2.7.7.23	evolution	although Entamoeba histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite Trypanosoma brucei	737391	
2.7.7.23	evolution	comparison of the activities of the ST0452 protein to those of similar enzymes from bacteria show that both the apparent Km and kcat values of the ST0452 GlcNAc-1-P UTase activity are smaller than those of Escherichia coli GlmU (EcGlmU) enzymes indicating that the archaeal ST0452 protein can accept a low concentration of substrate but that its turnover rate is lower than that of the EcGlmU enzyme	-, 755852	
2.7.7.23	evolution	GlmU belongs to the large family of sugar nucleotidyl transferases, which can be classified into group-I, which employs the two-metal mechanism-B as in GlmU, and group-II that employs a variant one metal mechanism-B, wherein the role of Mg2+ A is substituted by a conserved lysine. Eukaryotic sugar nucleotidyl transferases appear confined to group-II, structure-based sequence comparisons of sugar nucleotidyl transferases	740866	
2.7.7.23	evolution	organization andexpression of the mmy gene in Drosophila species, overview	738089	
2.7.7.23	evolution	the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence	-, 735569	
2.7.7.23	evolution	the N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme exclusive to prokaryotes, that belongs to the family of sugar nucleotidyltransferases (SNTs)	735396	
2.7.7.23	evolution	UAP isozymes are encoded by two different genes, LmUAP1 and LmUAP2	739475	
2.7.7.23	malfunction	GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview	-, 737150	
2.7.7.23	malfunction	independently-derived mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized Dpp-dependent closure abnormalities (dorsal closure and head involution). In particular, the mmy-associated cuticle defects are identical to those resulting from loss-of-function mutations in raw and anterior-open	738089	
2.7.7.23	malfunction	knockdown of LdUAP1 reduces chitin contents in whole larvae and integument samples, thins tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview	738383	
2.7.7.23	malfunction	silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages PM, and retards larval growth. The resulting larvae have lighter fresh weights, smaller body sizes and depleted fat body. As a result, the development is arrested. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview	738383	
2.7.7.23	malfunction	the inhibition of this enzyme results in the fungal cell death	722022	
2.7.7.23	malfunction	the lesion mimic spl29 mutant exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, leaf phenotype of wild-type and spl29 mutant plants, overview. The phenotype of spl29 is controlled by a single recessive nuclear gene, functional complementation with LOC_Os08g10600 in the spl29 mutant. Irreversible degradation of chloroplasts occurs in early senescent leaves of spl29 mutants. The early senescence phenotype involves upregulated expression levels of senescence-associated transcription factors and senescence-associated genes, and downregulated expression levels of photosynthesis-related genes, overview. Reactive oxygen species and malondialdehyde, as well as abscisic acid and jasmonic acid accumulate in the spl29 mutant accompanied by increased superoxide dismutase activity and normal catalase activity	-, 738765	
2.7.7.23	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	761091	
2.7.7.23	metabolism	N-acetylglucosamine-1-phosphate uridyltransferase is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway	740262	
2.7.7.23	metabolism	pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview	-, 761532	
2.7.7.23	metabolism	the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan	-, 756049	
2.7.7.23	metabolism	the enzyme is involved in biosyntheis of UDP-N-acetylglucosamine	-, 748113	
2.7.7.23	metabolism	the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms	-, 755865	
2.7.7.23	metabolism	the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview	-, 737291	
2.7.7.23	metabolism	the first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reactionis catalysed by N-acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities	-, 741091	
2.7.7.23	metabolism	the mmy-encoded N-acetylglucosamine pyrophosphorylase impacts multiple Drosophila developmental events via the action of several different downstream transferases, some of which modify proteins and lipids with GlcNAc	738089	
2.7.7.23	metabolism	uridine diphosphate N-acetylglucosamine pyrophosphorylase catalyzes the final step in the synthesis of UDP-GlcNAc, which is involved in cell-wall biogenesis in plants and fungi and in protein glycosylation	737391	
