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Information on EC 2.7.7.83 - UDP-N-acetylgalactosamine diphosphorylase for references in articles please use BRENDA:EC2.7.7.83
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EC Tree
IUBMB Comments The enzyme from plants and animals also has activity toward N-acetyl-alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
Word Map
2.7.7.83
curl
whitefly
tabaci
bemisia
begomovirus
intergenic
geminivirus
viruliferous
virus-induced
geminiviridae
agroinoculation
epidemic
lycopersicum
replication-associated
solanum
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
N-acetyl-D-galactosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase,
ST0452 ,
UAP1 , UDP-N-acetylglucosamine pyrophosphorylase AGX1, UDP-N-acetylglucosamine pyrophosphorylase AGX2, UDP-N-acetylhexosamine pyrophosphorylase AGX1, UDP-N-acetylhexosamine pyrophosphorylase AGX2,
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N-acetyl-D-galactosamine-1-phosphate uridyltransferase
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N-acetylglucosamine 1-phosphate uridyltransferase
-
UDP-N-acetylglucosamine pyrophosphorylase AGX1
alternatively spliced isoform to AGX2, differs from those referenced in the literature by one change: S445G (most probably a gene polymorphism)
UDP-N-acetylglucosamine pyrophosphorylase AGX2
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alternatively spliced isoform to AGX1, differs from those referenced in the literature by two changes: S445G and Q454S (most probably a gene polymorphism)
UDP-N-acetylhexosamine pyrophosphorylase AGX1
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isoform of AGX2
UDP-N-acetylhexosamine pyrophosphorylase AGX2
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isoform of AGX1
ST0452
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UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase
The enzyme from plants and animals also has activity toward N-acetyl-alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
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diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
UTP + N-acetylglucosamine 1-phosphate
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-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
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-
-
-
r
UTP + N-acetyl-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
-
r
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
-
-
-
r
additional information
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
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diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
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-
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r
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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the enzyme is involved in biosyntheis of UDP-N-acetyl-alpha-D-galactosamine
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-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
the enzyme is involved in biosyntheis of UDP-N-acetyl-alpha-D-galactosamine
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-
?
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UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
the enzyme is involved in biosyntheis of UDP-N-acetyl-alpha-D-galactosamine
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
the enzyme is involved in biosyntheis of UDP-N-acetyl-alpha-D-galactosamine
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-
?
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0.38 - 1.3
N-acetyl-D-galactosamine 1-phosphate
0.24 - 0.32
N-acetyl-D-glucosamine 1-phosphate
0.0053 - 0.006
N-acetylglucosamine 1-phosphate
0.5 - 0.53
UDP-N-acetyl-alpha-D-galactosamine
0.032
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C; wild type protein, pH 8.0, 30°C
0.38
N-acetyl-D-galactosamine 1-phosphate
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GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, pH 7.5, 37°C
1.3
N-acetyl-D-galactosamine 1-phosphate
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GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, pH 7.5, 37°C
0.24
N-acetyl-D-glucosamine 1-phosphate
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GST-fusion protein, N-acetylglucosamine 1-phosphate, pH 7.5, 37°C
0.32
N-acetyl-D-glucosamine 1-phosphate
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GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
0.0053
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
0.006
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
0.5
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
0.53
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
0.049
UTP
wild type protein, pH 8.0, 30°C
0.053
UTP
wild type protein, pH 8.0, 30°C
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11200 - 12200
N-acetylglucosamine 1-phosphate
180 - 200
UDP-N-acetyl-alpha-D-galactosamine
2000 - 2200
UDP-N-acetylglucosamine
11200
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
12200
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
180
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
200
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
2000
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
2200
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
1200
UTP
wild type protein, pH 8.0, 30°C
1400
UTP
wild type protein, pH 8.0, 30°C
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0.119
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GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, GST protein shows 0.02 micromol/min/mg in the assay, pH 7.5, 37°C
0.3
-
GST fusion removed, N-acetyl-D-galactosamine 1-phosphate, pH 7.5, 37°C
0.525
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GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, GST protein shows 0.033 micromol/min/mg in the assay, pH 7.5, 37°C
