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HAMAP rule MF_00536

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General rule information [?]

Accession MF_00536
Dates 30-JAN-2002 (Created)
1-JUN-2023 (Last updated, Version 36)
Name PdxA
Templates P19624 (PDXA_ECOLI); P58717 (PDXA_SALTY); Q9I5U4 (PDXA_PSEAE): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase;
Gene name

Comments [?]

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
case <OC:Pseudomonadota>
Cofactor Zn(2+)
Note: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
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 [?]

case <OC:Pseudomonadota>
end case

Gene Ontology [?]

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.
case <OC:Pseudomonadota>
GO:0050897; Molecular function: cobalt 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 [?]

Pfam PF04166; PdxA; 1;
NCBIfam TIGR00557; PdxA; 1;

Features [?]

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 [?]

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.