Information on EC 2.6.1.104 - 3-dehydro-glucose-6-phosphate-glutamate transaminase

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The expected taxonomic range for this enzyme is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
2.6.1.104
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RECOMMENDED NAME
GeneOntology No.
3-dehydro-glucose-6-phosphate-glutamate transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
kanosamine 6-phosphate + 2-oxoglutarate = 3-dehydro-D-glucose 6-phosphate + L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
kanosamine biosynthesis II
SYSTEMATIC NAME
IUBMB Comments
kanosamine 6-phosphate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
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
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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a pyridoxal-phosphate protein
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme shares the common type 1 aspartate aminotransferase fold with residues from both monomers forming the active site. The structure of the enzyme alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only alpha-D-kanosamine 6-phosphate is observed in the active site of NtdA, not the beta-anomer
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of the N-terminal hexahistidine-tagged protein in Escherichia coli
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