HAMAP rule MF_01629

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]

Triggered by

HAMAP; MF_01629 (Get profile general information and statistics)

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 [?]

Flavoprotein
FMN
Oxidoreductase
Pyridoxine biosynthesis

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).

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