FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis (By similarity).
CATALYTIC ACTIVITY: 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
COFACTOR: FAD (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.
SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.

Copyright

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Cross-references

Sequence databases

EMBL

CR858732; CAH90941.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q5RBB9; 1-230, 2-231.

ModBase

Q5RBB9.

Ontologies

GO:0001512;	Molecular function: dihydronicotinamide riboside quinone reductase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR003680; Flavodoxin_fold.
Graphical view of domain structure.

Pfam

PF02525; Flavodoxin_2; 1.
Pfam graphical view of domain structure.

BLOCKS

Q5RBB9.

Phylogenomic databases

HOVERGEN

Q5RBB9; -.

Other

ProtoNet

Q5RBB9.

UniRef

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

Keywords

Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 231`	`230`	`Ribosyldihydronicotinamide dehydrogenase [quinone].`	`PRO_0000071628`
`METAL`	`174 174`		`Zinc (By similarity).`
`METAL`	`178 178`		`Zinc (By similarity).`
`METAL`	`223 223`		`Zinc (By similarity).`

Sequence information

Length: 231 AA [This is the length of the unprocessed precursor]

Molecular weight: 26144 Da [This is the MW of the unprocessed precursor]

CRC64: 2CAD61FD15A415DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGKKVLIVY AHQEPRSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATKKDITGAL 

        70         80         90        100        110        120 
SNPEVFHYGV ETHEAYKQRS LASDITDEQK KVQEADLVIF QFPLYWFSVP AILKGWMDRV 

       130        140        150        160        170        180 
LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDFRYFLW PLQHGTLHFC 

       190        200        210        220        230 
GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWYFR Q

Q5RBB9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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