Reviewed,
UniProtKB/Swiss-Prot Q65FE0 (FENR2_BACLD)
Last modified
November 3, 2009.
Version 47.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Ferredoxin--NADP reductase 2 Short name=Fd-NADP+ reductase 2 Short name=FNR 2 EC=1.18.1.2 | ||
| Gene names |
| ||
| Organism | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 279010 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. HAMAP 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. |
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 | FAD binding Inferred from electronic annotation. Source: HAMAP NADP or NADPH bindingInferred from electronic annotation. Source: HAMAP ferredoxin-NADP+ reductase activityInferred 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 – 332 | 332 | Ferredoxin--NADP reductase 2 HAMAP MF_01685 | PRO_0000364798 | |||||
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 | 124 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 285 | 1 | FAD By similarity | ||||||
| Binding site | 326 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000002 Genomic DNA. Translation: AAU24855.1. AE017333 Genomic DNA. Translation: AAU42224.1. | |
| RefSeq | YP_080493.1. YP_092917.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65FE0. |
Genome annotation databases | |
| GeneID | 3027567. 3099711. |
| GenomeReviews | Gene locus BLi03393 in contig AE017333_GR. Gene locus BL03143 in contig CP000002_GR. |
| KEGG | bld:BLi03393. bli:BL03143. |
| NMPDR | fig|279010.5.peg.3642. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q65FE0. |
| OMA | DWALMLE. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010:BL03143-MON. |
Family and domain databases | |
| HAMAP | MF_01685. [Tree] |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. 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. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | FENR2_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65FE0 Secondary accession number(s): Q62QV5 | ||||||||
| 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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