A0A1W2FXB7 · A0A1W2FXB7_KIBAR
- ProteinMultifunctional fusion protein
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids906 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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).
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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 [4Fe-4S] cluster per subunit.
Note: Binds 1 thiamine pyrophosphate per subunit.
Pathway
Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6.
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, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 45 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 45 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 45 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 100 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 128 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 130 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 168 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 198 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 226 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 226 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 226 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 227 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 227 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 227 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 228 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 228 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 228 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 270 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 270 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 270 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 383 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 424-426 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: SHA | ||||||
Binding site | 456 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 457-458 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 485 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 485 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 554 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 635 | 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 | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | 1-deoxy-D-xylulose 5-phosphate biosynthetic process | |
Biological Process | dimethylallyl diphosphate 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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended name1-deoxy-D-xylulose-5-phosphate synthase
- EC number
- Alternative names
- Recommended name4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- EC number
- Short namesHMBPP reductase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Kibdelosporangium
Accessions
- Primary accessionA0A1W2FXB7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 584-748 | Transketolase-like pyrimidine-binding | ||||
Sequence: RSWTSVFADELVRLGGLREDVVAITAAMQDPTGLSRFAERYPARVVDVGIAEQHAVTAAAGMAMAGMRPVVAIYSTFLNRAIDQVLLDVALHSCPVIFVLDRAGVTGDDGPSHNGMWDMSLLNVVPKMRIAAPRDAATLRSALRGALDTVDGPSTIRFPKGEVGD |
Sequence similarities
Belongs to the IspH family.
Belongs to the transketolase family. DXPS subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length906
- Mass (Da)97,529
- Last updated2017-06-07 v1
- ChecksumFC74DC973B6051B6
Keywords
- Technical term