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HAMAP rule MF_01629

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General rule information [?]

Accession MF_01629
Dates 14-DEC-2005 (Created)
28-JUL-2023 (Last updated, Version 35)
Name PdxH
Scope(s) Bacteria
Actinomycetota
Bacteroidota
Cyanobacteriota
Deinococcota
Planctomycetota
Pseudomonadota
Spirochaetota
Template(s) 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 Name=pdxH;

Comments [?]

FUNCTIONCatalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
CATALYTIC ACTIVITY Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CATALYTIC ACTIVITY Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
COFACTOR Name=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 1 FMN per subunit.;
PATHWAYCofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
PATHWAYCofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
SUBUNITHomodimer.
SIMILARITYBelongs 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 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 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 Nter: None Cter: 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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