HAMAP rule MF_01629
General rule information
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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 |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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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 |
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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
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Gene Ontology
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GO:0004733; Molecular function: pyridoxamine-phosphate oxidase activity.
GO:0010181; Molecular function: FMN binding.
GO:0042816; Biological process: vitamin B6 metabolic process.
GO:0010181; Molecular function: FMN binding.
GO:0042816; Biological process: vitamin B6 metabolic process.
Cross-references
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Features
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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
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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). |