Reviewed, UniProtKB/Swiss-Prot A5E7U2 (NCB5R_LODEL)

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:	LELG_05681

Organism

Lodderomyces elongisporus (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

36914 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Lodderomyces

Protein attributes

Sequence length	300 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 – 300	300	NADH-cytochrome b5 reductase 1		PRO_0000330156
Regions
	Transmembrane	8 – 28	21	Potential
	Domain	57 – 160	104	FAD-binding FR-type
	Nucleotide binding	140 – 155	16	FAD By similarity
	Nucleotide binding	166 – 198	33	FAD By similarity
	Compositional bias	38 – 47	10	Poly-Ser

Sequences

	Sequence		Length	Mass (Da)
	A5E7U2-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: CFB31BB114073312	FASTA	300	32,936
	10 20 30 40 50 60 MAETETNPLV VFATVATIII SFVTLYFFKQ SAKSSTTSSS SSSSSKSKKG SPALIPDKFQ 70 80 90 100 110 120 KFPLISKTQV SHNSAIYRFG LPNPTDTLNL PIGQHISIGT IIDGKEVVRS YTPISLGDQQ 130 140 150 160 170 180 GHFDLLIKTY ENGNISRHVA EKQVGDFVEI RGPKGFFTYT PNMKKSLGLI AGGTGIAPMY 190 200 210 220 230 240 QIITAIMNNP EDKTKVHLLY ANVTENDILL RDELEQYAKE HPDRLKIHHV LNEAPEGWQH 250 260 270 280 290 300 LTGFVTPELI DKHLPKPSAD TNLLLCGPPP MISAMKKAAV SLGFDKAKPV SKLGDQVFVF

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981534 Genomic DNA. Translation: EDK47500.1.
RefSeq	XP_001523135.1.
3D structure databases
SMR	A5E7U2. Positions 49-300.
ModBase	Search...
Genome annotation databases
GeneID	5230252.
Phylogenomic databases
OMA	GNISRHV.
OrthoDB	EOG9KM0KS.
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_LODEL

Accession

Primary (citable) accession number: A5E7U2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	June 12, 2007
Last modified:	January 19, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)