A0A522DF09 · A0A522DF09_9MICO
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids359 (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 | 38 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 100 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 101 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 102 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 124 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 126 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 126 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 150 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 173 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 179 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 186 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 191 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 192 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 195 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 195 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Salinibacterium
Accessions
- Primary accessionA0A522DF09
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-65 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | ||||
Sequence: VIVLGSTGSIGTQALEVIAANRDRFKVVGLSAGSNRDALAQQAAAFGVEHVALGADEAMQLV | ||||||
Domain | 120-203 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | ||||
Sequence: IVPVDSEHSALAQALRAGSSSEVRRLVLTASGGPFRGRSRESLREVTPQEALAHPTWDMGLVVTTNSATLVNKGLEIIEAHLLF | ||||||
Domain | 236-350 | DXP reductoisomerase C-terminal | ||||
Sequence: SPPDMRLPISLGLDWPNRVAGVGAPLDWSAASEWTFEPLDTEVFTAVALAKRVGEAGSTWPAVFNAANEQAVLAFHAGHIGYLDILDIVEEVVDLHQPQGLSLELVFEAERWART |
Sequence similarities
Belongs to the DXR family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)37,747
- Last updated2019-10-16 v1
- Checksum88EB89627F00EA1B