Reviewed,
UniProtKB/Swiss-Prot P65529 (FPRB_MYCBO)
Last modified
June 16, 2009.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable ferredoxin/ferredoxin--NADP reductase Short name=FNR EC=1.18.1.2 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 575 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 | Binds 1 or 2 4Fe-4S clusters. FAD. |
| Sequence similarities | In the C-terminal section; belongs to the ferredoxin--NADP reductase family. Contains 2 4Fe-4S ferredoxin-type domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Domain | Repeat |
| Ligand | 4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 575 | 575 | Probable ferredoxin/ferredoxin--NADP reductase | PRO_0000167675 | |||||
Regions | |||||||||
| Domain | 2 – 29 | 28 | 4Fe-4S ferredoxin-type 1 | ||||||
| Domain | 37 – 66 | 30 | 4Fe-4S ferredoxin-type 2 | ||||||
| Nucleotide binding | 258 – 261 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 302 – 303 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 463 – 465 | 3 | FAD By similarity | ||||||
| Region | 115 – 575 | 461 | Ferredoxin--NADP reductase | ||||||
Sites | |||||||||
| Metal binding | 9 | 1 | Iron-sulfur 1 By similarity | ||||||
| Metal binding | 15 | 1 | Iron-sulfur 1 By similarity | ||||||
| Metal binding | 19 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 46 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 49 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 52 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 56 | 1 | Iron-sulfur 1 By similarity | ||||||
| Binding site | 123 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 143 | 1 | FAD By similarity | ||||||
| Binding site | 151 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 187 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 213 | 1 | NADP By similarity | ||||||
| Binding site | 314 | 1 | NADP By similarity | ||||||
| Binding site | 456 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 463 | 1 | NADP; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| BX248336 Genomic DNA. Translation: CAD93771.1. | |
| RefSeq | NP_854567.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H98 based on UniProtKB P03942. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1092796. |
| GenomeReviews | Gene locus Mb0910 in contig BX248333_GR. |
| KEGG | mbo:Mb0910. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P65529. |
| OMA | P65529. DRIKEVP. |
Enzyme and pathway databases | |
| BRENDA | 1.18.1.2. 3091. |
Family and domain databases | |
| InterPro | IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR000759. Adrndx_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00037. Fer4. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00419. ADXRDTASE. |
| PROSITE | PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FPRB_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P65529 Secondary accession number(s): Q10547 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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