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Information on EC 2.6.1.104 - 3-dehydro-glucose-6-phosphate-glutamate transaminase and Organism(s) Bacillus subtilis and UniProt Accession O07566

for references in articles please use BRENDA:EC2.6.1.104
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IUBMB Comments
A pyridoxal-phosphate protein. The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
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This record set is specific for:
Bacillus subtilis
UNIPROT: O07566
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
3-oxo-glucose-6-phosphate:glutamate aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-oxo-glucose-6-phosphate:glutamate aminotransferase
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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.
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 SUBSTRATE
NATURAL 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
the enzyme is involved in a kanosamine biosynthesis pathway
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a pyridoxal-phosphate protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in a kanosamine biosynthesis pathway
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the N-terminal hexahistidine-tagged protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vetter, N.D.; Langill, D.M.; Anjum, S.; Boisvert-Martel, J.; Jagdhane, R.C.; Omene, E.; Zheng, H.; van Straaten, K.E.; Asiamah, I.; Krol, E.S.; Sanders, D.A.; Palmer, D.R.
A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis
J. Am. Chem. Soc.
135
5970-5973
2013
Bacillus subtilis (O07566), Bacillus subtilis, Bacillus subtilis 168 (O07566)
Manually annotated by BRENDA team
van Straaten, K.E.; Ko, J.B.; Jagdhane, R.; Anjum, S.; Palmer, D.R.; Sanders, D.A.
The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases
J. Biol. Chem.
288
34121-34130
2013
Bacillus subtilis (O07566)
Manually annotated by BRENDA team