Information on EC 2.4.1.198 - phosphatidylinositol N-acetylglucosaminyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
2.4.1.198
-
RECOMMENDED NAME
GeneOntology No.
phosphatidylinositol N-acetylglucosaminyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
show the reaction diagram
In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycosylphosphatidylinositol(GPI)-anchor biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-alpha-D-glucosaminyl)transferase
Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetyl-D-glucosaminyltransferase, uridine diphosphoacetylglucosamine alpha1,6-
-
-
-
-
afpig-a
gene is the homologue of GPI3 /SPT14 /pig-A gene (encode the catalytic subunit of glycosylphosphatidylinositol-N-acetylglucoaminyltransferase complex) in Aspergillus fumigatus
afpig-a
Aspergillus fumigatus YJ-407.
gene is the homologue of GPI3 /SPT14 /pig-A gene (encode the catalytic subunit of glycosylphosphatidylinositol-N-acetylglucoaminyltransferase complex) in Aspergillus fumigatus
-
Down syndrome critical region protein 5
-
also known as Pigp, a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
DR437w
-
encodes an essential subunit of the yeast glycosylphosphatidylinositol N-acetylglucosaminyltransferase. The C-terminus is cytoplasmic, the N-terminus is also cytoplasmic and both transmembrane domains pass through the ER membrane. The N-terminal half (at least 60 residues) is dispensable for functions at low temperatures
Dscr5
-
also known as phosphatidylinositol glycan class P (Pigp), a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
glycosylphosphatidylinositol N-acetylglucosaminyltrans­ferase complex
-
-
glycosylphosphatidylinositol-N-acetylglucosaminyltransferase
-
-
GPI-GlcNAc transferase
-
GPI-GlcNAc transferase
-
-
GPI-GnT
Aspergillus fumigatus YJ-407.
-
-
GPI-GnT
-
-
GPI-GnT
-
-
GPI-N-acetylglucosaminyltransferase
-
GPI-N-acetylglucosaminyltransferase
-
-
GPI-N-acetylglucosaminyltransferase
Candida albicans BWP17
-
-
-
GPI-N-acetylglucosaminyltransferase
-
-
GPI-N-acetylglucosaminyltransferase
-
GPI-N-acetylglucosaminyltransferase
-
-
GPI-N-acetylglucosaminyltransferase complex
-
GPI-N-acetylglucosaminyltransferase complex
Aspergillus fumigatus YJ-407.
-
-
GPI19
-
YDR437w (encodes an essential subunit of the yeast glycosylphosphatidylinositol N-acetylglucosaminyltransferase) is also called GPI19 (for glycosylphosphatidylinositol anchor 19)
phosphatidylinositol/UDP-GlcNAc:GlcNAc transferase
-
-
UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase
-
-
-
-
uridine diphosphoacetylglucosamine alpha1,6-acetyl-D-glucosaminyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
144388-35-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
afpig-a; strain YJ-407. Most common opportunistic fungal pathogen of human
Swissprot
Manually annotated by BRENDA team
Aspergillus fumigatus YJ-407.
