Information on EC 1.1.1.262 - 4-hydroxythreonine-4-phosphate dehydrogenase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY
1.1.1.262
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxythreonine-4-phosphate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-phosphonooxy-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+
show the reaction diagram
-
-
-
-
4-phosphonooxy-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+
show the reaction diagram
3-amino-1-hydroxyacetone 1-phosphate,i.e. AHAB, is the primary product of the reaction, no formation of 2-amino-3-oxo-4-phosphonooxybutyrate as intermediate is detected, identification by electrospray ionization mass spectrometry
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4-phosphonooxy-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+
show the reaction diagram
Asp247 and Asp267 are involved in formation and maintaining of the integrity of the active site
-, P19624
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
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Vitamin B6 metabolism
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SYSTEMATIC NAME
IUBMB Comments
4-phosphonooxy-L-threonine:NAD+ oxidoreductase
The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-(phosphohydroxy)-L-threonine dehydrogenase
-
-
-
-
L-threonine 4-phosphate dehydrogenase
-
-
-
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NAD-dependent threonine 4-phosphate dehydrogenase
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-
-
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PdxA
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
230310-36-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-3-oxo-4-phosphonooxybutyrate + H2O
3-amino-1-hydroxyacetone 1-phosphate + CO2
show the reaction diagram
-, P19624
step 2 of the overall reaction
i.e. AHAP
-
?
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
undergoes decarboxylation either catalysed by the enzyme or after release, further formation of pyridoxal 5'-phosphate catalysed by PdxJ protein
r
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
show the reaction diagram
-, P19624
fourth step of the pyridoxal 5'-phosphate biosynthesis
-
-
?
4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
show the reaction diagram
-, P19624
i.e. 4-hydroxy-L-threonine phosphate or HTP, enzyme strictly requires the phosphate ester form of the substrate, interaction between enzyme and substrate via phosphate group, step 1 of the overall reaction
reaction intermediate
-
?
4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
show the reaction diagram
-
involved in the biosynthesis of vitamin B6
-
-
?
4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
show the reaction diagram
-
i.e. 4-hydroxy-L-threonine-4-phosphate, HTP
i.e. AHAB, primary product of the reaction, no formation of 2-amino-3-oxo-4-phosphonooxybutyrate as intermediate is detected, identification by electrospray ionization mass spectrometry
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
undergoes decarboxylation either catalysed by the enzyme or after release, further formation of pyridoxal 5'-phosphate catalysed by PdxJ protein
r
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
show the reaction diagram
-
involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
show the reaction diagram
-, P19624
fourth step of the pyridoxal 5'-phosphate biosynthesis
-
-
?
4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
show the reaction diagram
-
involved in the biosynthesis of vitamin B6
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD(P)+
-
dependent on
NAD(P)+
-, P19624
putative binding site structure
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zn2+
-
tightly bound, divalent metal ion-dependent enzyme, Zn2+ can be replaced by e.g. Mg2+
Zn2+
-, P19624
divalent metal ion-dependent enzyme, Zn2+ is bound to the active site of each monomer coordinated by 3 histidine residues from both monomer
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
inhibition at 1 mM, fully restored by addition of 1 mM Mn2+, Co2+, Mg2+ or Ca2+, partially restored by 1 mM Ni2+ or Zn2+
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.4
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4-(phosphohydroxy)-L-threonine
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-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
pdxA gene product
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia phymatum (strain DSM 17167 / STM815)
Burkholderia xenovorans (strain LB400)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-, P19624
tightly bound, monomer fold is alpha/beta/alpha divided into 2 subdomains, the active site is located at the dimer interface
monomer
-
gel filtration, native PAGE, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
8.1 mg/ml purified recombinant enzyme in complex with substrate 4-(phosphonooxy)threonine and Zn2+ in 20 mM Tris-HCl, pH 8.0, 0.2 M NaCl, 10 mM DTT, 5% w/v glycerol, hanging drop vapour diffusion method, 0.002 ml protein solution with 0.004 ml reservoir solution, usage of 2 reservoir solution variants resulting in 2 differen crystal forms, solution 1 contains 7.5% w/v PEG 8000, 0.1 M NaOAc, pH 5.5, 10 mM MgCl2, 10 mM NaKHPO4, pH 5.9, solution 2 contains 20% w/v PEG 8000, 100 mM HEPES, pH 7.5, 75 mM citrate, and 100 mM MgCl2, suspension over reservoir solution, X-ray diffraction structure determination and analysis at 2,0 and 2.45 A resolution, respectively
-, P19624
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, cleavage by thrombin
-, P19624
to homogeneity, recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene pdxA, expression of the His-tagged enzyme with a thrombin cleavage site in Escherichia coli
-, P19624
overexpression in Escherichia coli
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