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: Monomer (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Mitochondrion outer membrane; Single-pass membrane protein (By similarity).
SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CH981534; EDK47500.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001523135.1; -.

3D structure databases

ModBase

A5E7U2.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004128;	Molecular function: cytochrome-b5 reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00406; CYTB5RDTASE.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

5230252; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 300`	`300`	`NADH-cytochrome b5 reductase 1.`	`PRO_0000330156`
`TRANSMEM`	`8 28`	`21`	`Potential.`
`DOMAIN`	`57 160`	`104`	`FAD-binding FR-type.`
`NP_BIND`	`140 155`	`16`	`FAD (By similarity).`
`NP_BIND`	`166 198`	`33`	`FAD (By similarity).`
`COMPBIAS`	`38 47`	`10`	`Poly-Ser.`

Sequence information

Length: 300 AA [This is the length of the unprocessed precursor]

Molecular weight: 32936 Da [This is the MW of the unprocessed precursor]

CRC64: CFB31BB114073312 [This is a checksum on the sequence]

        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

A5E7U2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools