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Annotation rule MF_02086
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General rule information [?]

Accession MF_02086
Dates 14-MAR-2017 (Created)
20-NOV-2019 (Last updated, Version 4)
Name PdxA_Epsilonprot
Scope
Bacteria; Epsilonproteobacteria
Templates Q9PN58 (PDXA_CAMJE); P19624 (PDXA_ECOLI): [Recover all]

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
pdxA

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
EC 1.1.1.262
Cofactor Zn(2+)
Mg(2+)
Co(2+)
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 [?]


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;
TIGRFAMs TIGR00557; pdxA; 1;

Features [?]

From: PDXA_CAMJE (Q9PN58)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     177     177       Divalent metal cation; shared with dimeric partner     H  
METAL     216     216       Divalent metal cation; shared with dimeric partner     H  
METAL     301     301       Divalent metal cation; shared with dimeric partner     H  
BINDING (Optional)     148     148       Substrate     H  
BINDING (Optional)     149     149       Substrate     T  
BINDING (Optional)     309     309       Substrate     K  
BINDING (Optional)     318     318       Substrate     N  
BINDING (Optional)     327     327       Substrate     R  

Additional information [?]

Size range 296-375 amino acids
Related rules None
Fusion None