A0A4R2S0J6 · A0A4R2S0J6_9FIRM
- ProteinMultifunctional fusion protein
- GenethiE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Miscellaneous
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Catalytic activity
- 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H+ = thiamine phosphate + CO2 + diphosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 44-48 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 76 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 77 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 96 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 115 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 141-143 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 144 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | |||
Binding site | 171 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 191-192 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 300 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 300 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 315 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 316 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 317 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 317 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 324 | substrate | |||
Binding site | 346 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 346 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 346 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 376 | ATP (UniProtKB | ChEBI) | |||
Binding site | 393-394 | ATP (UniProtKB | ChEBI) | |||
Binding site | 394 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 418 | ATP (UniProtKB | ChEBI) | |||
Binding site | 496 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 498 | ATP (UniProtKB | ChEBI) | |||
Binding site | 499 | Mg2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 549 | substrate | |||
Binding site | 610 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine-phosphate diphosphorylase activity | |
Molecular Function | thiamine-phosphate kinase activity | |
Biological Process | phosphorylation | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameThiamine-phosphate synthase
- EC number
- Short namesTP synthase ; TPS
- Alternative names
- Recommended nameThiamine-monophosphate kinase
- EC number
- Short namesTMP kinase ; Thiamine-phosphate kinase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Heliobacteriaceae > Heliophilum
Accessions
- Primary accessionA0A4R2S0J6
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 15-194 | Thiamine phosphate synthase/TenI | |||
Domain | 298-411 | PurM-like N-terminal | |||
Domain | 422-587 | PurM-like C-terminal | |||
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Belongs to the thiamine-phosphate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length615
- Mass (Da)65,052
- Last updated2019-07-31 v1
- ChecksumB01912F8636511A6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SLXT01000001 EMBL· GenBank· DDBJ | TCP68939.1 EMBL· GenBank· DDBJ | Genomic DNA |