AC   MF_02086;
DC   Protein; auto
TR   HAMAP; MF_02086; -; 1; level=0
XX
Names: PdxA_Epsilonprot
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;
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   -!- 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   Cobalt
KW   Cytoplasm
KW   Magnesium
KW   Metal-binding
KW   NAD
KW   NADP
KW   Oxidoreductase
KW   Pyridoxine biosynthesis
KW   Zinc
XX
GO   GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity
GO   GO:0046872; F:metal ion binding
GO   GO:0050897; F:cobalt ion binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0000287; F:magnesium ion binding
GO   GO:0042823; P:pyridoxal phosphate biosynthetic process
GO   GO:0008615; P:pyridoxine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PDXA_CAMJE (Q9PN58)
FT   BINDING         177
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         216
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         301
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         148
FT                   /ligand="substrate"
FT   Optional; Condition: H
FT   BINDING         149
FT                   /ligand="substrate"
FT   Optional; Condition: T
FT   BINDING         309
FT                   /ligand="substrate"
FT   Optional; Condition: K
FT   BINDING         318
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         327
FT                   /ligand="substrate"
FT   Optional; Condition: R
XX
Size: 296-375;
Related: None;
Template: Q9PN58; P19624;
Scope:
 Bacteria; Epsilonproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.7 2023/06/01
//