A5UDR7 · DXR_HAEIE
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids397 (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 | 12 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 13 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 14 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 15 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 38 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 39 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 40 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 126 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 127 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 128 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 152 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 153 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 154 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 154 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 188 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 211 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 217 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 224 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 229 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 230 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 233 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 233 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Haemophilus
Accessions
- Primary accessionA5UDR7
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000020267 | 1-397 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase | |||
Sequence: MQKQNIVILGSTGSIGKSTLSVIENNPEKYHAFALVGGKNVETMFEQCIKFRPHFAALDDVNAAKILREKLIAHHIPTEVLAGQRAICELAAHPDADQIMASIVGAAGLLPTLSAVKAGKRVLLANKESLVTCGQLFIDAVKNYSAKLLPVDSEHNAIFQSLPPEAQEKIGFCPLSELGVSKIILTGSGGPFRYTPLEQFTNITPEQAVAHPNWSMGKKISVDSATMMNKGLEYIEARWLFNASAEEMEVIIHPQSIIHSMVRYVDGSVIAQMGNPDMRTPIAETMAYPHRTFAGVEPLDFFKIKELTFIEPDFNRYPNLKLAIDAFAAGQYATTAMNTANEIAVQAFLDRQISFMDIAKINLKTIEKISPYTIQNIDDVLEIDAQAREIAKTLIRE |
Structure
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)43,712
- Last updated2007-07-10 v1
- ChecksumFD1198F20F53FE57
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000671 EMBL· GenBank· DDBJ | ABQ98918.1 EMBL· GenBank· DDBJ | Genomic DNA |