Reviewed,
UniProtKB/Swiss-Prot Q44549 (FENR_ANAVT)
Last modified
November 3, 2009.
Version 76.
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 variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 240292 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena |
Protein attributes
| Sequence length | 440 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. |
| 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 | internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell phycobilisomeInferred from electronic annotation. Source: UniProtKB-KW thylakoid membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred 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_0000167634 | |||||
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
| « Hide 'large scale' references | |
| [1] | "Cloning and molecular characterization of the petH gene in the cyanobacterium Anabaena variabilis ATCC 29413." Mannan R.M., Matthijs H.C.P., Pakrasi H.B. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| L26346 Genomic DNA. Translation: AAA91046.1. CP000117 Genomic DNA. Translation: ABA20406.1. | |
| RefSeq | YP_321301.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QUE based on UniProtKB P21890. |
| SMR | Q44549. Positions 146-440. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q44549. |
Genome annotation databases | |
| GeneID | 3680507. |
| GenomeReviews | Gene locus Ava_0782 in contig CP000117_GR. |
| KEGG | ava:Ava_0782. |
| NMPDR | fig|240292.3.peg.2575. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q44549. |
| OMA | GRMYIQD. |
Enzyme and pathway databases | |
| BioCyc | AVAR240292:AVA_0782-MON. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012146. Frd-NADP+_RD. IPR015701. FRD_Red. IPR001433. OxRdtase_FAD/NAD_bd. IPR008213. Phycobilisome_lnk_CpcD-like. [Graphical view] |
| PANTHER | PTHR19384:SF1. FRD_Red. 1 hit. |
| Pfam | PF01383. CpcD. 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_ANAVT | ||||||||
| Accession | Primary (citable) accession number: Q44549 Secondary accession number(s): Q3MF30 | ||||||||
| 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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