Reviewed,
UniProtKB/Swiss-Prot O05268 (FENR2_BACSU)
Last modified
November 3, 2009.
Version 65.
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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 2 Short name=Fd-NADP+ reductase 2 Short name=FNR 2 EC=1.18.1.2 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. Ref.4 |
| Cofactor | Binds 1 FAD per subunit. Ref.4 |
| Subunit structure | Homodimer. Ref.4 |
| Sequence similarities | Belongs to the ferredoxin--NADP reductase type 2 family. |
| Biophysicochemical properties | Kinetic parameters: KM for NADH is < 0.1 µM. KM=0.54 µM for NADPH (at 24 degrees Celsius and pH 7.0) HAMAP MF_01685 |
Ontologies
| Keywords | |
|---|---|
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| 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 – 332 | 332 | Ferredoxin--NADP reductase 2 HAMAP MF_01685 | PRO_0000360548 | |||||
Sites | |||||||||
| Binding site | 37 | 1 | FAD By similarity | ||||||
| Binding site | 45 | 1 | FAD By similarity | ||||||
| Binding site | 50 | 1 | FAD By similarity | ||||||
| Binding site | 90 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 124 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 285 | 1 | FAD By similarity | ||||||
| Binding site | 326 | 1 | FAD By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 105 – 116 | 12 | TNEET…SKTVI → QMKKPTTLKRSC in CAB07954. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Bacillus genome sequence project: sequence of yumA to pai; a segment of the bacillus genome at about 284 degrees." Oudega B., Koningsteyn G., Ramon-De Haan M., Rodrigues L. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.  Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 105-116. |
| [4] | "Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC." Seo D., Kamino K., Inoue K., Sakurai H. Arch. Microbiol. 182:80-89(2004) [PubMed: 15252706] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-17, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR. |
Cross-references
Sequence databases | |
|---|---|
| Z93939 Genomic DNA. Translation: CAB07954.1. AL009126 Genomic DNA. Translation: CAB15201.2. | |
| PIR | B70015. |
| RefSeq | NP_391091.2. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 936577. |
| GenomeReviews | Gene locus BSU32110 in contig AL009126_GR. |
| KEGG | bsu:BSU32110. |
| NMPDR | fig|224308.1.peg.3217. |
Organism-specific databases | |
| SubtiList | BG12391. yumC. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O05268. |
| OMA | DWALMLE. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3208-MON. |
Family and domain databases | |
| HAMAP | MF_01685. [Tree] |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | FENR2_BACSU | ||||||||
| Accession | Primary (citable) accession number: O05268 Secondary accession number(s): Q795K8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |
