A0A6L8T9Q2 · A0A6L8T9Q2_9FIRM
- Protein1-deoxy-D-xylulose-5-phosphate synthase
- Genedxs
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids627 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic activity
- D-glyceraldehyde 3-phosphate + H+ + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 thiamine pyrophosphate per subunit.
Pathway
Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 71 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 112-114 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GHS | ||||||
Binding site | 143 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 144-145 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 172 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 172 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 283 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 364 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 1-deoxy-D-xylulose-5-phosphate synthase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | 1-deoxy-D-xylulose 5-phosphate biosynthetic process | |
Biological Process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway | |
Biological Process | terpenoid biosynthetic process | |
Biological Process | thiamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-deoxy-D-xylulose-5-phosphate synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Blautia
Accessions
- Primary accessionA0A6L8T9Q2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 313-478 | Transketolase-like pyrimidine-binding | ||||
Sequence: PTYTDHFSGAICSLAEKNKKVVAITAAMPDGTGLNRFRKKFPERFFDVGIAEEHAVTFAAGMALGGMVPVFAVYSSFLQRGIDQILHDVCMQDLHVIFAIDRAGFVGADGETHHGCFDLSYLSMIPNMTVMAPKNGKELEEMLKFAVEELDGPCAIRYPKGSACTD |
Sequence similarities
Belongs to the transketolase family. DXPS subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length627
- Mass (Da)68,686
- Last updated2020-10-07 v1
- ChecksumD4E19AC5D46CDC99