O08394 (CYPD_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 111.
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 bifunctional P-450/NADPH-P450 reductase 1 | ||||||
| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 1061 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Functions as a fatty acid monooxygenase. The reductase domain is required for electron transfer from NADP to cytochrome P450 By similarity. |
| Catalytic activity | NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. |
| Cofactor | FAD By similarity. FMN By similarity. Heme group By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the cytochrome P450 family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Cytoplasm |
| Ligand | FAD FMN Flavoprotein Heme Iron Metal-binding NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activityInferred from electronic annotation. Source: EC aromatase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion 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 – 1061 | 1061 | Probable bifunctional P-450/NADPH-P450 reductase 1 | PRO_0000052206 | |||||
Regions | |||||||||
| Domain | 493 – 632 | 140 | Flavodoxin-like | ||||||
| Domain | 671 – 904 | 234 | FAD-binding FR-type | ||||||
| Region | 1 – 474 | 474 | Cytochrome P450 | ||||||
| Region | 475 – 1061 | 587 | NADPH-P-450 reductase | ||||||
Sites | |||||||||
| Metal binding | 403 | 1 | Iron (heme axial ligand) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of the Bacillus subtilis genome region in the vicinity of the lev operon reveals two new extracytoplasmic function RNA polymerase sigma factors SigV and SigZ." Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J., Duesterhoeft A., Ehrlich S.D. Microbiology 143:2939-2943(1997) [PubMed] [Europe PMC] [Abstract] 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D87979 Genomic DNA. Translation: BAA20123.1. AL009126 Genomic DNA. Translation: CAB12544.1. |
| PIR | D69799. |
| RefSeq | NP_388606.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O08394. |
| SMR | O08394. Positions 7-454, 476-1059. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU07250. |
Proteomic databases | |
| PaxDb | O08394. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12544; CAB12544; BSU07250. |
| GeneID | 938784. |
| KEGG | bsu:BSU07250. |
| PATRIC | 18973100. VBIBacSub10457_0764. |
Organism-specific databases | |
| GenoList | BSU07250. [Micado] |
Phylogenomic databases | |
| eggNOG | COG2124. |
| HOGENOM | HOG000093545. |
| KO | K14338. |
| OMA | CEIRFER. |
| ProtClustDB | CLSK886838. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU07250-MONOMER. |
| SABIO-RK | O08394. |
Family and domain databases | |
| Gene3D | 1.10.630.10. 1 hit. 1.20.990.10. 1 hit. |
| InterPro | IPR023206. Bifunctional_P450_P450_red. IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| Pfam | PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF00067. p450. 1 hit. [Graphical view] |
| PIRSF | PIRSF000209. Bifunctional_P450_P450R. 1 hit. |
| PRINTS | PR00369. FLAVODOXIN. PR00371. FPNCR. |
| SUPFAM | SSF48264. Cytochrome_P450. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYPD_BACSU | ||||||||
| Accession | Primary (citable) accession number: O08394 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
