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HAMAP rule MF_01629

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General rule information [?]

Accession MF_01629
Dates 14-DEC-2005 (Created)
1-JUN-2023 (Last updated, Version 34)
Name PdxH
Scope
Bacteria; Actinomycetota
Bacteria; Bacteroidota
Bacteria; Cyanobacteriota
Bacteria; Deinococcota
Bacteria; Planctomycetota
Bacteria; Pseudomonadota
Bacteria; Spirochaetota
Templates P0AFI7 (PDXH_ECOLI); P9WIJ1 (PDXH_MYCTU): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PDXH
Protein name
RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase;
EC 1.4.3.5;
AltName: Full=PNP/PMP oxidase;
Short=PNPOx;
AltName: Full=Pyridoxal 5'-phosphate synthase;
Gene name
pdxH

Comments [?]

Function Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic activity RHEA:15817: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
EC 1.4.3.5
RHEA:15149: O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate
EC 1.4.3.5
Cofactor FMN
Note: Binds 1 FMN per subunit.
Pathway Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit Homodimer.
Similarity Belongs to the pyridoxamine 5'-phosphate oxidase family.

Keywords [?]


Gene Ontology [?]

GO:0004733; Molecular function: pyridoxamine-phosphate oxidase activity.
GO:0010181; Molecular function: FMN binding.
GO:0042816; Biological process: vitamin B6 metabolic process.

Cross-references [?]

PROSITE PS01064; PYRIDOX_OXIDASE; 1;
Pfam PF01243; Pyridox_oxidase; 1;
NCBIfam TIGR00558; PdxH; 1;

Features [?]

From: PDXH_ECOLI (P0AFI7)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     67     72       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     R-x-x-L-x-[KR]  
BINDING     82     83       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [YF]-[TS]  
BINDING     146     147       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     Q-S  
BINDING (Optional)     14     17       /ligand="substrate     R-x-x-Y  
BINDING     197     199       /ligand="substrate     R-x-[HN]  
BINDING     72     72       /ligand="substrate     [KR]  
BINDING     88     88       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [RK]  
BINDING     89     89       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     K  
BINDING     111     111       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     Q  
BINDING     129     129       /ligand="substrate     Y  
BINDING     133     133       /ligand="substrate     R  
BINDING (Optional)     137     137       /ligand="substrate     S  
BINDING     191     191       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     W  
BINDING     201     201       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     R  

Additional information [?]

Size range 192-267 amino acids
Related rules None
Fusion None
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).