A0A8C2NLP0 · A0A8C2NLP0_CAPHI
- ProteinPyridoxal kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively. PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions.
Catalytic activity
- pyridoxal + ATP = pyridoxal 5'-phosphate + ADP + H+This reaction proceeds in the forward direction.
Pathway
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1.
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | pyridoxal kinase activity | |
Biological Process | pyridoxal 5'-phosphate salvage |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxal kinase
- EC number
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Capra
Accessions
- Primary accessionA0A8C2NLP0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)42,429
- Last updated2022-01-19 v1
- MD5 Checksum6034C265976AA42DD685A8D67CF64C5C