P28861 · FENR_ECOLI
- ProteinFlavodoxin/ferredoxin--NADP reductase
- Genefpr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transports electrons between flavodoxin or ferredoxin and NADPH (PubMed:12234497, PubMed:21306142, PubMed:8449868, PubMed:9839946).
Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497).
Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617).
Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497).
Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617).
Catalytic activity
- H+ + NADP+ + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.85 μM | NADPH | |||||
3.9 μM | NADPH | |||||
2.04 mM | NADH | |||||
12 μM | ferredoxin | |||||
7.6 μM | flavodoxin 1 | |||||
4 μM | flavodoxin 2 | |||||
6.84 μM | flavodoxin | |||||
17.6 μM | cytochrome c | |||||
23.6 μM | potassium ferricyanide |
kcat is 338.9 min-1 with NADPH as the donor. kcat is 33 min-1 with NADP as the donor (PubMed:11085917).
kcat is 0.15 sec-1 with ferredoxin as substrate. kcat is 0.0042 sec-1 with flavodoxin 1 as substrate. kcat is 0.0039 sec-1 with flavodoxin 2 as substrate (PubMed:12234497).
kcat is 0.15 sec-1 with ferredoxin as substrate. kcat is 0.0042 sec-1 with flavodoxin 1 as substrate. kcat is 0.0039 sec-1 with flavodoxin 2 as substrate (PubMed:12234497).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 50-53 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RAYS | ||||||
Binding site | 66 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 74-76 | FAD (UniProtKB | ChEBI) | ||||
Sequence: KLS | ||||||
Binding site | 116 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 143-144 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: AR | ||||||
Binding site | 173-174 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 184 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214-216 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NPQ | ||||||
Binding site | 220 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 247-248 | FAD (UniProtKB | ChEBI) | ||||
Sequence: YW |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aconitate hydratase activity | |
Molecular Function | FAD binding | |
Molecular Function | ferredoxin-NADP+ reductase activity | |
Molecular Function | succinate dehydrogenase activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | heme catabolic process | |
Biological Process | iron-sulfur cluster assembly | |
Biological Process | response to superoxide | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlavodoxin/ferredoxin--NADP reductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP28861
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
The deletion mutant is highly sensitive to methyl viologen.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 126 | No change in enzyme activity. Crystallized in 1FDR and 2XNJ. | ||||
Sequence: Q → R | ||||||
Mutagenesis | 144 | Increases Km for NADPH. 2-fold decrease in catalytic efficiency. | ||||
Sequence: R → A | ||||||
Mutagenesis | 174 | Increases Km for NADPH. 13-fold decrease in catalytic efficiency. | ||||
Sequence: R → A | ||||||
Mutagenesis | 184 | Increases Km for NADPH. 15-fold decrease in catalytic efficiency. | ||||
Sequence: R → A |
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000167643 | 2-248 | Flavodoxin/ferredoxin--NADP reductase | |||
Sequence: ADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPHCETLWMLATGTAIGPYLSILQLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGSLTGRIPALIESGELESTIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-101 | FAD-binding FR-type | ||||
Sequence: ADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLD |
Sequence similarities
Belongs to the ferredoxin--NADP reductase type 1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length248
- Mass (Da)27,751
- Last updated2007-01-23 v4
- ChecksumCBF46435A95709E4
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L04757 EMBL· GenBank· DDBJ | AAA23805.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L19201 EMBL· GenBank· DDBJ | AAB03056.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77386.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z11767 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M19644 EMBL· GenBank· DDBJ | AAA24189.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |