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

AACQ01000198; EAK92221.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000197; EAK92238.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_711449.1; -.
XP_711466.1; -.

3D structure databases

ModBase

Q59P03.

Organism-specific databases

CGD

CAL0001574; orf19.1801.

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:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
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).

ProtoNet

Q59P03.

Genome annotation databases

GeneID

3646945; -.
3646961; -.

KEGG

cal:CaO19.1801; -.
cal:CaO19.9367; -.

Other

UniRef

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

Keywords

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`	`1 294`	`294`	`NADH-cytochrome b5 reductase 1.`	`PRO_0000330148`
`TRANSMEM`	`18 38`	`21`	`Potential.`
`DOMAIN`	`51 154`	`104`	`FAD-binding FR-type.`
`NP_BIND`	`134 149`	`16`	`FAD (By similarity).`
`NP_BIND`	`160 192`	`33`	`FAD (By similarity).`

Sequence information

Length: 294 AA [This is the length of the unprocessed precursor]

Molecular weight: 32472 Da [This is the MW of the unprocessed precursor]

CRC64: EC4D6DB09B6733B4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSETTTVPPI ETVSEPNPFI VFATVATIIS AFIGYYFLQQ SKKHTPVLKP DEFQKFPLIE 

        70         80         90        100        110        120 
KIRVSHNSAI YRFGLPKSTD RLGLPIGQHI SIGATIDGKE VVRSYTPIST DDQLGHFDLL 

       130        140        150        160        170        180 
IKTYENGNIS RHVAGKNVGE HIEIRGPKGF FTYTPNMVKS FGMIAGGTGI APMYQIITAI 

       190        200        210        220        230        240 
LKNPEDKTKI HLVYANVTES DILLKEELDN FAARHPDRLK IHYVLNEAPA NWQGSVGFVT 

       250        260        270        280        290 
PEIIDTHLPK ASNDTNLLLC GPPPMVSAMK KAAVELGFQK AKPVSKLGDQ VFVF

Q59P03 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