Information on EC 2.6.1.34 - UDP-N-acetylbacillosamine transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.34
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylbacillosamine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
show the reaction diagram
; A pyridoxal-phosphate protein; A pyridoxal-phosphate protein.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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CMP-diacetamido-8-epilegionaminic acid biosynthesis
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UDP-N,N'-diacetylbacillosamine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
CAS REGISTRY NUMBER
COMMENTARY hide
37277-89-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Campylobacter jejuni subsp. jejuni serotype O:2
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UniProt
Manually annotated by BRENDA team
Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819
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UniProt
Manually annotated by BRENDA team
type XIV, ATCC 6314
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
show the reaction diagram
UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
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
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
show the reaction diagram
UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a pyridoxal 5'-phosphate protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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not affected by MgCl2 at 0.01 M
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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absolute requirement
additional information
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not affected by EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose
pH 7.7, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose
Campylobacter jejuni
Q0P9D3
pH 7.7, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of PglE in complex with an external aldimine, to 2.0 A resolution. In presence of the external aldimine, a dramatic movement of the loops defined by Ser24 to Gly31 and Tyr180 to Gly190 takes place. Comparison of PglE to sugar aminotransferases PseC, DesI, and ArnB
Campylobacter jejuni subsp. jejuni serotype O:2
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, stable for at least 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
type XIV, ATCC 6314, partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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