Q053M2 · DXS_LEPBL
- Protein1-deoxy-D-xylulose-5-phosphate synthase
- Genedxs
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids635 (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 | 77 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 118-120 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GHA | ||||||
Binding site | 150 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 151-152 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: AS | ||||||
Binding site | 179 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 290 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 372 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
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 | 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 > Spirochaetota > Spirochaetia > Leptospirales > Leptospiraceae > Leptospira
Accessions
- Primary accessionQ053M2
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000019037 | 1-635 | 1-deoxy-D-xylulose-5-phosphate synthase | |||
Sequence: MQQESTLLDKIDYPADLRNIPLEKLPQVCKEVRNYIIDTLSGVGGHFASNLGVVELTVALHYVFDTPKDRLIWDVGHQTYPHKILTGRKDRLKTVRKFNGLSGFPKREESPYDLYNTGHAGTSISQALGEAAARDLTKGEDYSVVAIIGDASIATGMALEAMNHAGHLKKDMIVILNDNYMSISKNVGSISNYLNNIITSHFYNHWKRVFYTFLKWLPIVGPAAERFFKKVEKGFKDVLTPGGLFEDLGFGYIGPEDGHDVIRLVNMLAKVKKMKGPILLHLITQKGKGYDPAERDPIKYHGVTPFRKEDGAMDSGDTSKIAYSKIVGRMLSILTEANPKIAAITPAMIEGSGLKEYAEKYPDHLFDVGIAEQHSVAFAGAMTNGSIIPYMCIYSTFLTRAIDQLVQDVSLMNLPVRFVIDRAGCVGPDGETHQGLFDLGYLLGLPNMDVFVPSNGQDMIDSLRWMETYDKAPIAIRFPKANVDLKTLDFYKEVDLRPGTFRVLKRGTDLALLSIGSMIDEAKKATEILESAGFSVTLIDLIWLRPLGVEALNEELSNVRRFVIIDESYVDAGASGYLLNRILPENLSKYVKTFGFPPEPIHHGERKEIIQAYRLDGASIAESVADVLKKNLIKP |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length635
- Mass (Da)70,591
- Last updated2006-11-14 v1
- Checksum83D42B3C01EA9994
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000348 EMBL· GenBank· DDBJ | ABJ78473.1 EMBL· GenBank· DDBJ | Genomic DNA |