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wrbA NAD(P)H:quinone oxidoreductase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947263, updated on 3-Dec-2024

Summary

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Official Symbol
wrbA
Official Full Name
NAD(P)H:quinone oxidoreductase
Primary source
ECOCYC:EG11540
Locus tag
b1004
See related
ASAP:ABE-0003392
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0995
Summary
WrbA was originally identified as a stationary phase TrpR-binding protein that affected the interaction of TrpR with its operator sites in vitro (Yang, 1993). [More information is available at EcoGene: EG11540]. The purified WrbA protein has NAD(P)H:quinone oxidoreductase activity . [More information is available at EcoCyc: EG11540].
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Genomic context

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Sequence:
NC_000913.3 (1067112..1067708, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene glucose-1-phosphatase Neighboring gene PF13993 family protein YccJ Neighboring gene stress-induced bacterial acidophilic repeat motifs-containing protein YmdF Neighboring gene pyrimidine:H(+) symporter

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structural organization of WrbA in apo- and holoprotein crystals. Wolfova J, et al. Biochim Biophys Acta, 2009 Sep. PMID 19665595
  2. Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode. Nöll G, et al. Langmuir, 2006 Feb 28. PMID 16489832
  3. Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Natalello A, et al. Biochemistry, 2007 Jan 16. PMID 17209564
  4. Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Wolfová J, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007 Jul 1. PMID 17620713, Free PMC Article
  5. WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Carey J, et al. Protein Sci, 2007 Oct. PMID 17893367, Free PMC Article

See all (28) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Topologically non-equivalent residues undergo remarkably similar local structural changes upon Flavin Mononucleotide binding to WrbA or to flavodoxin, despite differences in multimeric organization and residue types at the binding sites.
    Title: Structural organization of WrbA in apo- and holoprotein crystals.
  2. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners.
    Title: WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.
  3. N-terminus verified by Edman degradation on mature peptide
    Title: A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA.
  4. FMN binding has a dramatic effect on WrbA thermal stability, shifting the Tm by approximately 40 degrees C.
    Title: Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables FMN binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables FMN binding IEA
Inferred from Electronic Annotation
more info
  
enables NAD binding IEA
Inferred from Electronic Annotation
more info
  
enables NAD(P)H dehydrogenase (quinone) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables NAD(P)H dehydrogenase (quinone) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables NAD(P)H dehydrogenase (quinone) activity IEA
Inferred from Electronic Annotation
more info
  
enables NAD(P)H dehydrogenase (quinone) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables NADH:ubiquinone reductase (non-electrogenic) activity IEA
Inferred from Electronic Annotation
more info
  
enables NADP binding IEA
Inferred from Electronic Annotation
more info
  
enables NADPH dehydrogenase (quinone) activity IEA
Inferred from Electronic Annotation
more info
  
enables flavin adenine dinucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within response to oxidative stress IEP
Inferred from Expression Pattern
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane HDA PubMed 
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of protein-containing complex IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
NAD(P)H:quinone oxidoreductase

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1067112..1067708 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415524.1 NAD(P)H:quinone oxidoreductase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415524.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A6M9WX62, A0A8S7E8G3
    Conserved Domains (1) summary
    PRK03767
    Location:1 → 198
    PRK03767; NAD(P)H:quinone oxidoreductase; Provisional
Nucleotide Protein
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