B5ZAB7 · DXS_HELPG
- Protein1-deoxy-D-xylulose-5-phosphate synthase
- Genedxs
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids618 (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 + pyruvate + H+ = 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 | 70 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 111-113 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GHS | ||||||
Binding site | 142 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 143-144 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 171 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 171 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 278 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 360 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter
Accessions
- Primary accessionB5ZAB7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000115746 | 1-618 | 1-deoxy-D-xylulose-5-phosphate synthase | |||
Sequence: MILQNRTFDLNPNDIAGLELVCQTLRNRILEVVSANGGHLSSSLGAVELIVGMHALFDCQKNPFIFDTSHQAYAHKLLTGRFESFSTLRQFKGLSGFTKPSESAYDYFIAGHSSTSVSIGVGVAKAFCLKQALGMPIALLGDGSISAGIFYEALNELGDRKYPMIMILNDNEMSISTPIGALSKALSQLMKGPFYQSFRSKVKKILSTLPESVNYLASRFEESFKLITPGVFFEELGINYIGPINGHDLSAIIETLKLAKELKEPVLIHAQTLKGKGYKIAEGRYEKWHGVGPFDLDTGLSKKSKSAILSPTEAYSNTLLELAKKDEKIVGVTAAMPSGTGLDKLIDAYPLRFFDVAIAEQHALTSSSAMAKEGFKPFVSIYSTFLQRAYDSIVHDACISSLPIKLAIDRAGIVGEDGETHQGLLDVSYLRSIPNMVIFAPRDNETLKNAVRFANEHDSSPCAFRYPRGSFVLKEGVFEPSGFVLGQSELLKKEGEILLIGYGNGVGRAHLVQLALKEKNIECALLDLRFLKPLDPNLSAIVAPYQKLYVFSDNYKLGGVASAILEFLSEQNILKPVKSFEIIDEFIMHGNTALVEKSLGLDTESLTDAILKDLGQER |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length618
- Mass (Da)67,690
- Last updated2008-11-25 v1
- ChecksumEB6A862C0BF1B83E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001173 EMBL· GenBank· DDBJ | ACI27097.1 EMBL· GenBank· DDBJ | Genomic DNA |