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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.
The enzyme appears in viruses and cellular organisms
Synonyms
3-oxo-glucose-6-phosphate:glutamate aminotransferase,
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3-oxo-glucose-6-phosphate:glutamate aminotransferase
3-oxo-glucose-6-phosphate:glutamate aminotransferase
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3-oxo-glucose-6-phosphate:glutamate aminotransferase
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ntdA
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kanosamine 6-phosphate + 2-oxoglutarate = 3-dehydro-D-glucose 6-phosphate + L-glutamate
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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.
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kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
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?
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
the enzyme is involved in a kanosamine biosynthesis pathway
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?
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
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?
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
the enzyme is involved in a kanosamine biosynthesis pathway
-
?
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kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
the enzyme is involved in a kanosamine biosynthesis pathway
-
-
?
kanosamine 6-phosphate + 2-oxoglutarate
3-dehydro-D-glucose 6-phosphate + L-glutamate
the enzyme is involved in a kanosamine biosynthesis pathway
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-
?
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pyridoxal 5'-phosphate
a pyridoxal-phosphate protein
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SwissProt
brenda
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SwissProt
brenda
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physiological function
the enzyme is involved in a kanosamine biosynthesis pathway
physiological function
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the enzyme is involved in a kanosamine biosynthesis pathway
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NTDA_BACSU
Bacillus subtilis (strain 168)
441
0
50141
Swiss-Prot
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A0A6I7CQC2_BACIU
441
0
50153
TrEMBL
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A0A1D8FIP6_BACIU
441
0
50141
TrEMBL
-
A0A1J5R4J7_9ZZZZ
556
0
61262
TrEMBL
other Location (Reliability: 5 )
A0A5C0WEE1_BACIA
441
0
49134
TrEMBL
-
A0A498U4V8_BACPU
441
0
49160
TrEMBL
-
A0A1F2PFG1_9FIRM
445
0
50687
TrEMBL
-
A0A654N5B3_BACIU
441
0
50141
TrEMBL
-
A0A6I7BW06_BACIU
441
0
50094
TrEMBL
-
A0A6G2IV72_BACIU
441
0
50109
TrEMBL
-
A0A6H0H0G1_BACIU
441
0
50141
TrEMBL
-
A0A6D1P1W4_ECOLX
408
0
45665
TrEMBL
-
A0A410YQJ5_BACIU
441
0
50157
TrEMBL
-
A0A6I7A0G8_BACIU
441
0
50127
TrEMBL
-
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Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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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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expression in Escherichia coli
expression of the N-terminal hexahistidine-tagged protein in Escherichia coli
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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)
brenda
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)
brenda
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2.6.1.104 3-dehydro-glucose-6-phosphate-glutamate transaminase
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