A0A2N3B5T4 · A0A2N3B5T4_9PROT
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids285 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
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
- thiamine phosphate + ATP = thiamine diphosphate + ADP
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 25 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 48 | substrate | ||||
Sequence: H | ||||||
Binding site | 69 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 111-112 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 112 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 138 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 192 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 194 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 195 | Mg2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 235 | substrate | ||||
Sequence: D | ||||||
Binding site | 282 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
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 nameThiamine-monophosphate kinase
- EC number
- Short namesTMP kinase ; Thiamine-phosphate kinase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria
Accessions
- Primary accessionA0A2N3B5T4
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-129 | PurM-like N-terminal | ||||
Sequence: DDCALITIGNETLVINHEMMAEGTHFRPDADMADVAWKLVASNISDLAAKGAEPVGVLLGHSLGRDDARFLQGLKEALLAFNVPLLGGDTVTATGASTFAMTAIGR | ||||||
Domain | 144-249 | PurM-like C-terminal | ||||
Sequence: GDAVYVTGTIGRAMLGFEGAAHHRAAFDRPEPRLAEGLALAPLVSAIMDVSDGLLLDCWRMAKLNNQTFAIDPDAVPVADNARRDECMRWGDDYELLFTAAPGAAI |
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)30,022
- Last updated2018-04-25 v1
- ChecksumDD96BF7B2C34D5D2