Reviewed,
UniProtKB/Swiss-Prot P28901 (FENR_SHIFL)
Last modified
June 16, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ferredoxin--NADP reductase Short name=FNR EC=1.18.1.2 Alternative name(s): Flavodoxin reductase Short name=FLXR Methyl viologen resistance protein A | ||||||
| Gene names |
| ||||||
| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 623 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
Protein attributes
| Sequence length | 248 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Together with flavodoxin is involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen By similarity. |
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. |
| Cofactor | FAD. |
| Sequence similarities | Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 FAD-binding FR-type domain. |
| Sequence caution | The sequence CAA77813.1 differs from that shown. Reason: Frameshift at positions 94 and 126. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 248 | 248 | Ferredoxin--NADP reductase | PRO_0000167644 | |||||
Regions | |||||||||
| Domain | 2 – 101 | 100 | FAD-binding FR-type | ||||||
| Nucleotide binding | 50 – 53 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 73 – 76 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 143 – 144 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 173 – 174 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 213 – 214 | 2 | NADP By similarity | ||||||
Sites | |||||||||
| Binding site | 53 | 1 | NADP By similarity | ||||||
| Binding site | 116 | 1 | FAD By similarity | ||||||
| Binding site | 116 | 1 | NADP; via amide nitrogen By similarity | ||||||
| Binding site | 245 | 1 | NADP By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
| [3] | "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri." Truniger V., Boos W., Sweet G. J. Bacteriol. 174:6981-6991(1992) [PubMed: 1400248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135. Strain: M4243. |
Cross-references
Sequence databases | |
|---|---|
| AE005674 Genomic DNA. Translation: AAN45435.1. AE014073 Genomic DNA. Translation: AAP18765.1. Z11766 Genomic DNA. Translation: CAA77813.1. Frameshift. | |
| PIR | S23906. |
| RefSeq | NP_709728.1. NP_838954.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FDR based on UniProtKB P28861. |
| SMR | P28901. Positions 2-248. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1023471. 1079956. |
| GenomeReviews | Gene locus SF4002 in contig AE005674_GR. Gene locus S3745 in contig AE014073_GR. |
| KEGG | sfl:SF4002. sfx:S3745. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P28901. |
| OMA | P28901. IMLCGNP. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN45435.1-MON. |
| BRENDA | 1.18.1.2. 189495. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FENR_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P28901 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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