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ECOLI:FENR
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | fpr (synonyms: mvrA) | |
| Protein Name(s) | Ferredoxin--NADP reductase
FNR DA1 Flavodoxin reductase FLDR FLXR Methyl viologen resistance protein A | |
| External Links | ||
| UniProt | P28861 | |
| EMBL | L04757 L19201 U00096 AP009048 Z11767 M19644 | |
| PIR | S40867 | |
| RefSeq | NP_418359.1 YP_491527.1 | |
| PDB | 1FDR 2XNJ | |
| PDBsum | 1FDR 2XNJ | |
| ProteinModelPortal | P28861 | |
| SMR | P28861 | |
| IntAct | P28861 | |
| STRING | 511145.b3924 | |
| DrugBank | DB03147 | |
| PaxDb | P28861 | |
| PRIDE | P28861 | |
| EnsemblBacteria | AAC76906 BAE77386 | |
| GeneID | 12932121 948414 | |
| KEGG | ecj:Y75_p3263 eco:b3924 | |
| PATRIC | 32123361 | |
| EchoBASE | EB1480 | |
| EcoGene | EG11518 | |
| eggNOG | COG1018 | |
| HOGENOM | HOG000265758 | |
| InParanoid | P28861 | |
| KO | K00528 | |
| OMA | LDEIPDC | |
| OrthoDB | EOG66F050 | |
| PhylomeDB | P28861 | |
| BioCyc | EcoCyc:FLAVONADPREDUCT-MONOMER ECOL316407:JW3895-MONOMER MetaCyc:FLAVONADPREDUCT-MONOMER | |
| EvolutionaryTrace | P28861 | |
| PRO | PR:P28861 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P28861 | |
| GO | GO:0005737 GO:0004324 GO:0016491 GO:0006001 GO:0042493 | |
| InterPro | IPR017927 IPR008333 IPR001433 IPR017938 | |
| Pfam | PF00970 PF00175 | |
| SUPFAM | SSF63380 | |
| PROSITE | PS51384 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11518 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0042493 |
response to drug |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006001 |
fructose catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004324 |
ferredoxin-NADP+ reductase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0071949 |
FAD binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0071949 |
FAD binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0016226 |
iron-sulfur cluster assembly |
ECO:0000314 |
direct assay 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 | |||
|
enables |
GO:0004324 |
ferredoxin-NADP+ reductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004324 |
ferredoxin-NADP+ reductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000303 |
response to superoxide |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000303 |
response to superoxide |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004324 |
ferredoxin-NADP+ reductase activity |
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 | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004324 |
ferredoxin-NADP+ reductase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
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 | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
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.
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Morimyo, M (1988) Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12. J. Bacteriol. 170 2136-42 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Kornberg, H (1986) The roles of HPr and FPr in the utilization of fructose by Escherichia coli. FEBS Lett. 194 12-5 PubMed GONUTS page
- ↑ Ingelman, M et al. (1997) The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution. J. Mol. Biol. 268 147-57 PubMed GONUTS page
- ↑ Fujii, K & Huennekens, FM (1974) Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system. J. Biol. Chem. 249 6745-53 PubMed GONUTS page
- ↑ Yan, R et al. (2015) Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly. Biochim. Biophys. Acta 1854 1113-7 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Bianchi, V et al. (1993) Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein. J. Bacteriol. 175 1590-5 PubMed GONUTS page
- ↑ Blaschkowski, HP et al. (1982) Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase. Eur. J. Biochem. 123 563-9 PubMed GONUTS page
- ↑ 10.0 10.1 Bianchi, V et al. (1995) Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat. J. Bacteriol. 177 4528-31 PubMed GONUTS page
