Literature summary for 2.7.7.83 extracted from

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 (2015), Extremophiles, 19, 417-427.

Search for more literature for 2.7.7.83

Cloned(Commentary)

Cloned (Comment)	Organism
gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL	Sulfurisphaera tokodaii

Protein Variants

Protein Variants	Comment	Organism
H308A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type	Sulfurisphaera tokodaii
K337A	site-directed mutagenesis	Sulfurisphaera tokodaii
K340A	site-directed mutagenesis	Sulfurisphaera tokodaii
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	Sulfurisphaera tokodaii
N331A	site-directed mutagenesis	Sulfurisphaera tokodaii
Y311A	site-directed mutagenesis	Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?

Organism

Organism	UniProt	Comment	Textmining
Sulfurisphaera tokodaii	Q975F9	-	-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7	Q975F9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	Sulfurisphaera tokodaii	?	-	?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), 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	Sulfurisphaera tokodaii
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	Sulfurisphaera tokodaii

Synonyms

Synonyms	Comment	Organism
N-acetyl-D-galactosamine-1-phosphate uridyltransferase	-	Sulfurisphaera tokodaii
ST0452	-	Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
80	-	assay at	Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Sulfurisphaera tokodaii

General Information

General Information	Comment	Organism
additional information	the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability	Sulfurisphaera tokodaii

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Release 2023.1 (January 2023)