A0A3A9LK82 · A0A3A9LK82_MORCA
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids325 (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 | 28 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 28 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 45 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 45 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 52 | substrate | ||||
Sequence: H | ||||||
Binding site | 73 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 73 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 73 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 122 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 147 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 219 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 221 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 222 | Mg2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 269 | substrate | ||||
Sequence: D | ||||||
Binding site | 322 | 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 > Moraxellales > Moraxellaceae > Moraxella
Accessions
- Primary accessionA0A3A9LK82
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-139 | PurM-like N-terminal | ||||
Sequence: GDDCAISNIPPNSQLVSCVDTLVAGRHFVHETSPHAIAYKSVAVNLSDLASMGAMPYAILVGLSLPKSMANDDFCQAFAEGLAAACTPFGVELIGGDTTSSPILTISVTALGFV |
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length325
- Mass (Da)34,391
- Last updated2018-12-05 v1
- Checksum1E185741DEF75592