Q1QUD0 · Q1QUD0_CHRSD
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids319 (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 | 31 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 31 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 46 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 48 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 48 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 55 | substrate | ||||
Sequence: H | ||||||
Binding site | 76 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 76 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 76 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122-123 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 123 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 147 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 209 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 212 | Mg2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260 | substrate | ||||
Sequence: D | ||||||
Binding site | 311 | substrate | ||||
Sequence: W |
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 > Oceanospirillales > Halomonadaceae > Chromohalobacter
Accessions
- Primary accessionQ1QUD0
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-139 | PurM-like N-terminal | ||||
Sequence: GDDCALLSPEAGHELALSVDTSVVDVHFPGDAPPEAIGHRALAVALSDLAAMGARPRGCLMALTLSHAEPDWLERFAHGFRELGRRTATPLIGGDVTRGSLSIGVTVIGDV | ||||||
Domain | 152-300 | PurM-like C-terminal | ||||
Sequence: PGERLAVTGSLGGGHAGLRMWQAGGHDLADPLLAAYLTPTPQLAAGQALRDLASAGLDISDGLLADLGHLCRASGVGAVLSPDDLPLAPSLDMTLGREAALHAALNGGDDYQLLVSVPDAAWADAQQRCAACDVALTEIGRVTAEPGIR |
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length319
- Mass (Da)32,609
- Last updated2006-05-16 v1
- Checksum6A2FDB0887FF2FAB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000285 EMBL· GenBank· DDBJ | ABE59928.1 EMBL· GenBank· DDBJ | Genomic DNA |