A7H0K4 · DXR_CAMC5
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids365 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic activity
- 2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + H+ + NADPHThis reaction proceeds in the backward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Pathway
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 8 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 9 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 10 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 31 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 32 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 33 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 114 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 115 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 116 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 134 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 135 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 136 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 136 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 158 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 181 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 199 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 200 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 203 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 203 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NADPH binding | |
Biological Process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-deoxy-D-xylulose 5-phosphate reductoisomerase
- EC number
- Short namesDXP reductoisomerase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter
Accessions
- Primary accessionA7H0K4
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000020236 | 1-365 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase | |||
Sequence: MVILGSTGSIGTNTLEICSRHGVSVEALSCAKNIALLNEQIARFRPKFVCVADESLASEVKILKKSQIFVGAGGLLEMLEACHSQKVVNAIVGFAGLAPSLKTQELGKSLALANKESLVAGGKFLDTAKISPIDSEHFGLKFLLQNRTAPNRLIITASGGAFYRTPMKNLAKVTPSDALKHPNWSMGAKITIDSATMANKLFEVMEAFWLYGTSRIDALIEPTSMVHALVEFMDGSCTAHISRADMKLAIAHAVLENVSENVVAHADLLALKDIKFHKINLKKYPIFSLKEQVLERADLGVVINAANEVGVFAFLKGECRFLDISRIVLAAAKRFADVKIETKDEIFAIDAEVRNFTKRGLNAKI |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)39,640
- Last updated2007-09-11 v1
- ChecksumE941E52D95598B93
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000767 EMBL· GenBank· DDBJ | EAU01416.2 EMBL· GenBank· DDBJ | Genomic DNA |