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UniProtKB - P0A8G6 (NQOR_ECOLI)
Protein
NAD(P)H dehydrogenase (quinone)
Gene
wrbA
Organism
Escherichia coli (strain K12)
Status
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. It prefers NADH over NADPH.
2 PublicationsMiscellaneous
FMN promotes WrbA association into tetramers, which are more thermoresistant than dimers or monomers, suggesting that multimerization underlies the FMN effect on WrbA thermostability.1 Publication
Caution
Was originally (PubMed:9694845) thought to enhance the formation and/or stability of non-covalent complexes between the trp repressor protein and operator-bearing DNA. However, WrbA does not specifically influence the affinity or mode of binding of TrpR to its operator.1 Publication
Catalytic activityi
Cofactori
FMNUniRule annotation2 PublicationsNote: Binds 1 FMN per monomer.UniRule annotation2 Publications
Kineticsi
- KM=5.8 µM for benzoquinone1 Publication
- KM=14 µM for NADH1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 12 | NAD1 Publication | 1 | |
Binding sitei | 51 | NAD; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 98 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 133 | FMNUniRule annotation2 Publications | 1 | |
Binding sitei | 169 | NAD1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 10 – 15 | FMNUniRule annotation2 Publications | 6 | |
Nucleotide bindingi | 78 – 80 | FMNUniRule annotation2 Publications | 3 | |
Nucleotide bindingi | 113 – 118 | FMNUniRule annotation2 Publications | 6 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: UniProtKB-UniRule
- FMN binding Source: EcoCyc
- identical protein binding Source: IntAct
- NAD(P)H dehydrogenase (quinone) activity Source: EcoCyc
- NAD binding Source: UniProtKB-UniRule
- NADH dehydrogenase (quinone) activity Source: RHEA
- NADP binding Source: UniProtKB-UniRule
- NADPH dehydrogenase (quinone) activity Source: RHEA
GO - Biological processi
- response to oxidative stress Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Flavoprotein, FMN, NAD, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:PD01343 |
BRENDAi | 1.6.5.2, 2026 |
SABIO-RKi | P0A8G6 |
Names & Taxonomyi
Protein namesi | Recommended name: NAD(P)H dehydrogenase (quinone)UniRule annotation (EC:1.6.5.2UniRule annotation1 Publication)Alternative name(s): Flavoprotein WrbA NAD(P)H:quinone oxidoreductaseUniRule annotation Short name: NQOUniRule annotation |
Gene namesi | Name:wrbA Ordered Locus Names:b1004, JW0989 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
Other locations
- membrane Source: UniProtKB
- protein-containing complex Source: EcoCyc
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene show no phenotypes, however, N-trichloromethyl-mercapto-4-cyclohexene-1,2-dicarboximide and 8-hydroxyquinoline significantly inhibit the growth of the wrbA knockout relative to the wild-type, which is consistent with a role for WrbA in protecting against environmental stressors through its quinone reductase activity.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed3 Publications | |||
ChainiPRO_0000200746 | 2 – 198 | NAD(P)H dehydrogenase (quinone)Add BLAST | 197 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 50 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A8G6 |
PaxDbi | P0A8G6 |
PRIDEi | P0A8G6 |
2D gel databases
SWISS-2DPAGEi | P0A8G6 |
PTM databases
iPTMneti | P0A8G6 |
Interactioni
Subunit structurei
Homodimer and homotetramer; in equilibrium.
