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HAMAP rule MF_02086

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General rule information [?]

Accession MF_02086
Dates 14-MAR-2017 (Created)
1-JUN-2023 (Last updated, Version 7)
Name PdxA_Epsilonprot
Scope(s) Bacteria
Template(s) Q9PN58 (PDXA_CAMJE); P19624 (PDXA_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_02086 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PDXA
Protein name RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
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=;
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Co(2+); Xref=ChEBI:CHEBI:48828;
PATHWAYCofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
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:0050897; Molecular function:cobalt ion binding
GO:0008270; Molecular function:zinc ion binding
GO:0000287; Molecular function:magnesium ion binding
GO:0042823; Biological process:pyridoxal phosphate biosynthetic process
GO:0008615; Biological process:pyridoxine biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

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

Features [?]

Key From To Description Tag Condition FTGroup
BINDING 177 177 /ligand="a divalent metal cation"
/ligand_note="ligand shared between dimeric partners"
BINDING 216 216 /ligand="a divalent metal cation"
/ligand_note="ligand shared between dimeric partners"
BINDING 301 301 /ligand="a divalent metal cation"
/ligand_note="ligand shared between dimeric partners"
BINDING 148 148 /ligand="substrate" H
BINDING 149 149 /ligand="substrate" T
BINDING 309 309 /ligand="substrate" K
BINDING 318 318 /ligand="substrate" N
BINDING 327 327 /ligand="substrate" R

Additional information [?]

Size range 296-375 amino acids
Related rules None
Fusion Nter: None Cter: None

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