AC MF_01639; DC Protein; auto TR HAMAP; MF_01639; -; 1; level=0 XX Names: PdxY XX ID PDXY DE RecName: Full=Pyridoxal kinase PdxY; DE Short=PL kinase; DE EC=2.7.1.35; GN Name=pdxY; XX CC -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal CC 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; CC Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; CC EC=2.7.1.35; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxal: step 1/1. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily. XX DR Pfam; PF08543; Phos_pyr_kin; 1; trigger=no DR NCBIfam; TIGR00687; pyridox_kin; 1; trigger=no XX KW ATP-binding KW Kinase KW Magnesium KW Nucleotide-binding KW Transferase XX GO GO:0000287; F:magnesium ion binding GO GO:0005524; F:ATP binding GO GO:0008478; F:pyridoxal kinase activity GO GO:0009443; P:pyridoxal 5'-phosphate salvage XX FT From: PDXY_ECOLI (P77150) FT BINDING 209..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R-x-x-[VLI] FT BINDING 45..46 FT /ligand="substrate" FT Optional; Condition: [TM]-Q FT BINDING 10 FT /ligand="substrate" FT Condition: S FT BINDING 112 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: D FT BINDING 144 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [AV] FT BINDING 149 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: E FT BINDING 182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: K FT BINDING 224 FT /ligand="substrate" FT Condition: D XX Size: 283-299; Related: None; Template: P77150; Scope: Bacteria; Actinomycetota Bacteria; Deinococci Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: SALTI contains a C-terminal deletion removing the last 68 aa, and may therefore be non-functional. This sequence is not shown in alignment and was not taken into account for the size range field. XX # Revision 1.24 2023/06/01 //