[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	PROTEIN SEQUENCE OF 184-201, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.

Comments

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

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

Cross-references

Sequence databases

EMBL

BC079157; AAH79157.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001004214.1; -.

UniGene

Rn.7882

3D structure databases

SMR

Q6AY80; 1-228, 2-229.

ModBase

Q6AY80.

Organism-specific databases

RGD

1303320; Nqo2.

Gene expression databases

ArrayExpress

Q6AY80; -.

GermOnline

ENSRNOG00000017820; Rattus norvegicus.

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

Q6AY80.

Genome annotation databases

Ensembl

ENSRNOG00000017820; Rattus norvegicus. [Contig view]

GeneID

291084; -.

KEGG

rno:291084; -.

NMPDR

fig|10116.3.peg.13235; -.

Phylogenomic databases

HOVERGEN

Q6AY80; -.

Other

ProtoNet

Q6AY80.

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; 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_0000071629`
`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: 26275 Da [This is the MW of the unprocessed precursor]

CRC64: 9B15F21CD005850A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGKKVLLVY AHQEPKSFNG SMKQVAVEEL SKQGCTVTVS DLYTMNFEPR ATRNDVTGAL 

        70         80         90        100        110        120 
SNPEVFKYGI EAYEAYKKKA LTSDILEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV 

       130        140        150        160        170        180 
LCQGFAFDVP GFYDSGFLKD KLALLSFTTG GTAEMYTKAG VNGDFRYFLW PLQHGTLHFC 

       190        200        210        220        230 
GFKVLAPQIS FGPEVSSEEQ RKVMLASWVQ RLKSIWKEEP IHCTPSWYFQ G

Q6AY80 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