O33064 (FPRB_MYCLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable ferredoxin/ferredoxin--NADP reductase Short name=FNR EC=1.18.1.2 | ||||||
| Gene names |
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| Organism | Mycobacterium leprae [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1769 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 555 AA. |
| Sequence status | Complete. |
| 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 555 | 555 | Probable ferredoxin/ferredoxin--NADP reductase | PRO_0000167674 | |||||
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 | 460 – 462 | 3 | FAD By similarity | ||||||
| Region | 115 – 555 | 441 | 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 | 453 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 460 | 1 | NADP; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G.Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z99494 Genomic DNA. Translation: CAB16679.1. AL583924 Genomic DNA. Translation: CAC31089.1. |
| PIR | T45351. |
| RefSeq | NP_302407.1. NC_002677.1. |
3D structure databases | |
| ProteinModelPortal | O33064. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000029433; EBMYCP00000029039; EBMYCG00000029428. |
| GeneID | 909093. |
| GenomeReviews | Gene locus ML2134 in contig AL450380_GR. |
| KEGG | mle:ML2134. |
| NMPDR | fig|272631.1.peg.1279. |
| PATRIC | 18058227. VBIMycLep78757_4036. |
Organism-specific databases | |
| Leproma | ML2134. |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000014581. |
| HOGENOM | HBG522200. |
| OMA | AWINGHP. |
| ProtClustDB | CLSK790809. |
Enzyme and pathway databases | |
| BioCyc | MLEP272631:ML2134-MONOMER. |
Family and domain databases | |
| InterPro | IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR021163. Adrenodoxin_Rdtase. IPR016040. NAD(P)-bd_dom. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00528. |
| Pfam | PF00037. Fer4. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000362. FNR. 1 hit. |
| PROSITE | PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FPRB_MYCLE | ||||||||
| Accession | Primary (citable) accession number: O33064 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with