A0A2C8F2Q8 · A0A2C8F2Q8_9BACT
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids399 (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 + NADPH + H+This 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 | 27 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 28 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 29 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 30 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 53 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 55 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 140 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 141 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 142 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 166 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 167 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 168 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 168 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 193 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 216 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 222 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 229 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 234 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 235 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 238 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 238 | Mn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity | |
Molecular Function | isomerase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | NADPH binding | |
Biological Process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae
Accessions
- Primary accessionA0A2C8F2Q8
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 21-148 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | |||
Domain | 162-246 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | |||
Domain | 278-394 | DXP reductoisomerase C-terminal | |||
Sequence similarities
Belongs to the DXR family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)42,907
- Last updated2017-12-20 v1
- MD5 ChecksumC2B245F211627AA1DB2524A1DB3AC277
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LT907975 EMBL· GenBank· DDBJ | SOB56878.1 EMBL· GenBank· DDBJ | Genomic DNA |