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Information on EC 2.7.7.83 - UDP-N-acetylgalactosamine diphosphorylase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q975F9

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].
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This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q975F9
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
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
Synonyms
N-acetyl-D-galactosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase, ST0452, UDP-N-acetylglucosamine pyrophosphorylase AGX1, UDP-N-acetylglucosamine pyrophosphorylase AGX2, UDP-N-acetylhexosamine pyrophosphorylase AGX1, UDP-N-acetylhexosamine pyrophosphorylase AGX2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetyl-D-galactosamine-1-phosphate uridyltransferase
299945
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ST0452
PATHWAY SOURCE
PATHWAYS
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
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-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
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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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
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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