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ECOLI:NQOR
Contents
| 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 |
ECO:0000314 |
P |
Refer to Figure 3, "Cell survival after exposure to uranyl at acidic pH" |
complete | |||||
|
part_of |
GO:0016020 |
membrane |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000777387 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003955 |
NAD(P)H dehydrogenase (quinone) activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051289 |
protein homotetramerization |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0010181 |
FMN binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006979 |
response to oxidative stress |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003955 |
NAD(P)H dehydrogenase (quinone) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003955 |
NAD(P)H dehydrogenase (quinone) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0010181 |
FMN binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003955 |
NAD(P)H dehydrogenase (quinone) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051287 |
NAD binding |
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 |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000100407 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0050661 |
NADP binding |
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 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 2.0 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
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 4.0 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
- ↑ 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
- ↑ 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
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ 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
