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IPR004625 is a Pyridoxine kinase.
<p>Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [[cite:PUB00035505], [cite:PUB00006322], [cite:PUB00035506]]. PLP-dependent enzymes are primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but they are also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters; pyridoxal phosphate can also inhibit DNA polymerases and several steroid receptors [[cite:PUB00035507]]. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [[cite:PUB00035508]].</p> <p>PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the ε-amino group of an active site lysine residue on the enzyme. The α-amino group of the substrate displaces the lysine ε-amino group, in the process forming a new aldimine with the substrate. This aldimine is the common central intermediate for all PLP-catalysed reactions, enzymatic and non-enzymatic [[cite:PUB00035504]].</p> <p>This entry represents pyridoxal kinase ([ec:2.7.1.35]), which is required for the synthesis of pyridoxal-5-phosphate from vitamin B6, and catalyses the conversion of pyridoxal to pyridoxal 5'-phosphate in the presence of ATP. Escherichia coli has an enzyme PdxK that acts<i>in vitro</i>as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxamine kinase, PdxY [[cite:PUB00017544]]. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Pyridoxal kinase activity | Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate. | ||
| Biological process | Pyridoxal 5'-phosphate salvage | Any process that generates pyridoxal 5'-phosphate, the active form of vitamin B6, from derivatives of it without de novo synthesis. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: pyridoxal kinase-like isoform X2 [Cicer arietinum] gi|502096904|ref|XP_004490860.1| | 10 | ||
| – | Pyridoxal kinase; TAIR: AT5G37850.2 pfkB-like carbohydrate kinase family protein; Swiss-Prot: sp|Q8W1X2|PDXK_ARATH Pyridoxal kinase; TrEMBL-Plants: tr|I3SC66|I3SC66_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0091400 | 9 | ||
| – | Pyridoxal kinase; TAIR: AT5G37850.2 pfkB-like carbohydrate kinase family protein; Swiss-Prot: sp|Q8W1X2|PDXK_ARATH Pyridoxal kinase; TrEMBL-Plants: tr|I3SC66|I3SC66_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0091400 | 9 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01173 | CDD | 1 | 33.33 |