AC   MF_00536;
DC   Protein; auto
TR   HAMAP; MF_00536; -; 1; level=0
XX
Names: PdxA
XX
ID   PDXA
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
DE            EC=1.1.1.262;
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase;
GN   Name=pdxA;
XX
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC       threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC       spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC       (AHAP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC         phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58452; EC=1.1.1.262;
case <OC:Pseudomonadota>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+).;
else
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 1 divalent metal cation per subunit.;
end case
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC   -!- SIMILARITY: Belongs to the PdxA family.
XX
DR   Pfam; PF04166; PdxA; 1; trigger=no
DR   NCBIfam; TIGR00557; PdxA; 1; trigger=no
XX
KW   Cytoplasm
KW   Pyridoxine biosynthesis
KW   Oxidoreductase
KW   NAD
KW   NADP
KW   Metal-binding
case <OC:Pseudomonadota>
KW   Cobalt
KW   Magnesium
KW   Zinc
end case
XX
GO   GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0042823; P:pyridoxal phosphate biosynthetic process
GO   GO:0008615; P:pyridoxine biosynthetic process
case <OC:Pseudomonadota>
GO   GO:0050897; F:cobalt ion binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: PDXA_ECOLI (P19624)
FT   BINDING         166
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: H
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: H
FT   BINDING         266
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: H
FT   BINDING         136
FT                   /ligand="substrate"
FT   Optional; Condition: H
FT   BINDING         137
FT                   /ligand="substrate"
FT   Optional; Condition: [TS]
FT   BINDING         274
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         283
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         292
FT                   /ligand="substrate"
FT   Optional; Condition: R
XX
Size: 307-364;
Related: None;
Template: P19624; P58717; Q9I5U4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in RHIME, SPHAR
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.
XX
# Revision 1.36 2023/06/01
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