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ECOLI:NQOR

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) wrbA
Protein Name(s) NAD(P)H dehydrogenase (quinone)

Flavoprotein WrbA NAD(P)H:quinone oxidoreductase NQO

External Links
UniProt P0A8G6
EMBL M99166
U00096
AP009048
PIR B64842
RefSeq NP_415524.1
YP_489277.1
PDB 2R96
2R97
2RG1
3B6I
3B6J
3B6K
3B6M
3ZHO
PDBsum 2R96
2R97
2RG1
3B6I
3B6J
3B6K
3B6M
3ZHO
ProteinModelPortal P0A8G6
SMR P0A8G6
DIP DIP-36231N
IntAct P0A8G6
MINT MINT-1272067
STRING 511145.b1004
SWISS-2DPAGE P0A8G6
PaxDb P0A8G6
PRIDE P0A8G6
EnsemblBacteria AAC74089
BAA35771
GeneID 12930556
947263
KEGG ecj:Y75_p0977
eco:b1004
PATRIC 32117233
EchoBASE EB1502
EcoGene EG11540
eggNOG COG0655
HOGENOM HOG000030539
InParanoid P0A8G6
KO K03809
OMA MAQHIVE
OrthoDB EOG6384K0
PhylomeDB P0A8G6
BioCyc EcoCyc:PD01343
ECOL316407:JW0989-MONOMER
MetaCyc:PD01343
EvolutionaryTrace P0A8G6
PRO PR:P0A8G6
Proteomes UP000000318
UP000000625
Genevestigator P0A8G6
GO GO:0016020
GO:0050660
GO:0010181
GO:0042802
GO:0051287
GO:0003955
GO:0050661
GO:0045892
GO:0006979
Gene3D 3.40.50.360
HAMAP MF_01017
InterPro IPR008254
IPR029039
IPR010089
Pfam PF00258
SUPFAM SSF52218
TIGRFAMs TIGR01755
PROSITE PS50902

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0010275

NAD(P)H dehydrogenase complex assembly

PMID:24587082[1]

ECO:0000314

P

Refer to Figure 3, "Cell survival after exposure to uranyl at acidic pH"

complete
CACAO 9662

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000777387
UniProtKB:Q9LSQ5

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A8G6

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

PMID:16672604[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:27183467[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

PMID:16672604[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:15489429[6]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

PMID:16672604[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010089
InterPro:IPR037513

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008254
InterPro:IPR010089
InterPro:IPR037513

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005025

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.6.5.2

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100407

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100407

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100407

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100407

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Khemiri, A et al. (2014) Escherichia coli response to uranyl exposure at low pH and associated protein regulations. PLoS ONE 9 e89863 PubMed GONUTS page
  2. 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. 4.0 4.1 4.2 Patridge, EV & Ferry, JG (2006) WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase. J. Bacteriol. 188 3498-506 PubMed GONUTS page
  5. Degtjarik, O et al. (2016) Quantum Calculations Indicate Effective Electron Transfer between FMN and Benzoquinone in a New Crystal Structure of Escherichia coli WrbA. J Phys Chem B 120 4867-77 PubMed GONUTS page
  6. Lacour, S & Landini, P (2004) SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences. J. Bacteriol. 186 7186-95 PubMed GONUTS page
  7. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page