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Information on EC 2.7.7.83 - UDP-N-acetylgalactosamine diphosphorylase
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2.7.7.83 UDP-N-acetylgalactosamine diphosphorylaseIUBMB 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].
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Word Map
- 2.7.7.83
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curl
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whitefly
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tabaci
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bemisia
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begomovirus
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intergenic
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geminivirus
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viruliferous
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virus-induced
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geminiviridae
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agroinoculation
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epidemic
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lycopersicum
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replication-associated
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solanum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ST0452
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
-
alternatively spliced isoform to AGX1, differs from those referenced in the literature by two changes: S445G and Q454S (most probably a gene polymorphism)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
UTP + N-acetylglucosamine 1-phosphate
-
-
-
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
-
-
-
-
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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-
-
r
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
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-
-
?
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
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-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
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
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
-
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
N-acetyl-D-galactosamine 1-phosphate
-
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
-
GST-fusion protein, N-acetylglucosamine 1-phosphate, pH 7.5, 37°C
0.32
N-acetyl-D-glucosamine 1-phosphate
-
GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.119
-
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
0.525
-
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
-
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
1.342
-
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
metabolism
-
the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
physiological function
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
-
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
additional information
the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
additional information
-
the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
additional information
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UAP1_ARATH
505
0
55992
Swiss-Prot
other Location (Reliability: 4)
UAP1_HUMAN
522
0
58769
Swiss-Prot
other Location (Reliability: 2)
UAP1_MOUSE
522
0
58609
Swiss-Prot
other Location (Reliability: 2)
UAP2_ARATH
502
0
55760
Swiss-Prot
other Location (Reliability: 4)
S1PNA_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
401
0
44516
Swiss-Prot
-
A0A2G9I7C4_9LAMI
486
0
53925
TrEMBL
other Location (Reliability: 3)
A0A5B6ZY38_DAVIN
488
0
54143
TrEMBL
other Location (Reliability: 4)
A0A084G4V5_PSEDA
487
0
53186
TrEMBL
other Location (Reliability: 2)
A0A1Z5KQN2_FISSO
467
0
50819
TrEMBL
other Location (Reliability: 2)
A0A1Z5K0U4_FISSO
466
0
50880
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
74000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
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
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R115A
H308A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type
additional information
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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