A0A2I0PLG9 · A0A2I0PLG9_9EURY
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids347 (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
- ATP + thiamine phosphate = ADP + thiamine diphosphate
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 | 45 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 45 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 59 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 60 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 61 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 61 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 68 | substrate | ||||
Sequence: H | ||||||
Binding site | 89 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 89 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 89 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 136-137 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 137 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 237 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 239 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 240 | Mg2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | substrate | ||||
Sequence: E | ||||||
Binding site | 342 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine-phosphate kinase activity | |
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 lineageArchaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales
Accessions
- Primary accessionA0A2I0PLG9
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-154 | PurM-like N-terminal | ||||
Sequence: GDDAALTDIGSGYLVSTSDMLLQETHFPPQMNHRQMGWKIVTVNVSDLAAMGAYPRGILISMGLPRDMTMEQFNELVEGILDACTYYETPLIGGDTNESPQIVLNGTALGEV | ||||||
Domain | 166-329 | PurM-like C-terminal | ||||
Sequence: QKGNLIVVTGSLGLAAAGFEILLADDNDSLQKIESLKGEFVKKAVKHALDPRAKIKEGIIAAESKLVTSCTDITDGLTSELYDMLKAENNIGIRIYEHKIPSHPLVEEVSKITGKNLHQMTLYYGEDFELLLTVKKEEIDVLKKLMDVYVVGEVTDSAYVEIVD |
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length347
- Mass (Da)38,372
- Last updated2018-02-28 v1
- Checksum01CB71634D1F70E7