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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
Scope(s) Bacteria
Template(s) P19624 (PDXA_ECOLI); P58717 (PDXA_SALTY); Q9I5U4 (PDXA_PSEAE); [ Recover all ]
Triggered by HAMAP; MF_00536 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PDXA
Protein name RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
                 EC=1.1.1.262;
AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase;
Gene name Name=pdxA;

Comments [?]

FUNCTIONCatalyzes 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 Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526, ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58452; EC=1.1.1.262;
case <OC:Pseudomonadota>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Note=Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).;
else
COFACTOR Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Note=Binds 1 divalent metal cation per subunit.;
end case
PATHWAYCofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
MISCELLANEOUSThe active site is located at the dimer interface.
SIMILARITYBelongs to the PdxA family.

Keywords [?]


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 <OCellular component: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 136 136 /ligand="substrate" H
BINDING 137 137 /ligand="substrate" [TS]
BINDING 274 274 /ligand="substrate" K
BINDING 283 283 /ligand="substrate" N
BINDING 292 292 /ligand="substrate" R

Additional information [?]

Size range 307-364 amino acids
Related rules None
Fusion Nter: None Cter: 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.



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