afpig-a; strain YJ-407. Most common opportunistic fungal pathogen of human
Swissprot
Manually annotated by BRENDA team
GPI-GlcNAc transferase subunit P; formerly Aspergillus nidulans
UniProt
Manually annotated by BRENDA team
gene piga-1 encoding the catalytic subunit of the phosphatidylinositol N-acetylglucosaminyltransferase complex
-
-
Manually annotated by BRENDA team
gene CaGPI19, encoding an accessory subunit of the enzyme complex
-
-
Manually annotated by BRENDA team
Candida albicans BWP17
gene CaGPI19, encoding an accessory subunit of the enzyme complex
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
cDNA that encode a 71-amino acid protein, which is termed PIG-Y (for phosphatidylinositlglycan-class Y). Mouse and rice homologues of PIG-Y, exhibit 79% and 25% amino acid identity with human PIG-Y, respectively. The hydropathy profile of Saccharomyces cerevisiae´s Eri1p is quite similar to PIG-Y and the amino acid identity is 22%. N-terminus and C-terminus face the cytoplasmic side.; from the human T lymphoma KT-3 cDNA library
Swissprot
Manually annotated by BRENDA team
gene hGPI1
SwissProt
Manually annotated by BRENDA team
gene PIG-P
SwissProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
gene mGPI1 clone
GenBank
Manually annotated by BRENDA team
gene PIG-P
Swissprot
Manually annotated by BRENDA team
at least 3 components forming the enzyme complex: GPI1, GPI2 or PIG-C, GPI3 or PIG-A; strain XM37-10c
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae XM37-10c
strain XM37-10c
-
-
Manually annotated by BRENDA team
cloned variant ILTat 1.3, isolated from rat blood
-
-
Manually annotated by BRENDA team
variant MITat 1.4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
knockdown of dscr5 disrupts Knypek membrane localization and causes an enhanced Frizzled 7 receptor endocytosis in a caveolin-dependent manner, dscr5 knockdown promotes specific Dishevelled degradation by the ubiquitin-proteosome pathway, knockdown of dscr5 disrupts convergence of lateral cells and extension of dorsal cells, knockdown of dscr5 does not affect embryonic patterning
malfunction
-
depletingCaGpi19p, an accessory subunit of the enzyme complex that initiates GPI biosynthesis, specifically down-regulates ERG11, altering ergosterol levels and drug response. ERG11 down-regulation is not due to general cell wall defects or GPI deficiency. CaGPI19 mutants show increased cAMP/PKA signalling
malfunction
-
piga-1-knockout worms show 100% lethality, with decreased mitotic germline cells and abnormal eggshell formation. Cell-specific rescue of the null allele, expression of piga-1 in somatic gonads and/or in germline is sufficient for normal embryonic development and the maintenance of the germline mitotic cells. The RNAi phenotypes of each gene, including larval arrest, scrawny larvae, and germline defects, may result from N-/O-glycosylation inhibition as well as GPI-anchor inhibition
malfunction
Candida albicans BWP17
-
depletingCaGpi19p, an accessory subunit of the enzyme complex that initiates GPI biosynthesis, specifically down-regulates ERG11, altering ergosterol levels and drug response. ERG11 down-regulation is not due to general cell wall defects or GPI deficiency. CaGPI19 mutants show increased cAMP/PKA signalling
-
physiological function
-
Dscr5 functionally interacts with Knypek/Glypican 4 and is required for its localization at the cell surface, Dscr5 interacts with the planar cell polarity pathway in convergent extension movements
physiological function
-
the enzyme is part of the enzyme complex that initiates glycosylphosphatidylinositol, GPI, biosynthesis, it catalyzes the first step of GPI anchor biosynthesis. CaGPI19 appears to be mutually regulated with ERG11
physiological function
-
the phosphatidylinositol N-acetylglucosaminyltransferase complex catalyzes the first step of GPI-anchor syn­thesis, which is indispensable for the germline development of the nematode Caenorhabditis elegans. GPI-anchor synthesis is indispens­able for the maintenance of mitotic germline cell number
physiological function
Candida albicans BWP17
-
the enzyme is part of the enzyme complex that initiates glycosylphosphatidylinositol, GPI, biosynthesis, it catalyzes the first step of GPI anchor biosynthesis. CaGPI19 appears to be mutually regulated with ERG11
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
in alpha1-6 linkage
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
in alpha1-6 linkage
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
substrate specificity, enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Saccharomyces cerevisiae XM37-10c
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Saccharomyces cerevisiae XM37-10c
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
additional information
?
-
-
-
-
-
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
-
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
-
additional information
?
-
-
enzyme defect in paroxysmal nocturnal hemoglobinuria
-
-
-
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
-
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
-
additional information
?
-
-
glycosylphosphatidylinositol anchoring is essential for transport of cell surface proteins and enzyme deficieny leads to defective cell wall synthesis and cell death
-
-
-
additional information
?
-
Saccharomyces cerevisiae XM37-10c
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Q9BRB3
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
P57054, Q9BRB3
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Q9QYT7
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Q9JHG1
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
show the reaction diagram
Saccharomyces cerevisiae XM37-10c
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
additional information
?
-
P57054, Q9BRB3
-
-
-
-
additional information
?
-
Q9BRB3
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
Q9QYT7
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
-
additional information
?
-
P57054, Q9BRB3
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
-
additional information
?
-
Q9JHG1
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
-
additional information
?
-
-
enzyme defect in paroxysmal nocturnal hemoglobinuria
-
-
-
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
-
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
-
additional information
?
