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Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Drosophila melanogaster and UniProt Accession Q9Y0Z0

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EC Tree
IUBMB Comments
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate .
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Drosophila melanogaster
UNIPROT: Q9Y0Z0
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-n-acetylglucosamine pyrophosphorylase, lmuap1, glmumtb, glcnac-1-p utase, spl29, udp-n-acetylglucosamine pyrophosphorylase (uap), udp-n-acetylglucosamine pyrophosphorylase 1, n-acetylglucosamine 1-phosphate uridyltransferase, agx-1, udp-n-acetylhexosamine pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-N-acetylglucosamine pyrophosphorylase
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acetylglucosamine 1-phosphate uridylyltransferase
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GlmU
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UDP-GlcNAc pyrophosphorylase
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-
-
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UDP-HexNAc pyrophosphorylase
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-
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UDP-N-acetylglucosamine-diphosphorylase
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UDPacetylglucosamine pyrophosphorylase
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uridine diphosphate-N-acetylglucosamine pyrophosphorylase
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uridine diphosphoacetylglucosamine phosphorylase
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uridine diphosphoacetylglucosamine pyrophosphorylase
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UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase
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Ydl103c protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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-
SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
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SUBSTRATE
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-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
?
additional information
?
-
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glycosylation pathway
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-
?
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-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
?
additional information
?
-
-
glycosylation pathway
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
temporal profile of mmy transcription in early embryogenesis, overview
Manually annotated by BRENDA team
expression early in embryogenesis, expression occurs ubiquitously and uniformly in the cellular blastoderm and accumulates in the developing mesoderm, gut primordia, and trachea
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
organization andexpression of the mmy gene in Drosophila species, overview
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
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
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9Y0Z0_DROME
520
0
58214
TrEMBL
Mitochondrion (Reliability: 3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mmy, quantitative RT-PCR expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schimmelpfeng, K.; Strunk, M.; Stork, T.; Klaembt, C.
Mummy encodes an UDP-N-acetylglucosamine-dipohosphorylase and is required during Drosophila dorsal closure and nervous system development
Mech. Dev.
123
487-499
2006
Drosophila melanogaster
Manually annotated by BRENDA team
Humphreys, G.B.; Jud, M.C.; Monroe, K.M.; Kimball, S.S.; Higley, M.; Shipley, D.; Vrablik, M.C.; Bates, K.L.; Letsou, A.
Mummy, A UDP-N-acetylglucosamine pyrophosphorylase, modulates DPP signaling in the embryonic epidermis of Drosophila
Dev. Biol.
381
434-445
2013
Drosophila melanogaster, Drosophila melanogaster (Q9Y0Z0)
Manually annotated by BRENDA team