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Q5RD31 (NQO1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NAD(P)H dehydrogenase [quinone] 1

EC=1.6.5.2
Alternative name(s):
Azoreductase
DT-diaphorase
Short name=DTD
Menadione reductase
NAD(P)H:quinone oxidoreductase 1
Phylloquinone reductase
Quinone reductase 1
Short name=QR1
Gene names
Name:NQO1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons 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

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD(P)H dehydrogenase (quinone) activity

Inferred from electronic annotation. Source: EC

coenzyme binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274NAD(P)H dehydrogenase [quinone] 1
PRO_0000071624

Regions

Nucleotide binding18 – 192FAD By similarity
Nucleotide binding104 – 1074FAD By similarity
Nucleotide binding148 – 1514FAD By similarity
Region126 – 1283Substrate binding By similarity

Sites

Binding site121FAD By similarity
Binding site671FAD By similarity
Binding site1561FAD By similarity
Binding site2011FAD By similarity

Amino acid modifications

Modified residue591N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RD31 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 87588D65B8E92A67

FASTA27430,940
        10         20         30         40         50         60 
MVGRRALIVL AHSERTSFNY AMKEAAVAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL 

        70         80         90        100        110        120 
KDPENFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV 

       130        140        150        160        170        180 
FVGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC 

       190        200        210        220        230        240 
GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK 

       250        260        270 
KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858087 mRNA. Translation: CAH90326.1.
RefSeqNP_001125152.1. NM_001131680.1.
UniGenePab.19304.

3D structure databases

ProteinModelPortalQ5RD31.
SMRQ5RD31. Positions 2-274.
ModBaseSearch...

Proteomic databases

PRIDEQ5RD31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000008824; ENSPPYP00000008478; ENSPPYG00000007508.
GeneID100172039.
KEGGpon:100172039.

Organism-specific databases

CTD1728.

Phylogenomic databases

HOVERGENHBG029104.
InParanoidQ5RD31.
OMAGILHYPG.
OrthoDBEOG44BB36.

Family and domain databases

InterProIPR003680. Flavodoxin_fold.
[Graphical view]
KOK00355.
PfamPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNQO1_PONAB
AccessionPrimary (citable) accession number: Q5RD31
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families