AC   MF_01629;
DC   Protein; auto
TR   HAMAP; MF_01629; -; 1; level=0
XX
Names: PdxH
XX
ID   PDXH
DE   RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase;
DE            EC=1.4.3.5;
DE   AltName: Full=PNP/PMP oxidase;
DE            Short=PNPOx;
DE   AltName: Full=Pyridoxal 5'-phosphate synthase;
GN   Name=pdxH;
XX
CC   -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC       (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC       (PLP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC         pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
XX
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1; trigger=no
DR   Pfam; PF01243; Pyridox_oxidase; 1; trigger=no
DR   NCBIfam; TIGR00558; PdxH; 1; trigger=no
XX
KW   Flavoprotein
KW   FMN
KW   Oxidoreductase
KW   Pyridoxine biosynthesis
XX
GO   GO:0004733; F:pyridoxamine phosphate oxidase activity
GO   GO:0010181; F:FMN binding
GO   GO:0042816; P:vitamin B6 metabolic process
XX
FT   From: PDXH_ECOLI (P0AFI7)
FT   BINDING         67..72
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: R-x-x-L-x-[KR]
FT   BINDING         82..83
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [YF]-[TS]
FT   BINDING         146..147
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: Q-S
FT   BINDING         14..17
FT                   /ligand="substrate"
FT   Optional; Condition: R-x-x-Y
FT   BINDING         197..199
FT                   /ligand="substrate"
FT   Condition: R-x-[HN]
FT   BINDING         72
FT                   /ligand="substrate"
FT   Condition: [KR]
FT   BINDING         88
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [RK]
FT   BINDING         89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: K
FT   BINDING         111
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: Q
FT   BINDING         129
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         133
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         137
FT                   /ligand="substrate"
FT   Optional; Condition: S
FT   BINDING         191
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: W
FT   BINDING         201
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: R
XX
Size: 192-267;
Related: None;
Template: P0AFI7; P9WIJ1;
Scope:
 Bacteria; Actinomycetota
 Bacteria; Bacteroidota
 Bacteria; Cyanobacteriota
 Bacteria; Deinococcota
 Bacteria; Planctomycetota
 Bacteria; Pseudomonadota
 Bacteria; Spirochaetota
Fusion:
 Nter: None
 Cter: None
Duplicate: in RALN1, HYDCU
Plasmid: in RALN1
Comments: In M.tuberculosis, the enzyme catalyzes only the oxidation of pyridoxine 5'-phosphate (PNP),
 it does not recognize pyridoxamine 5'-phosphate (PMP) as a substrate (PubMed:22110704).
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# Revision 1.36 2023/11/28
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