4 PublicationsBinary interactionsi
P0A8G6
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-553971,EBI-553971 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4259550, 24 interactors |
DIPi | DIP-36231N |
IntActi | P0A8G6, 4 interactors |
MINTi | P0A8G6 |
STRINGi | 511145.b1004 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A8G6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A8G6 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 4 – 189 | Flavodoxin-likeUniRule annotationAdd BLAST | 186 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0655, Bacteria |
HOGENOMi | CLU_051402_0_2_6 |
InParanoidi | P0A8G6 |
PhylomeDBi | P0A8G6 |
Family and domain databases
Gene3Di | 3.40.50.360, 1 hit |
HAMAPi | MF_01017, NQOR, 1 hit |
InterProi | View protein in InterPro IPR008254, Flavodoxin/NO_synth IPR029039, Flavoprotein-like_sf IPR010089, Flavoprotein_WrbA-like IPR005025, FMN_Rdtase-like IPR037513, NQO |
Pfami | View protein in Pfam PF03358, FMN_red, 1 hit |
SUPFAMi | SSF52218, SSF52218, 1 hit |
TIGRFAMsi | TIGR01755, flav_wrbA, 1 hit |
PROSITEi | View protein in PROSITE PS50902, FLAVODOXIN_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A8G6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAKVLVLYYS MYGHIETMAR AVAEGASKVD GAEVVVKRVP ETMPPQLFEK
60 70 80 90 100
AGGKTQTAPV ATPQELADYD AIIFGTPTRF GNMSGQMRTF LDQTGGLWAS
110 120 130 140 150
GALYGKLASV FSSTGTGGGQ EQTITSTWTT LAHHGMVIVP IGYAAQELFD
160 170 180 190
VSQVRGGTPY GATTIAGGDG SRQPSQEELS IARYQGEYVA GLAVKLNG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 142 | G → A in AAA24759 (PubMed:8516330).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M99166 Genomic DNA Translation: AAA24759.1 U00096 Genomic DNA Translation: AAC74089.1 AP009048 Genomic DNA Translation: BAA35771.1 |
PIRi | B64842 |
RefSeqi | NP_415524.1, NC_000913.3 WP_001151437.1, NZ_STEB01000006.1 |
Genome annotation databases
EnsemblBacteriai | AAC74089; AAC74089; b1004 BAA35771; BAA35771; BAA35771 |
GeneIDi | 66670718 947263 |
KEGGi | ecj:JW0989 eco:b1004 |
PATRICi | fig|1411691.4.peg.1267 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M99166 Genomic DNA Translation: AAA24759.1 U00096 Genomic DNA Translation: AAC74089.1 AP009048 Genomic DNA Translation: BAA35771.1 |
PIRi | B64842 |
RefSeqi | NP_415524.1, NC_000913.3 WP_001151437.1, NZ_STEB01000006.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2R96 | X-ray | 2.60 | A/C | 1-198 | [»] | |
2R97 | X-ray | 2.00 | A/C | 1-198 | [»] | |
2RG1 | X-ray | 1.85 | A/B | 1-198 | [»] | |
3B6I | X-ray | 1.66 | A/B | 1-198 | [»] | |
3B6J | X-ray | 2.05 | A/B | 1-198 | [»] | |
3B6K | X-ray | 1.99 | A/B | 1-198 | [»] | |
3B6M | X-ray | 1.85 | A/B | 1-198 | [»] | |
3ZHO | X-ray | 1.20 | A/B | 2-198 | [»] | |
4YQE | X-ray | 1.33 | A/B | 2-198 | [»] | |
5F12 | X-ray | 1.50 | A/B | 2-198 | [»] | |
SMRi | P0A8G6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259550, 24 interactors |
DIPi | DIP-36231N |
IntActi | P0A8G6, 4 interactors |
MINTi | P0A8G6 |
STRINGi | 511145.b1004 |
PTM databases
iPTMneti | P0A8G6 |
2D gel databases
SWISS-2DPAGEi | P0A8G6 |
Proteomic databases
jPOSTi | P0A8G6 |
PaxDbi | P0A8G6 |
PRIDEi | P0A8G6 |
Genome annotation databases
EnsemblBacteriai | AAC74089; AAC74089; b1004 BAA35771; BAA35771; BAA35771 |
GeneIDi | 66670718 947263 |
KEGGi | ecj:JW0989 eco:b1004 |
PATRICi | fig|1411691.4.peg.1267 |
Organism-specific databases
EchoBASEi | EB1502 |
Phylogenomic databases
eggNOGi | COG0655, Bacteria |
HOGENOMi | CLU_051402_0_2_6 |
InParanoidi | P0A8G6 |
PhylomeDBi | P0A8G6 |
Enzyme and pathway databases
BioCyci | EcoCyc:PD01343 |
BRENDAi | 1.6.5.2, 2026 |
SABIO-RKi | P0A8G6 |
Miscellaneous databases
EvolutionaryTracei | P0A8G6 |
PROi | PR:P0A8G6 |
Family and domain databases
Gene3Di | 3.40.50.360, 1 hit |
HAMAPi | MF_01017, NQOR, 1 hit |
InterProi | View protein in InterPro IPR008254, Flavodoxin/NO_synth IPR029039, Flavoprotein-like_sf IPR010089, Flavoprotein_WrbA-like IPR005025, FMN_Rdtase-like IPR037513, NQO |
Pfami | View protein in Pfam PF03358, FMN_red, 1 hit |
SUPFAMi | SSF52218, SSF52218, 1 hit |
TIGRFAMsi | TIGR01755, flav_wrbA, 1 hit |
PROSITEi | View protein in PROSITE PS50902, FLAVODOXIN_LIKE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NQOR_ECOLI | |
Accessioni | P0A8G6Primary (citable) accession number: P0A8G6 Secondary accession number(s): P30849, P75890, P77543 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 7, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 138 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families