A0A2L0UBC3 · A0A2L0UBC3_9MICC
- ProteinPN/PL/PM kinase
- GenethiD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids275 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic activity
- 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | hydroxymethylpyrimidine kinase activity | |
Molecular Function | phosphomethylpyrimidine kinase activity | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePN/PL/PM kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Arthrobacter
Accessions
- Primary accessionA0A2L0UBC3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-257 | Pyridoxamine kinase/Phosphomethylpyrimidine kinase | ||||
Sequence: TGGAGAQADLKTFQELGVYGVVALTCIVSFDPKQEWQHRFVPVDQQVIADQLEAIQSCYPLTTVKLGMLGTPATIDTVAAALRSQAWDNVVLDPVLICKGQEPGAALDTDQALKANILPLATFVTPNHFEAESLSGITIENLADLEEAARIIHAQSGAVVLAKGGVRIEGPDAVDVYFDGETLEVLSAPKVGEVAVSGAGCTLAAAIAAELAKGAAPLEAARTAKEFVTEGIRNRV |
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)28,536
- Last updated2018-04-25 v1
- Checksum0B86F6F66D7E1C46