ID NCB5R_ASPTN Reviewed; 296 AA. AC Q0CY37; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 21. 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=ATEG_01397; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., 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., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., RA Denning D.W., Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) 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; CH476595; EAU38154.1; -; Genomic_DNA. DR RefSeq; XP_001208762.1; -. DR GeneID; 4315740; -. 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 1 296 NADH-cytochrome b5 reductase 1. FT /FTId=PRO_0000330147. FT TRANSMEM 11 31 Potential. FT DOMAIN 47 152 FAD-binding FR-type. FT NP_BIND 132 147 FAD (By similarity). FT NP_BIND 158 195 FAD (By similarity). SQ SEQUENCE 296 AA; 32523 MW; 6E6CAF6589D35A17 CRC64; MSTFLQDNGD LSAVLVKFAP FAVAVIAILA AWKFTGSSKP RKVLNPSEFQ NFVLKEKTDI SHNVAIYRFA LPRPTDILGL PIGQHISLAA TIEGQPKEVV RSYTPISSDN EAGYFDLLVK AYPQGNISKY LTTLKIGDTL KVRGPKGAMV YTPNMCRHIG MIAGGTGITP MLQIIKAIIR NRPRNGGNDT TKIDLIFANV NEEDILLRDE LEKLAKEDDG FRIFYVLNNP PPGWNGGFGF VTAEMIKEHL PAPAKDVKIL LCGPPPMVSA MKKATESLGY TKARPVSKLE DQVFCF //