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ECOLI:FENR

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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

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11518
PANTHER:PTN000452442

C

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:2834327[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:3510127[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006001

fructose catabolic process

PMID:3510127[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:3510127[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004324

ferredoxin-NADP+ reductase activity

PMID:3510127[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0071949

FAD binding

PMID:9149148[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0071949

FAD binding

PMID:4154078[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:25688831[6]

ECO:0000314

direct assay 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

enables

GO:0004324

ferredoxin-NADP+ reductase activity

PMID:8449868[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004324

ferredoxin-NADP+ reductase activity

PMID:7042345[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000303

response to superoxide

PMID:7635836[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000303

response to superoxide

PMID:7635836[10]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004324

ferredoxin-NADP+ reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033892

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:IPR001433
InterPro:IPR017927

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001433
InterPro:IPR017927

P

Seeded From UniProt

complete

enables

GO:0004324

ferredoxin-NADP+ reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.18.1.2

F

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

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

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. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. 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. 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
  4. 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
  5. 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
  6. 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
  7. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. 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
  9. 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. 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