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	-, 760395	
2.7.7.23	additional information	enzyme structure modeling and structure comparisons, detailed overview. Conformational changes occur in apo- and ligand-bound BmUAPs. Docking and molecular dynamics simulation studies of ligand-bound complexes of BmUAP, determination of binding mode of UTP, GlcNAc-1-P, and UDP-GlcNAc	760749	
2.7.7.23	additional information	GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein. The enzyme uses a two-metal ion mechanism (mechanism-B). In contrast to well-established two-metal mechanism (mechanism-A) for enzymes acting on nucleic acids, mechanism-B is distinct in the way the two Mg2+ ions (Mg2+A and Mg2+B) are positioned and stabilized. Analysis of the catalytic mechanism for the uridyltransfer reaction in GlmU, role of metal ions in substrate binding, overview	740866	
2.7.7.23	additional information	GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus	720042	
2.7.7.23	additional information	the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism	737391	
2.7.7.23	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	761091	
2.7.7.23	additional information	the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability	-, 729696	
2.7.7.23	additional information	the Tyr103-Asp105 segment is located at the floor of the uridyltransferase active pocket and is involved in interactions with UTP and GlcNAc-1-P substrates	740262	
2.7.7.23	additional information	Tyr at the 97th position of the ST0452 protein plays an important role in catalysis. Reaction scheme of the sugar-1-P UTase, overview	-, 755852	
2.7.7.23	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	-, 725249	
2.7.7.23	physiological function	down-regulation of transcripts by RNA interference prevents larval growth or results in pupal paralysis, depending on time of injection of double-stranded RNAs. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes	722387	
2.7.7.23	physiological function	down-regulation of transcripts by RNA interference results for isoform UAP1 in specific arrest at the larval-larval, larval-pupal or pupal-adult molts, depending on time of injection of double-stranded RNAs, loss of structural integrity and chitin staining and loss of peritrophic matrix-associated chitin. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes	722387	
2.7.7.23	physiological function	enzyme ST0452 is multifunctional	-, 760395	
2.7.7.23	physiological function	injection of early second- and fifth-instar nymphs (1-day-old) or middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP2 RNAi does not interfere with normal development and molting of insects	739475	
2.7.7.23	physiological function	injection of early second- and fifth-instar nymphs (1-day-old) with UAP1 RNAi results in 100% mortality 2 days after the injection. Injection of middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP1 RNAi results in 100% mortality during their next molting process	739475	
2.7.7.23	physiological function	knockdown of UAP1 reduces chitin contents in whole larvae and integument samples, thinned tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of UAP1 and UAP2 causes an additive negative effect	738383	
2.7.7.23	physiological function	N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes	720042	
2.7.7.23	physiological function	N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction	740262	
2.7.7.23	physiological function	N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall	-, 737291	
2.7.7.23	physiological function	N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is exclusive to prokaryotes and a bifunctional enzyme that synthesizes UDP-GlcNAc, an important component of the cell wall of many microorganisms	740866	
2.7.7.23	physiological function	silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages peritrophic matrix, and retards larval growth	738383	
2.7.7.23	physiological function	spl29 mutants display early leaf senescence, chloroplast degradation and both upregulation of senescence transcription factors and senescence-associated genes, and downregulation of photosynthesis-related genes. Defence responses are induced in the spl29 mutant. Reactive oxygen species, including O2 – and H2O2, accumulate in spl29 plants, there is also increased malondialdehyde content. The plant hormones jasmonic acid and abscisic acid also accumulate in spl29 plants	-, 738765	
