Information on EC 5.1.3.22 - L-ribulose-5-phosphate 3-epimerase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
5.1.3.22
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RECOMMENDED NAME
GeneOntology No.
L-ribulose-5-phosphate 3-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-ribulose 5-phosphate = L-xylulose 5-phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
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L-ascorbate degradation I (bacterial, anaerobic)
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L-ascorbate degradation II (bacterial, aerobic)
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L-lyxose degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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degradation of pentoses
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SYSTEMATIC NAME
IUBMB Comments
L-ribulose-5-phosphate 3-epimerase
Along with EC 4.1.1.85, 3-dehydro-L-gulonate-6-phosphate decarboxylase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-19-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-ribulose 5-phosphate
L-xylulose 5-phosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-ribulose 5-phosphate
L-xylulose 5-phosphate
show the reaction diagram
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along with EC 4.1.1.83, 3-dehydro-L-gulonate-6-phosphate decarboxylase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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the enzyme binds Zn2+, which is coordinated by Glu155, Asp185, His211, and Glu25, crystallization data
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein has a triosephosphate isomerase barrel fold and forms dimers. The active site is located at the C-terminal ends of the parallel beta-strands. The enzyme binds Zn2+, which is coordinated by Glu155, Asp185, His211, and Glu251. A phosphate-binding site is formed by residues from the beta1/alpha1 loop and alpha3'-helix in the N-terminal region
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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Show AA Sequence (782 entries)
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