A0A4Y9QK11 · A0A4Y9QK11_9BACT
- Protein1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Genedxr
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids388 (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 | 13 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 14 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 15 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 16 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 41 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 125 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 126 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 127 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 151 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 153 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 153 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 177 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 200 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 206 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 213 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 218 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 219 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 222 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 222 | 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 > Bacteroidota > Cytophagia > Cytophagales > Cyclobacteriaceae > Algoriphagus
Accessions
- Primary accessionA0A4Y9QK11
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-133 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal | ||||
Sequence: VAILGSTGSIGRQTLDVIRQHPEDFQVEVLTAQNNCDLLIQQALEFQPNAVVITNEAKYQVVKDALIPHDIKVFAGPKALAQVVEMETIDVVLTALVGYSGLIPTVQAIRAGKQIALANKETLVVAG | ||||||
Domain | 147-230 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | ||||
Sequence: IYPVDSEHSAIFQCLVGEWHNPIEKIILTASGGPFRGKDRQFLESVTKEQALKHPNWDMGAKITIDSASLMNKGLEVIEAKWLF | ||||||
Domain | 262-378 | DXP reductoisomerase C-terminal | ||||
Sequence: LGLPDMRIPIQFALSYPHRLKSDFERFDFLNYPNLTFEQPDLKTFRNLQLAFDALEKGGNAPCMLNAANEIAVEAFLKDQIGFLQMSELIENAMNRADFISHPSLEDYVASDEQVRT |
Sequence similarities
Belongs to the DXR family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)43,205
- Last updated2019-09-18 v1
- Checksum2B7FC73A363E7492
Keywords
- Technical term