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Protein

NAD(P)H dehydrogenase (quinone)

Gene

DR_A0214

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide (By similarity).By similarity

Catalytic activityi

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

Cofactori

FMN1 PublicationNote: Binds 1 FMN per monomer.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei142 – 1421FMN1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 185FMN1 Publication
Nucleotide bindingi86 – 883FMN1 Publication
Nucleotide bindingi121 – 1277FMN1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2904-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H dehydrogenase (quinone) (EC:1.6.5.2)
Alternative name(s):
Flavoprotein WrbA
NAD(P)H:quinone oxidoreductase
Short name:
NQO
Gene namesi
Ordered Locus Names:DR_A0214
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 200199NAD(P)H dehydrogenase (quinone)PRO_0000422321Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243230.DR_A0214.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi14 – 163Combined sources
Helixi17 – 3115Combined sources
Beta strandi35 – 406Combined sources
Helixi47 – 504Combined sources
Helixi54 – 629Combined sources
Turni63 – 653Combined sources
Helixi71 – 766Combined sources
Beta strandi78 – 8710Combined sources
Helixi93 – 1008Combined sources
Helixi103 – 1075Combined sources
Turni108 – 1136Combined sources
Beta strandi115 – 12410Combined sources
Helixi131 – 14111Combined sources
Turni142 – 1443Combined sources
Helixi155 – 1595Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1703Combined sources
Helixi178 – 19922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDGX-ray2.00A/B/C/D/E/F/G/H2-199[»]
1YRHX-ray3.11A/B/C/D/E/F/G/H2-199[»]
ProteinModelPortaliQ9RYU4.
SMRiQ9RYU4. Positions 2-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RYU4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 199193Flavodoxin-likeAdd
BLAST

Sequence similaritiesi

Belongs to the WrbA family.Curated
Contains 1 flavodoxin-like domain.Curated

Phylogenomic databases

eggNOGiENOG4105CS1. Bacteria.
COG0655. LUCA.
HOGENOMiHOG000030539.
InParanoidiQ9RYU4.
KOiK03809.
OMAiQAGGLWM.
OrthoDBiEOG6384K0.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
HAMAPiMF_01017. NQOR.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR010089. Flavoprotein_WrbA.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01755. flav_wrbA. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9RYU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPVKLAIV FYSSTGTGYA MAQEAAEAGR AAGAEVRLLK VRETAPQDVI
60 70 80 90 100
DGQDAWKANI EAMKDVPEAT PADLEWAEAI VFSSPTRFGG ATSQMRAFID
110 120 130 140 150
TLGGLWSSGK LANKTFSAMT SAQNVNGGQE TTLQTLYMTA MHWGAVLTPP
160 170 180 190 200
GYTDEVIFKS GGNPYGASVT ANGQPLLEND RASIRHQVRR QVELTAKLLG
Length:200
Mass (Da):21,298
Last modified:May 1, 2000 - v1
Checksum:iFD2FEA38E9775909
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12417.1.
PIRiG75573.
RefSeqiNP_285537.1. NC_001264.1.
WP_010889473.1. NC_001264.1.

Genome annotation databases

EnsemblBacteriaiAAF12417; AAF12417; DR_A0214.
GeneIDi1798184.
KEGGidra:DR_A0214.
PATRICi21633468. VBIDeiRad64572_3103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12417.1.
PIRiG75573.
RefSeqiNP_285537.1. NC_001264.1.
WP_010889473.1. NC_001264.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDGX-ray2.00A/B/C/D/E/F/G/H2-199[»]
1YRHX-ray3.11A/B/C/D/E/F/G/H2-199[»]
ProteinModelPortaliQ9RYU4.
SMRiQ9RYU4. Positions 2-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_A0214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF12417; AAF12417; DR_A0214.
GeneIDi1798184.
KEGGidra:DR_A0214.
PATRICi21633468. VBIDeiRad64572_3103.

Phylogenomic databases

eggNOGiENOG4105CS1. Bacteria.
COG0655. LUCA.
HOGENOMiHOG000030539.
InParanoidiQ9RYU4.
KOiK03809.
OMAiQAGGLWM.
OrthoDBiEOG6384K0.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2904-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RYU4.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
HAMAPiMF_01017. NQOR.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR010089. Flavoprotein_WrbA.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR01755. flav_wrbA. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  2. "Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide."
    Gorman J., Shapiro L.
    Protein Sci. 14:3004-3012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-199 IN COMPLEX WITH FMN, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiNQOR_DEIRA
AccessioniPrimary (citable) accession number: Q9RYU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: May 1, 2000
Last modified: January 20, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.