Reviewed,
UniProtKB/Swiss-Prot O31753 (DXR_BACSU)
Last modified
November 3, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (3) |
 Third-party data |
 Customize display | text xml rdf/xml gff fasta |
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: 1-deoxy-D-xylulose 5-phosphate reductoisomerase Short name=DXP reductoisomerase EC=1.1.1.267 Alternative name(s): 1-deoxyxylulose-5-phosphate reductoisomerase 2-C-methyl-D-erythritol 4-phosphate synthase | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 383 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity. |
| Catalytic activity | 2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183 |
| Cofactor | Divalent cation By similarity. |
| Pathway | Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183 |
| Sequence similarities | Belongs to the DXR family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Isoprene biosynthesis |
| Ligand | Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW terpenoid biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: HAMAP metal 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 – 383 | 383 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183 | PRO_0000163610 | |||||
Regions | |||||||||
| Nucleotide binding | 7 – 36 | 30 | NADP By similarity | ||||||
Sites | |||||||||
| Metal binding | 148 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 150 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 219 | 1 | Divalent metal cation By similarity | ||||||
| Binding site | 123 | 1 | Substrate By similarity | ||||||
| Binding site | 150 | 1 | Substrate By similarity | ||||||
| Binding site | 174 | 1 | Substrate By similarity | ||||||
| Binding site | 197 | 1 | Substrate By similarity | ||||||
| Binding site | 219 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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. |
| [2] | "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 C-TERMINUS. |
Cross-references
Sequence databases | |
|---|---|
| AL009126 Genomic DNA. Translation: CAB13528.2. | |
| PIR | B69881. |
| RefSeq | NP_389537.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K5H based on UniProtKB P45568. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 939636. |
| GenomeReviews | Gene locus BSU16550 in contig AL009126_GR. |
| KEGG | bsu:BSU16550. |
| NMPDR | fig|224308.1.peg.1658. |
Organism-specific databases | |
| SubtiList | BG13409. dxr. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O31753. |
| OMA | IHSMVEY. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1656-MON. |
| BRENDA | 1.1.1.267. 150. |
Family and domain databases | |
| HAMAP | MF_00183. [Tree] |
| InterPro | IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [Graphical view] |
| Pfam | PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DXR_BACSU | ||||||||
| Accession | Primary (citable) accession number: O31753 | ||||||||
| Entry history |
| ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
