Reviewed,
UniProtKB/Swiss-Prot P58558 (FENR_ANASP)
Last modified
February 9, 2010.
Version 67.
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 | ||||
| Gene names |
| ||||
| Organism | Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. |
| Cofactor | FAD. |
| Subcellular location | Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes By similarity. |
| Sequence similarities | Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 cpcD-like domain. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Phycobilisome Thylakoid |
| 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 |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell phycobilisomeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH bindingInferred 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 – 440 | 440 | Ferredoxin--NADP reductase | PRO_0000167633 | |||||
Regions | |||||||||
| Domain | 17 – 75 | 59 | CpcD-like | ||||||
| Domain | 155 – 279 | 125 | FAD-binding FR-type | ||||||
| Nucleotide binding | 214 – 217 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 235 – 237 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 253 – 255 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 330 – 331 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 360 – 361 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 370 – 374 | 5 | NADP By similarity | ||||||
| Nucleotide binding | 399 – 400 | 2 | NADP By similarity | ||||||
Sites | |||||||||
| Binding site | 217 | 1 | NADP By similarity | ||||||
| Binding site | 237 | 1 | NADP By similarity | ||||||
| Binding site | 241 | 1 | FAD By similarity | ||||||
| Binding site | 294 | 1 | FAD By similarity | ||||||
| Binding site | 294 | 1 | NADP; via amide nitrogen By similarity | ||||||
| Binding site | 438 | 1 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. Tabata S.DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000019 Genomic DNA. Translation: BAB75820.1. |
| PIR | AB2321. |
| RefSeq | NP_488161.1. |
3D structure databases | |
| SMR | P58558. Positions 138-440. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P58558. |
Genome annotation databases | |
| GeneID | 1107723. |
| GenomeReviews | Gene locus all4121 in contig BA000019_GR. |
| KEGG | ana:all4121. |
| NMPDR | fig|103690.1.peg.4428. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0369. |
| HOGENOM | HBG353752. |
| OMA | ANGKPHK. |
Enzyme and pathway databases | |
| BioCyc | NSP103690:ALL4121-MONOMER. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012146. Frd-NADP+_RD. IPR015701. FRD_Red. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR008213. Phycobilisome_lnk_CpcD-like. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| PANTHER | PTHR19384:SF1. FRD_Red. 1 hit. |
| Pfam | PF01383. CpcD. 1 hit. PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF000361. Frd-NADP+_RD. 1 hit. |
| PRINTS | PR00371. FPNCR. |
| PROSITE | PS51441. CPCD_LIKE. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FENR_ANASP | ||||||||
| Accession | Primary (citable) accession number: P58558 | ||||||||
| 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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