A0A2G5WXN9 · A0A2G5WXN9_9BACL
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids384 (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 | 10 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 11 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 13 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 36 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 37 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 38 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 120 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 121 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 122 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 146 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 147 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 148 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 148 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 172 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 195 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 201 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 208 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 213 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 214 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 217 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 217 | 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 > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina
Accessions
- Primary accessionA0A2G5WXN9
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-128 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | |||
Domain | 142-225 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | |||
Domain | 257-374 | DXP reductoisomerase C-terminal | |||
Sequence similarities
Belongs to the DXR family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)42,551
- Last updated2018-01-31 v1
- MD5 Checksum64C9F063C49AA6767EF5ADF807BEB74A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PDYN01000001 EMBL· GenBank· DDBJ | PIC68740.1 EMBL· GenBank· DDBJ | Genomic DNA |