O31475 (FENR1_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ferredoxin--NADP reductase 1 Short name=FNR 1 Short name=Fd-NADP(+) reductase 1 EC=1.18.1.2 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 336 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. HAMAP-Rule MF_01685 |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the ferredoxin--NADP reductase type 2 family. |
| Sequence caution | The sequence BAA08961.1 differs from that shown. Reason: Frameshift at positions 49 and 104. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Molecular_function | NADP binding Inferred from electronic annotation. Source: HAMAP ferredoxin-NADP+ reductase activityInferred from electronic annotation. Source: HAMAP flavin adenine dinucleotide bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 336 | 336 | Ferredoxin--NADP reductase 1 HAMAP-Rule MF_01685 | PRO_0000364801 | |||||
Sites | |||||||||
| Binding site | 37 | 1 | FAD By similarity | ||||||
| Binding site | 45 | 1 | FAD By similarity | ||||||
| Binding site | 50 | 1 | FAD By similarity | ||||||
| Binding site | 90 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 125 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 287 | 1 | FAD By similarity | ||||||
| Binding site | 328 | 1 | FAD By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes." Yamane K., Kumano M., Kurita K. Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D50453 Genomic DNA. Translation: BAA08961.1. Frameshift. AL009126 Genomic DNA. Translation: CAB12121.1. |
| PIR | G69759. |
| RefSeq | NP_388209.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O31475. |
| SMR | O31475. Positions 6-330. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU03270. |
Proteomic databases | |
| PaxDb | O31475. |
| PRIDE | O31475. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12121; CAB12121; BSU03270. |
| GeneID | 938327. |
| KEGG | bsu:BSU03270. |
| PATRIC | 18972213. VBIBacSub10457_0335. |
Organism-specific databases | |
| GenoList | BSU03270. |
Phylogenomic databases | |
| eggNOG | COG0492. |
| HOGENOM | HOG000072909. |
| KO | K00384. |
| OMA | FGGHEKN. |
| ProtClustDB | CLSK886666. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU03270-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01685. FENR2. |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR022890. Fd--NADP_Rdtase_type_2. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| ProtoNet | Search... |
Entry information
| Entry name | FENR1_BACSU | ||||||||
| Accession | Primary (citable) accession number: O31475 Secondary accession number(s): P94397 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
