA_073550; OS Aspergillus clavatus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1; 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: 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; DS027045; EAW14320.1; -; Genomic_DNA. DR RefSeq; XP_001275746.1; -. DR GeneID; 4707891; -. 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 1 309 NADH-cytochrome b5 reductase 1. FT /FTId=PRO_0000330144. FT TRANSMEM 29 49 Potential. FT DOMAIN 60 165 FAD-binding FR-type. FT NP_BIND 145 160 FAD (By similarity). FT NP_BIND 171 208 FAD (By similarity). SQ SEQUENCE 309 AA; 33772 MW; 214157BBE69E47B3 CRC64; MSALSSENVN GVYIPSALLV FGTFLVKKEF VPYAVALTAV LAGFKLFTGD SKARKVLNPT EFQEFVLKEK TDISHNVSIY RFALPRPTDI LGLPIGQHIS LAATIEGQPK EVVRSYTPIS SDNEAGYFDL LVKAYPQGNI SKHLTTLKVG DVMKVRGPKG AMVYTPNMCR HIGMIAGGTG ITPMLQVIKA IIRNRPRNGG TDITKVDLIF ANVNPEDILL KEELDKLAAE DEDFNIYYVL NNPPQGWTGG VGFVTPEMIK ERLPAPASDV KVLLCGPPPM ISAMKKATES LGFTKARPVS KLEDQVFCF //