A0A799GJM0 · A0A799GJM0_ECOLX
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- GeneispC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids398 (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 | 10 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 11 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 13 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 36 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 37 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 38 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 124 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 125 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 126 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 150 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 151 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 152 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 152 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 186 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 209 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 215 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 222 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 227 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 228 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 231 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 231 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity | |
Molecular Function | isomerase 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
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A799GJM0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-132 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | ||||
Sequence: LTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQSACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCG | ||||||
Domain | 146-239 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | ||||
Sequence: LLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLF | ||||||
Domain | 271-387 | DXP reductoisomerase C-terminal | ||||
Sequence: LGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANARE |
Sequence similarities
Belongs to the DXR family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)43,404
- Last updated2020-12-02 v1
- ChecksumD15D96E77EFBC6B7