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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: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
AGX-1, AGX1, GalNAc-1-P UTase, More, N-acetyl-D-galactosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase, ST0452, STK_04520, UAP1, UDP-N-acetylgalactosamine pyrophosphorylase, 
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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)
additional information
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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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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 + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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
?
-
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
-
-
?
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
r
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
AGX1
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
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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-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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
-
-
?
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
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
reaction of EC 2.7.7.23
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
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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
-
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
7.5
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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
additional information
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues. AGX-1 is an UDP-N-acetylgalactosamine diphosphorylase, EC 2.7.7.83, and AGX-2 is an UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the naturally occuring UAP1 A229T mutation is potentially pathogenic. The A229T mutation induces structural changes, leading to reduced thermal stability and activity of the mutant compared to wild-type
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 CysâCys bonds contribute to its thermostability
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
additional information
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues
additional information
-
the ST0452 protein contains only two Cys residues, it is unlikely that CysâCys bonds contribute to its thermostability
-
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
-
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
-
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
-
additional information
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
the ST0452 protein contains only two Cys residues, it is unlikely that CysâCys bonds contribute to its thermostability
-
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
-
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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). S1PNA_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
401
0
44516
Swiss-Prot
-
UAP1_MOUSE
522
0
58609
Swiss-Prot
other Location (Reliability: 2)
UAP2_ARATH
502
0
55760
Swiss-Prot
other Location (Reliability: 4)
UAP1_ARATH
505
0
55992
Swiss-Prot
other Location (Reliability: 4)
UAP1_HUMAN
522
0
58769
Swiss-Prot
other Location (Reliability: 2)
A0A2G9I7C4_9LAMI
486
0
53925
TrEMBL
other Location (Reliability: 3)
A0A5B6ZY38_DAVIN
488
0
54143
TrEMBL
other Location (Reliability: 4)
A0A1Z5KQN2_FISSO
467
0
50819
TrEMBL
other Location (Reliability: 2)
A0A1Z5K0U4_FISSO
466
0
50880
TrEMBL
other Location (Reliability: 2)
A0A084G4V5_PSEDA
487
0
53186
TrEMBL
other Location (Reliability: 2)
A0A7W0C7N1_9DELT
396
0
42777
TrEMBL
-
A0A7R8CVS3_LEPSM
306
0
33540
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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 1â210) and the C-terminal acetyltransferase domain (residues 211â401), 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
purified recombinant detagged AGX1A229T in complex with UDP-GlcNAc, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement using the published AGX1 structure (PDB ID 1JV1) as a search model
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A229T
naturally occuring enzyme AGX1 mutation, and site-directed mutagenesis, the A229T mutation causes a reduction of protein thermal stability compared to wild-type AGX1, and AGX1A229T has lower activity in producing UDP-GlcNA. In diploid organisms, haploinsufficiency is a phenomenon in which a single copy of a functional gene is not sufficient to produce the normal/wild-type phenotype. The patient is only heterozygous for the UAP1 A229T missense mutation. The UAP1 gene is potentially haploinsufficient and LoF intolerant, and the heterozygous UAP1 A229T mutation is potentially pathogenic. The recombinant mutant enzyme shows a reduction of the melting temperature (Tm) by approximately 5.3°C compared to wild-type. The A229T mutation induces structural changes. The R228-E44 interaction is abolished in the AGX1A229T structure caused by the position shift of R228. The pushing effect is likely due to the bulkier side chain of threonine compared to that of alanine. Along with the conformational change of the N-terminal domain in the AGX1A229T structure, M218 is shifted by 0.8 A away from R169, weakening the Q112-R169-M218 interaction
R115A
H308A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type
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
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
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
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
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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
recombinant N-terminally GST-tagged wild-type and mutant AGX1 from Escherichia coli strain (DE3) pLysS by glutathione affinity chromatography, the tag is cleaved off by PreScission protease, followed by gel filtration, and ultrafiltration
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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
gene UAP1 encodes two different isoforms, named AGX1 and AGX2, recombinant expression of N-terminally GST-tagged wild-type and mutant AGX1 in Escherichia coli strain (DE3) pLysS
recombinant expression of His-tagged wild-type enzyme and mutant Y97N in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
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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, 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
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)
brenda
Chen, X.; Raimi, O.G.; Ferenbach, A.T.; van Aalten, D.M.F.
A missense mutation in a patient with developmental delay affects the activity and structure of the hexosamine biosynthetic pathway enzyme AGX1
FEBS Lett.
595
110-122
2020
Homo sapiens (Q16222)
brenda
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