Literature summary extracted from

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 (2018), Appl. Environ. Microbiol., 84, e02213-18 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.7.7.23	recombinant expression of His-tagged wild-type enzyme and mutant Y97N in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL	Sulfurisphaera tokodaii
2.7.7.83	recombinant expression of His-tagged wild-type enzyme and mutant Y97N in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL	Sulfurisphaera tokodaii

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.7.7.23	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 crystallization 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	Sulfurisphaera tokodaii
2.7.7.83	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	Sulfurisphaera tokodaii

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.7.7.23	additional information	all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein	Sulfurisphaera tokodaii
2.7.7.23	T80A	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80C	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80D	site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80E	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80F	site-directed mutagenesis, the mutant shows no and Glc-1-P UTase and GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80G	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80H	site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80I	site-directed mutagenesis, the mutant shows no Glc-1-P UTase and GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80K	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80L	site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80M	site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80N	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80P	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80Q	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80R	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80S	site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	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	Sulfurisphaera tokodaii
2.7.7.23	T80V	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.23	T80W	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	T80Y	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.23	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	Sulfurisphaera tokodaii
2.7.7.83	additional information	all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein	Sulfurisphaera tokodaii
2.7.7.83	T80A	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80C	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80D	site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80E	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80F	site-directed mutagenesis, the mutant shows no and Glc-1-P UTase and GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80G	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80H	site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80I	site-directed mutagenesis, the mutant shows no Glc-1-P UTase and GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80K	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80L	site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80M	site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80N	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80P	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80Q	site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80R	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80S	site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	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	Sulfurisphaera tokodaii
2.7.7.83	T80V	site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type	Sulfurisphaera tokodaii
2.7.7.83	T80W	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	T80Y	site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity	Sulfurisphaera tokodaii
2.7.7.83	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	Sulfurisphaera tokodaii

Metals/Ions

EC Number	Metals/Ions	Comment	Organism
2.7.7.23	Mg2+	required	Sulfurisphaera tokodaii
2.7.7.23	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	Sulfurisphaera tokodaii
2.7.7.83	Mg2+	required	Sulfurisphaera tokodaii
2.7.7.83	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	Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii	reaction of EC 2.7.7.83	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii 7	reaction of EC 2.7.7.83	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii DSM 16993	reaction of EC 2.7.7.83	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii JCM 10545	reaction of EC 2.7.7.83	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii NBRC 100140	reaction of EC 2.7.7.83	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii	-	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii 7	-	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii DSM 16993	-	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii JCM 10545	-	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii NBRC 100140	-	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii 7	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii DSM 16993	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii JCM 10545	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	Sulfurisphaera tokodaii NBRC 100140	-	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii	reaction of EC 2.7.7.23	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii 7	reaction of EC 2.7.7.23	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii DSM 16993	reaction of EC 2.7.7.23	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii JCM 10545	reaction of EC 2.7.7.23	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	Sulfurisphaera tokodaii NBRC 100140	reaction of EC 2.7.7.23	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.7.23	Sulfurisphaera tokodaii	Q975F9	Sulfolobus tokodaii	-
2.7.7.23	Sulfurisphaera tokodaii 7	Q975F9	Sulfolobus tokodaii	-
2.7.7.23	Sulfurisphaera tokodaii DSM 16993	Q975F9	Sulfolobus tokodaii	-
2.7.7.23	Sulfurisphaera tokodaii JCM 10545	Q975F9	Sulfolobus tokodaii	-
2.7.7.23	Sulfurisphaera tokodaii NBRC 100140	Q975F9	Sulfolobus tokodaii	-
2.7.7.83	Sulfurisphaera tokodaii	Q975F9	Sulfolobus tokodaii	-
2.7.7.83	Sulfurisphaera tokodaii 7	Q975F9	Sulfolobus tokodaii	-
2.7.7.83	Sulfurisphaera tokodaii DSM 16993	Q975F9	Sulfolobus tokodaii	-
2.7.7.83	Sulfurisphaera tokodaii JCM 10545	Q975F9	Sulfolobus tokodaii	-
2.7.7.83	Sulfurisphaera tokodaii NBRC 100140	Q975F9	Sulfolobus tokodaii	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.7.7.23	recombinant His-tagged wild-type enzyme and mutant Y97N from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and ultrafiltration	Sulfurisphaera tokodaii
2.7.7.83	recombinant His-tagged wild-type enzyme and mutant Y97N from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and ultrafiltration	Sulfurisphaera tokodaii

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.7.7.23	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.23	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii 7	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.23	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii DSM 16993	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.23	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii JCM 10545	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.23	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii NBRC 100140	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	reaction of EC 2.7.7.83	Sulfurisphaera tokodaii	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	reaction of EC 2.7.7.83	Sulfurisphaera tokodaii 7	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	reaction of EC 2.7.7.83	Sulfurisphaera tokodaii DSM 16993	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	reaction of EC 2.7.7.83	Sulfurisphaera tokodaii JCM 10545	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	reaction of EC 2.7.7.83	Sulfurisphaera tokodaii NBRC 100140	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	-	Sulfurisphaera tokodaii	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	-	Sulfurisphaera tokodaii 7	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	-	Sulfurisphaera tokodaii DSM 16993	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	-	Sulfurisphaera tokodaii JCM 10545	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.23	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	-	Sulfurisphaera tokodaii NBRC 100140	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + alpha-D-glucose 1-phosphate	-	Sulfurisphaera tokodaii	diphosphate + UDP-alpha-D-glucose	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii 7	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii DSM 16993	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii JCM 10545	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-galactosamine 1-phosphate	-	Sulfurisphaera tokodaii NBRC 100140	diphosphate + UDP-N-acetyl-alpha-D-galactosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	reaction of EC 2.7.7.23	Sulfurisphaera tokodaii	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	reaction of EC 2.7.7.23	Sulfurisphaera tokodaii 7	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	reaction of EC 2.7.7.23	Sulfurisphaera tokodaii DSM 16993	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	reaction of EC 2.7.7.23	Sulfurisphaera tokodaii JCM 10545	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?
2.7.7.83	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate	reaction of EC 2.7.7.23	Sulfurisphaera tokodaii NBRC 100140	diphosphate + UDP-N-acetyl-alpha-D-glucosamine	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
2.7.7.23	GlcNAc-1-P UTase	-	Sulfurisphaera tokodaii
2.7.7.23	More	see also EC 2.7.7.83	Sulfurisphaera tokodaii
2.7.7.23	ST0452	-	Sulfurisphaera tokodaii
2.7.7.23	STK_04520	-	Sulfurisphaera tokodaii
2.7.7.83	GalNAc-1-P UTase	-	Sulfurisphaera tokodaii
2.7.7.83	More	see also EC 2.7.7.23	Sulfurisphaera tokodaii
2.7.7.83	ST0452	-	Sulfurisphaera tokodaii
2.7.7.83	STK_04520	-	Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.7.7.23	80	-	assay at	Sulfurisphaera tokodaii
2.7.7.83	80	-	assay at	Sulfurisphaera tokodaii

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.7.7.23	7.5	-	assay at	Sulfurisphaera tokodaii
2.7.7.83	7.5	-	assay at	Sulfurisphaera tokodaii

General Information

EC Number	General Information	Comment	Organism
2.7.7.23	additional information	analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP	Sulfurisphaera tokodaii
2.7.7.23	physiological function	enzyme ST0452 is multifunctional	Sulfurisphaera tokodaii
2.7.7.83	additional information	analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP	Sulfurisphaera tokodaii
2.7.7.83	physiological function	enzyme ST0452 is multifunctional	Sulfurisphaera tokodaii