AC   MF_01638;
DC   Protein; auto
TR   HAMAP; MF_01638; -; 1; level=0
XX
Names: PdxK
XX
ID   PDXK
DE   RecName: Full=Pyridoxine/pyridoxal/pyridoxamine kinase;
DE            Short=PN/PL/PM kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=B6-vitamer kinase;
GN   Name=pdxK;
XX
CC   -!- FUNCTION: B6-vitamer kinase involved in the salvage pathway of
CC       pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of
CC       pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their
CC       respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate;
CC         Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate;
CC         Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216;
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   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxine 5'-phosphate from pyridoxine: step 1/1.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxK 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   Metal-binding
KW   Nucleotide-binding
KW   Transferase
KW   Zinc
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0008270; F:zinc 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: PDXK_ECOLI (P40191)
FT   BINDING         221..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: H-x-x-[VI]
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: Y
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: E
FT   BINDING         23
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         59
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         233
FT                   /ligand="substrate"
FT   Condition: D
XX
Size: 283-296;
Related: None;
Template: P40191;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in CUPMC
Comments: None
XX
# Revision 1.20 2023/06/01
//