HAMAP rule MF_00536
General rule information
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Accession | MF_00536 |
Dates | 30-JAN-2002 (Created) 1-JUN-2023 (Last updated, Version 36) |
Name | PdxA |
Scope | Bacteria |
Templates | P19624 (PDXA_ECOLI); P58717 (PDXA_SALTY); Q9I5U4 (PDXA_PSEAE): [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 NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). |
Catalytic activity | RHEA:32275: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
EC 1.1.1.262 |
case <OC:Pseudomonadota>
Cofactor | Zn(2+) Mg(2+) Co(2+) Note: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+). |
else
Cofactor | a divalent metal cation Note: Binds 1 divalent metal cation per subunit. |
end case
Pathway | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. |
Subunit | Homodimer. |
Subcellular location | Cytoplasm. |
Miscellaneous | The active site is located at the dimer interface. |
Similarity | Belongs to the PdxA family. |
Keywords
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case <OC:Pseudomonadota>
end case
Gene Ontology
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GO:0050570; Molecular function: 4-hydroxythreonine-4-phosphate dehydrogenase activity.
GO:0046872; Molecular function: metal ion binding.
GO:0042823; Biological process: pyridoxal phosphate biosynthetic process.
GO:0008615; Biological process: pyridoxine biosynthetic process.
GO:0046872; Molecular function: metal ion binding.
GO:0042823; Biological process: pyridoxal phosphate biosynthetic process.
GO:0008615; Biological process: pyridoxine biosynthetic process.
case <OC:Pseudomonadota>
GO:0050897; Molecular function: cobalt ion binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0005737; Cellular component: cytoplasm.
Cross-references
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Features
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From: PDXA_ECOLI (P19624) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 166 | 166 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners | H | ||||||||
BINDING | 211 | 211 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners | H | ||||||||
BINDING | 266 | 266 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="ligand shared between dimeric partners | H | ||||||||
BINDING (Optional) | 136 | 136 | /ligand="substrate | H | ||||||||
BINDING (Optional) | 137 | 137 | /ligand="substrate | [TS] | ||||||||
BINDING | 274 | 274 | /ligand="substrate | K | ||||||||
BINDING (Optional) | 283 | 283 | /ligand="substrate | N | ||||||||
BINDING (Optional) | 292 | 292 | /ligand="substrate | R |
Additional information
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Size range | 307-364 amino acids |
Related rules | None |
Fusion | None |
Comments | MF_00536 signature has been revised (March 2017) to avoid wrong annotation of DUF1537-linked PdxA2, which are paralogs of PdxA and are involved in carbon source metabolism rather than PLP biosynthesis. |