-
-
glycosylphosphatidylinositol anchoring is essential for transport of cell surface proteins and enzyme deficieny leads to defective cell wall synthesis and cell death
-
-
-
additional information
?
-
Saccharomyces cerevisiae XM37-10c
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activates
K+
-
activates
Mg2+
-
activates
Mn2+
-
activates
additional information
-
requires cations for activity, such as Mn2+, Mg2+, K+ or Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
binding site is close or at the active site, UDP-N-acetyl-D-glucosamine protects; strong
p-Chloromercuriphenylsulfonic acid
-
-
SH-alkylating reagents
-
-
-
iodoacetic acid
-
-
additional information
-
GTP-bound Ras2 protein associates in vivo with enzyme complex and inhibits its activity. Ras2 associates with enzyme complex subunit Eri1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
component 2 of dolichyl-phosphate-mannose synthase
DPM2 protein binds directly to the enzyme complex and enhances the enzyme activity, regulatory role; i.e. DPM2
-
additional information
-
no activation by Triton X-100 or Triton X-114
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
overexpression of active froms of the Ras family of proteins does not affect glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
assay at; assay at
7.4
-
assay at
7.4
assay at; assay at; assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
37
-
assay at
37
assay at
37
assay at; assay at
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CHO-K1 cell lines G9PLAP and mutant G9PLAP.85
Manually annotated by BRENDA team
-
5th instar larvae
Manually annotated by BRENDA team
-
with paroxysmal nocturnal hemoglobinuria phenotype, i.e. PNH, obtained by Epstein-Barr immortalization of lymphocytes from PNH-patients
Manually annotated by BRENDA team
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BW514.3 thymoma cell line
Manually annotated by BRENDA team
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of the 5th instar larvae
Manually annotated by BRENDA team
additional information
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the wild-type PIGA-1 protein is solely detected in the germline, and no EGFP-tagged PIGA-1 is detected in so­matic cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization; enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
638131
additional information
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638131
additional information
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enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
638132
additional information
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
638132
additional information
; enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H; enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
638134
additional information
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
638134
additional information
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enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
638135
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
structure of enzyme complex, overview; structure of enzyme complex, overview
additional information
structure of enzyme complex, overview
additional information
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topological model of the enzyme complex
additional information
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GTP-bound Ras2 protein associates in vivo with enzyme complex and inhibits its activity
additional information
the six other components of glycosylphosphatidylinositol-N-acetylglucosaminyltransferase can form a complex without PIG-Y, but this complex does not have any detectable glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity. In PIG-A-deficient JY5 cells, PIG-Y is not coprecipitated with any other components. PIG-Y associates directly with PIG-A and indirectly with other components through the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex. Additionally, there is no detectable association between PIG-Y and any of Ras proteins
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity purified
purification of GPI1 by overexpression of PIG-A in JY5 cells and isolation of the complex by affinity chromatography; purification of GPI1 by overexpression of PIG-A in JY5 cells and isolation of the complex by affinity chromatography
recombinant FLAG-tagged and His-tagged PIG-A from human B lymphoblastoid JY5 cells and from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha
genes involved in GPI-anchor synthesis in Caenorhabditis elegans, overview. Isolation and analysis of piga-1-knockout allele tm2939
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expressed in Daudi cells. Daudi cells have no PIG-Y transcritpt. PIG-Y cDNA restores the surface expression of CD59, DAF and CD48, but an empty vector does not. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity is also restored; expressed in HeLa cells; in chinese hamster ovary cells
expression of FLAG-tagged and His-tagged PIG-A in PIG-A-deficient human B lymphoblastoid JY5 cells and in Escherichia coli, complementation in JY5 cells
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expression of PIG-P in enzyme deficient mouse mutant T cell line can complement and restore the enzyme activity; overexpression of FLAG- and GST-double tagged PIG-A in human B lymphoblastoid JY5 cells
