G2GWD2 · G2GWD2_9ENTR
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids337 (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 | 30 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 30 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 45 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 46 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 47 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 47 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 54 | substrate | |||
Binding site | 75 | Mg2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 75 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 75 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 121-122 | ATP (UniProtKB | ChEBI) | |||
Binding site | 122 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 146 | ATP (UniProtKB | ChEBI) | |||
Binding site | 212 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 214 | ATP (UniProtKB | ChEBI) | |||
Binding site | 215 | Mg2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 263 | substrate | |||
Binding site | 324 | substrate | |||
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 > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > aphid secondary symbionts > Candidatus Regiella
Accessions
- Primary accessionG2GWD2
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 28-136 | PurM-like N-terminal | |||
Domain | 152-301 | PurM-like C-terminal | |||
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length337
- Mass (Da)37,143
- Last updated2011-11-16 v1
- ChecksumBDC6C902D2A1FE08
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGCA01000017 EMBL· GenBank· DDBJ | EGY29943.1 EMBL· GenBank· DDBJ | Genomic DNA |