A0A514LLX9 · A0A514LLX9_9BACI
- ProteinThiamine-monophosphate kinase
- GenethiL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids327 (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 | 27 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 27 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 44 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 44 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 51 | 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 | 103 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 120-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 121 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 147 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 216 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 218 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 219 | Mg2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 267 | substrate | ||||
Sequence: E | ||||||
Binding site | 324 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Salicibibacter
Accessions
- Primary accessionA0A514LLX9
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-139 | PurM-like N-terminal | ||||
Sequence: GDDAAVTSSHAHKDVISCVDTICEGIHFKRSTLHLSDIGYKALAVNLSDIAAMGGTPRYYLVSLAMSPEWKQEEILEIYRGMNDLAERYGVLLIGGDTVSAQHDLMISVTVLGEI | ||||||
Domain | 151-308 | PurM-like C-terminal | ||||
Sequence: REGDVVFASGTLGDSRGGLDLLLSGGLTAPRTEQEHALVGVHQRPEPQLTLGQLLKESGCRIALNDISDGLSSESWELAEASRVCICLEEEKIPVSENATKLFGNETAYEYALTGGEDFQLVGTVAKSDWPAIASAAKEKGIRLSAIGSVTQEGAPQV |
Sequence similarities
Belongs to the thiamine-monophosphate kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)35,339
- Last updated2019-10-16 v1
- ChecksumDE2F65C2E5FC28AE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP035485 EMBL· GenBank· DDBJ | QDI92535.1 EMBL· GenBank· DDBJ | Genomic DNA |