Reviewed,
UniProtKB/Swiss-Prot Q73EA6 (FENR1_BACC1)
Last modified
January 19, 2010.
Version 44.
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 1 Short name=Fd-NADP+ reductase 1 Short name=FNR 1 EC=1.18.1.2 | ||
| Gene names |
| ||
| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 222523 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 349 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01685 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01685 |
| 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 – 349 | 349 | Ferredoxin--NADP reductase 1 HAMAP MF_01685 | PRO_0000364788 | |||||
Sites | |||||||||
| Binding site | 36 | 1 | FAD By similarity | ||||||
| Binding site | 44 | 1 | FAD By similarity | ||||||
| Binding site | 48 | 1 | FAD By similarity | ||||||
| Binding site | 88 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 123 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 290 | 1 | FAD By similarity | ||||||
| Binding site | 331 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS39388.1. |
| RefSeq | NP_976780.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q73EA6. |
Genome annotation databases | |
| GeneID | 2749891. |
| GenomeReviews | Gene locus BCE_0452 in contig AE017194_GR. |
| KEGG | bca:BCE_0452. |
| NMPDR | fig|222523.1.peg.452. |
| TIGR | BCE_0452. |
Phylogenomic databases | |
| eggNOG | COG0492. |
| HOGENOM | HBG669726. |
| OMA | KKVYVTY. |
Family and domain databases | |
| HAMAP | MF_01685. FENR2. [Tree] |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [Graphical view] |
| Pfam | PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| ProtoNet | Search... |
Entry information
| Entry name | FENR1_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q73EA6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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