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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
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Word Map
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  • 2.7.7.83
  • curl
  • whitefly
  • tabaci
  • bemisia
  • begomovirus
  • intergenic
  • geminivirus
  • viruliferous
  • virus-induced
  • geminiviridae
  • agroinoculation
  • epidemic
  • lycopersicum
  • replication-associated
  • solanum
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
galnac-1-p utase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetyl-D-galactosamine-1-phosphate uridyltransferase
-
additional information
see also EC 2.7.7.23
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
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
show the reaction diagram
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
reaction of EC 2.7.7.23
-
-
?
additional information
?
-
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
-
-
?
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
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
reaction of EC 2.7.7.23
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the three-dimensional structure of the ST0452 mutant Y97N is not changed by due to lack of metals but the interactions with the substrate is slightly modified, which might cause the activity to increase
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
the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine
physiological function
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant Y97N in complex with UTP or N-acetyl-alpha-D-glucosamine 1-phosphate, sitting drop vapor diffusion method, mixing of 11 mg/ml protein with ligands 5 mM UDP-GlcNAc and 10 mM (NH4)2SO4 (to form the complex with UDP-GlcNAc) or 5 mM UTP and 10 mM (NH4)2SO4 (to form the complex with UTP), and with cyrstallization solution containing 20% w/v PEG 3350 and 0.2 M potassium citrate tribasic monohydrate, X-ray diffraction structure determination and analysis at 2.91 and 2.09 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H308A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type
K337A
site-directed mutagenesis
K340A
site-directed mutagenesis
N331A
site-directed mutagenesis
T80A
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80C
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80D
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
T80E
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80F
site-directed mutagenesis, the mutant shows no and Glc-1-P UTase and GlcNAc-1-P UTase activity
T80G
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80H
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
T80I
site-directed mutagenesis, the mutant shows no Glc-1-P UTase and GlcNAc-1-P UTase activity
T80K
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80L
site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity
T80M
site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity
T80N
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
T80P
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80Q
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80R
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80S
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
T80S/Y97N
site-directed mutagenesis, the mutant shows 6.5times higher activity with N-acetylglucosamine-1-phosphate compared to that of the wild-type ST0452 protein
T80V
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80W
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80Y
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
Y311A
site-directed mutagenesis
Y97N
naturally occuring mutation, the Y97N mutant of the ST0452 protein, isolated from Sulfolobus tokodaii, exhibits over 4times higher N-acetylglucosamine-1-phosphate (GlcNAc-1-P) uridyltransferase (UTase, EC 2.7.7.23) activity, compared with that of the wild-type ST0452 protein, three-dimensional structure analysis of the Y97N protein. The overall structure is almost identical to that of the wild-type ST0452 protein (PDB ID 2GGO), with residue 97 (Asn) interacting with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme and mutant Y97N from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and ultrafiltration
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
recombinant expression of His-tagged wild-type enzyme and mutant Y97N in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
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, 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
Honda, Y.; Nakano, S.; Ito, S.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering
Appl. Environ. Microbiol.
84
e02213-18
2018
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9), Sulfurisphaera tokodaii JCM 10545 (Q975F9), Sulfurisphaera tokodaii NBRC 100140 (Q975F9)
Manually annotated by BRENDA team