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Reviewed, UniProtKB/Swiss-Prot Q6AY80 (NQO2_RAT)

Last modified February 9, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribosyldihydronicotinamide dehydrogenase [quinone]
    EC=1.10.99.2
Alternative name(s):
    NRH dehydrogenase [quinone] 2
    NRH:quinone oxidoreductase 2
    Quinone reductase 2
      Short name=QR2
Gene names
Name: Nqo2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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.

FAD By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.

Sequence similarities

Belongs to the NAD(P)H dehydrogenase (quinone) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 231230Ribosyldihydronicotinamide dehydrogenase [quinone]
PRO_0000071629

Regions

Nucleotide binding18 – 214FAD By similarity
Nucleotide binding104 – 1074FAD By similarity
Nucleotide binding148 – 1514FAD By similarity
Region127 – 1293Substrate binding By similarity

Sites

Metal binding1741Zinc By similarity
Metal binding1781Zinc By similarity
Metal binding2231Zinc By similarity
Binding site121FAD By similarity
Binding site1561FAD By similarity
Binding site1941FAD By similarity
Binding site2011FAD By similarity

Amino acid modifications

Modified residue311Phosphoserine By similarity
Modified residue1971Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AY80-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9B15F21CD005850A

FASTA23126,275
        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 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 184-201, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC079157 mRNA. Translation: AAH79157.1.
IPIIPI00464620.
RefSeqNP_001004214.1.
UniGeneRn.7882

3D structure databases

SMRQ6AY80. Positions 2-229.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6AY80.

Genome annotation databases

EnsemblENSRNOT00000024141; ENSRNOP00000024141; ENSRNOG00000017820; Rattus norvegicus. [Genome view]
GeneID291084.
KEGGrno:291084.
NMPDRfig|10116.3.peg.13235.
UCSCNM_001004214. rat.

Organism-specific databases

CTD291084.
RGD1303320. Nqo2.

Phylogenomic databases

eggNOGmaNOG11886.
HOVERGENQ6AY80.
InParanoidQ6AY80.
PhylomeDBQ6AY80.

Enzyme and pathway databases

BRENDA1.10.99.2. 248.

Gene expression databases

ArrayExpressQ6AY80.
GenevestigatorQ6AY80.
GermOnlineENSRNOG00000017820. Rattus norvegicus.

Family and domain databases

InterProIPR003680. Flavodoxin_fold.
[Graphical view]
PfamPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio632093.

Entry information

Entry nameNQO2_RAT
AccessionPrimary (citable) accession number: Q6AY80
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 49 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents