A0A6J4KAE5 · A0A6J4KAE5_9BACT
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids383 (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 | 117 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 118 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 119 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 143 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 144 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 145 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 145 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 169 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 192 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 198 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 205 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 210 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 211 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 214 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 214 | 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
- Strain
- Taxonomic lineageBacteria > Gemmatimonadota > environmental samples
Accessions
- Primary accessionA0A6J4KAE5
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-125 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | |||
Domain | 139-222 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | |||
Domain | 254-370 | DXP reductoisomerase C-terminal | |||
Sequence similarities
Belongs to the DXR family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)39,684
- Last updated2020-10-07 v1
- Checksum97C0FAE63A6BE70B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CADCTW010000022 EMBL· GenBank· DDBJ | CAA9300063.1 EMBL· GenBank· DDBJ | Genomic DNA |