Reviewed,
UniProtKB/Swiss-Prot A7H243 (DXR_CAMJD)
Last modified
November 3, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 | Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360109 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 356 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 – 356 | 356 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183 | PRO_1000020239 | |||||
Regions | |||||||||
| Nucleotide binding | 4 – 30 | 27 | NADP By similarity | ||||||
Sites | |||||||||
| Metal binding | 131 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 133 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 200 | 1 | Divalent metal cation By similarity | ||||||
| Binding site | 112 | 1 | Substrate By similarity | ||||||
| Binding site | 133 | 1 | Substrate By similarity | ||||||
| Binding site | 155 | 1 | Substrate By similarity | ||||||
| Binding site | 178 | 1 | Substrate By similarity | ||||||
| Binding site | 200 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000768 Genomic DNA. Translation: ABS43260.1. | |
| RefSeq | YP_001397573.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7H243. |
Genome annotation databases | |
| GeneID | 5390301. |
| GenomeReviews | Gene locus JJD26997_0364 in contig CP000768_GR. |
| KEGG | cjd:JJD26997_0364. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | IHSMVEY. |
Family and domain databases | |
| HAMAP | MF_00183. [Tree] |
| InterPro | IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [Graphical view] |
| Pfam | PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. [Graphical view] |
| PIRSF | PIRSF006205. Dxp_reductismrs. 1 hit. |
| TIGRFAMs | TIGR00243. Dxr. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DXR_CAMJD | ||||||||
| Accession | Primary (citable) accession number: A7H243 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