0.887
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GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, GST protein shows 0.033 micromol/min/mg in the assay, pH 7.5, 37°C
0.9
R115A mutant protein, pH 8.0, 30°C
1.342
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GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, GST protein shows 0.02 micromol/min/mg in the assay, pH 7.5, 37°C
1.5
R115A mutant protein, pH 8.0, 30°C
14.9
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GST fusion removed, N-acety-D-lgalactosamine 1-phosphate, pH 7.5, 37°C
5.873
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GST fusion removed, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
5.919
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GST fusion removed, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
68
wild type protein, pH 8.0, 30°C
69
wild type protein, pH 8.0, 30°C
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SwissProt
brenda
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SwissProt
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SwissProt
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SwissProt
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UniProt
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brenda
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brenda
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metabolism
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the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
metabolism
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the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
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physiological function
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because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
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because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
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additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
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UAP1_HUMAN
522
0
58769
Swiss-Prot
UAP1_MOUSE
522
0
58609
Swiss-Prot
UAP2_ARATH
502
0
55760
Swiss-Prot
S1PNA_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
401
0
44516
Swiss-Prot
UAP1_ARATH
505
0
55992
Swiss-Prot
Q9Z750_CHLPN
461
0
51990
TrEMBL
A0A2G9I7C4_9LAMI
486
0
53925
TrEMBL
A0A084G4V5_9PEZI
487
0
53186
TrEMBL
A0A1Z5KQN2_FISSO
467
0
50819
TrEMBL
A0A1Z5K0U4_FISSO
466
0
50880
TrEMBL
A0A5B6ZY38_DAVIN
488
0
54143
TrEMBL
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57000
-
x * 57000, SDS-PAGE
64000
-
x * 64000, SDS-PAGE
74000
2 * 74000, gel filtration; gel filtration
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?
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x * 57000, SDS-PAGE; x * 64000, SDS-PAGE
homodimer
2 * 74000, gel filtration
monomer
74000, gel filtration
trimer
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the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
additional information
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the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability
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vapor diffusion technique, PEG600, 20°C, pH5.7; vapor diffusion technique, PEG600, 20°C, pH5.7
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R115A
activity drastically affected; activity drastically affected, no dimer formation
H308A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type
K337A
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site-directed mutagenesis
K340A
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site-directed mutagenesis
N331A
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site-directed mutagenesis
Y311A
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site-directed mutagenesis
additional information
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construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein
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affinity chromatography (glutathione-Sepharose), GST part removed
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anion exchange, phenyl interaction and gel filtration; anion exchange, phenyl interaction and gel filtration
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expressed in Escherichia coli XL1 Blue; expressed in Escherichia coli XL1 Blue
gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
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GST fusion protein expressed in Escherichia coli JM109
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Wang-Gillam, A.; Pastuszak, I.; Elbein, A.D.
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc
J. Biol. Chem.
273
27055-27057
1998
Homo sapiens
brenda
Peneff, C.; Ferrari, P.; Charrier, V.; Taburet, Y.; Monnier, C.; Zamboni, V.; Winter, J.; Harnois, M.; Fassy, F.; Bourne, Y.
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: Role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture
EMBO J.
20
6191-6202
2001
Homo sapiens, Homo sapiens (Q16222)
brenda
Zhang, Z.; Akutsu, J.; Kawarabayasi, Y.
Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7
J. Bacteriol.
192
3287-3293
2010
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
brenda
Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.
Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein
Extremophiles
19
417-427
2015
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q975F9)
brenda
Dadashipour, M.; Iwamoto, M.; Hossain, M.M.; Akutsu, J.I.; Zhang, Z.; Kawarabayasi, Y.
Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii
J. Bacteriol.
200
e00048-18
2018
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9)
brenda
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2.7.7.83 UDP-N-acetylgalactosamine diphosphorylase
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