Reviewed, UniProtKB/Swiss-Prot Q5AZB4 (NCB5R_EMENI)

Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 1
    EC=1.6.2.2
Alternative name(s):
    Microsomal cytochrome b reductase

Gene names

Name:	cbr1
ORF Names:	AN6366

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Mitochondrion outer membrane; Single-pass membrane protein By similarity.
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 313	313	NADH-cytochrome b5 reductase 1		PRO_0000330153
Regions
	Transmembrane	33 – 53	21	Potential
	Domain	64 – 169	106	FAD-binding FR-type
	Nucleotide binding	149 – 163	15	FAD By similarity
	Nucleotide binding	175 – 212	38	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5AZB4-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 9265550D517C8BDE	FASTA	313	34,107
	10 20 30 40 50 60 MPVSSALSLE NITGVYAPSA LLVVGTFILK KEWVPFAVAL AAGFVAWKLS VGGSSKPRKV 70 80 90 100 110 120 LNPNEFQNFV LKEKNDISHN VTIYRFALPR PTDILGLPIG QHISLAATIE GQPKEVVRSY 130 140 150 160 170 180 TPISSDNEAG YFDLLVKAYP QGNISKYLTT LKVGDTMKVR GPKGAMVYTP NMCRHIGMIA 190 200 210 220 230 240 GGTGITPMLQ IIKAIIRNRP RNGGNDTTQV DLIFANVNPD DILLKDELEK LAAEDDGFRI 250 260 270 280 290 300 YYVLNNPPEG WTGGVGFVTP DMIKERLPAP ASDIKILLCG PPPMVSAMKK ATESLGYTKA 310 RPVSKLEDQV FCF

References

[1]

"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000107 Genomic DNA. Translation: EAA58750.1.
RefSeq	XP_663970.1.
3D structure databases
HSSP	HSSP built from PDB template 1QX4 based on UniProtKB P20070.
SMR	Q5AZB4. Positions 56-300.
ModBase	Search...
Genome annotation databases
GeneID	2871257.
KEGG	ani:AN6366.2.
Phylogenomic databases
PhylomeDB	Q5AZB4.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCB5R_EMENI

Accession

Primary (citable) accession number: Q5AZB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 26, 2005
Last modified:	January 19, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)