2.7.7.23	physiological function	SPL29 or UAP1 is probably involved in regulating leaf senescence and defence responses in rice. Leaf senescence is a complex process controlled by a large number of different genes	-, 738765	
2.7.7.23	physiological function	the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively	-, 737150	
2.7.7.23	physiological function	the bifunctional enzyme is found exclusively in bacteria and catalyzes the development of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), an essential intermediate in peptidoglycan biosynthesis in Mycobacterium tuberculosis (Mtb)	-, 760857	
2.7.7.23	physiological function	the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia	-, 735569	
2.7.7.23	physiological function	the enzyme binds N-acetylglucosamine-1-phosphate and UTP, and catalyzes an uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis	735396	
2.7.7.23	physiological function	the enzyme catalyzes the final reaction in the biosynthesis of UDP-GlcNAc, an essential metabolite in many organisms including Trypanosoma brucei,	737319	
2.7.7.23	physiological function	the enzyme functions in the formation of extracellular matrix by producing N-acetylglucosamine (GlcNAc) residues needed for chitin biosynthesis and protein glycosylation	739475	
2.7.7.23	physiological function	the enzyme is essential for chitin synthesis	760749	
2.7.7.23	physiological function	the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms	-, 725308	
2.7.7.23	physiological function	the enzyme is involved in the biosynthesis of chitin, an essential component of the epidermal cuticle and midgut peritrophic matrix in insects	738383	
2.7.7.23	physiological function	the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes	-, 737096	
2.7.7.23	physiological function	the JNK/AP-1 signaling cascade transcriptionally activates BMP signaling in leading edge epidermal cells, while the mummy (mmy) gene product is required for dorsal closure, and functions as a BMP signaling antagonist. The evolutionarily conserved JNK/AP-1 (Jun N-terminal kinase/activator protein 1) and BMP (bone morphogenetic protein) signaling cascades are deployed hierarchically to regulate dorsal closure in the fruit fly Drosophila melanogaster. The mmy gene product is a type of epidermal BMP regulator that transforms a BMP ligand from a long to a short range signal. Gene mmy codes for the single UDP-N-acetylglucosamine pyrophosphorylase in Drosophila, and its requirement for attenuating epidermal BMP signaling during dorsal closure points to another role for glycosylation in defining a highly restricted BMP activity field in the fly. In addition to being the building block of chitin, UDP-GlcNAc is an essential precursor for the synthesis of heparin and chondroitin sulfate proteoglycans, the former having been shown to play an essential role in modulating the effects of Dpp/BMP, Wingless (Wg)/WNT, and Hedgehog (Hh) morphogen signaling in Drosophila and other eukaryotes, usually as a facilitator of long-range signaling. Crucial role for Mmy in regulating embryonic Dpp signaling. Mmy modulation of Dpp signaling is Dpp-dependent and AP-1-independent	738089	
2.7.7.23	physiological function	the mmy gene product isoform RA is an orthologue of the yeast N-acetylglucosamine diphosphorylase QRI1. In Drosophila melanogaster, mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized decapentaplegic-dependent closure abnormalities. UDP-N-acetylglucosamine diphosphorylase activity is required to spatially limit decapentaplegic, the Drosophila melanogaster BMP homolog, activity in a JNK/AP-1-independent fashion	738089	
2.7.7.23	physiological function	the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively	-, 735518	
2.7.7.23	physiological function	the ST0452 protein, a thermostable protein isolated from the thermophilic archaeon Sulfolobus tokodaii, is a bifunctional protein exhibiting sugar-1-phosphate nucleotidylyltransferase (sugar-1-PNTase) and amino-sugar-1-phosphate acetyltransferase activities. ST0452 protein exhibits increased activity following single amino acid substitutions of Ala	-, 755852	
2.7.7.23	physiological function	UDP-N-acetylglucosamine diphosphorylase of Bombyx mori (BmUAP) is an essential enzyme for chitin synthesis in insects. The higher levels of gene expression in integument infer that BmUAP has a significant role in cuticle formation and molting	760749	
2.7.7.23	physiological function	UDP-N-acetylglucosamine pyrophosphorylase (UNAcP) is a key enzyme to construct the fungal cell wall	722022