hGPI1, DNA sequence determination, coexpression as GST-tagged protein in human B lymphoblastoid JY25 or JY5 cells with the other three GST- or FLAG-tagged protein of the active protein complex
coexpression of FLAG-tagged PIG-C, GST-tagged PIG-A and PIG-H with and without mGPI1 in the mGPI1-deficient F9 cells; mGPI1, DNA sequence determination, expression in embryonal carcinoma F9 cells
expression of PIG-A/GPI3 and PIG-C/GPI2 as FLAG-tagged fusion proteins in yeast, expression of FLAG-tagged PIG-A/GPI3 in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulation of ERG11 downregulates CaGPI19 and GPI biosynthesis
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downregulation of ERG11 downregulates CaGPI19 and GPI biosynthesis
Candida albicans BWP17
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
afpig-a null mutant, strain CEA17 (pyrG-). This mutant shows a complete loss in glycosylphosphatidylinositol-N-acetylglucoaminyltransferase activity. None of the membrane bound glycosylphosphatidylinositol-anchored phospholipases, phosphatase, eCM33por Gl1p is found in the membrane preparation of the mutant. The mutant can grow at temperatures from 30°C to 50°C, but the growth rates are greatly inhibited. When the mutant is grown in the presence of various cell wall-disrupting agents, it is more sensitive to Calcofluor white, Congo-red, Nikkomycin Z and SDS, than the wild type. The mannoproteins and beta-glucans in mycelial cell wall of the mutant is 2.5fold and 2fold of the wild type or revertant respectively. The deletion of the afpig-a gene leads to earlier polarity, germ tube emergence and septation of mutant conidiospores in the early duplication cycles and to significant changes in developmental events and morphogenesis during conidiation. Two virulence factors, mycelial catalase Cat1 and Asp-haemolysin, are missing in the mutant, but the chitinase ChiB is found remarkably increased. After the inoculation of wild-type and mutant conidia into immunocompromised mice, early mortality is nearly identical among all groups. The remaining mice receiving the deletion mutant survived significantly longer.
additional information
Aspergillus fumigatus YJ-407.
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afpig-a null mutant, strain CEA17 (pyrG-). This mutant shows a complete loss in glycosylphosphatidylinositol-N-acetylglucoaminyltransferase activity. None of the membrane bound glycosylphosphatidylinositol-anchored phospholipases, phosphatase, eCM33por Gl1p is found in the membrane preparation of the mutant. The mutant can grow at temperatures from 30°C to 50°C, but the growth rates are greatly inhibited. When the mutant is grown in the presence of various cell wall-disrupting agents, it is more sensitive to Calcofluor white, Congo-red, Nikkomycin Z and SDS, than the wild type. The mannoproteins and beta-glucans in mycelial cell wall of the mutant is 2.5fold and 2fold of the wild type or revertant respectively. The deletion of the afpig-a gene leads to earlier polarity, germ tube emergence and septation of mutant conidiospores in the early duplication cycles and to significant changes in developmental events and morphogenesis during conidiation. Two virulence factors, mycelial catalase Cat1 and Asp-haemolysin, are missing in the mutant, but the chitinase ChiB is found remarkably increased. After the inoculation of wild-type and mutant conidia into immunocompromised mice, early mortality is nearly identical among all groups. The remaining mice receiving the deletion mutant survived significantly longer.
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additional information
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the RNAi phenotypes of each gene, including larval arrest, scrawny larvae, and germline defects, may result from N-/O-glycosylation inhibition as well as GPI-anchor inhibition
additional information
disruption of the genes in F9 cells via homologous recombination, causing a severe but not complete defect in the generation of glycosylphosphatidylinositol-anchored proteins, highly reduced activity in vivo, no activity in vitro, decrease in GPI1 also caused decrease of PIG-C and PIG-H
additional information
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subunit eri1 deletion mutant, displays growth arrest at 37°C and cell wall defect at permissive temperature, defect is suppressed by increased UDP-GlcNAc levels. Mutant also accumulates chitin and is deficient in maturation of glucosamine phosphatidyl-inositol anchor proteins in the ER
additional information
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a gpi19 deletion allele that lacks nearly the entire coding sequence in the EG123 strain background confirmed the lethality of this mutation; a set of temperature-sensitive gpi19 allels is created using error-prone PCR. All of the gpi19 alleles, with the exception of gpi19-4, are osmotically remedial. The gpi19 mutants are hypersensitive to zymolyase treatment. The least severely impaired alleles of gpi19 (gpi19-1 and gpi19-2) are suppressed for their growth defects at restrictive temperature by either GFA1 overexpression or exogenous glucosamine. The gpi19 mutants display weak filamentation phenotypes and invasive growth, which is enhanced by the inclusion of sorbitol in the medium to suppress their growth defects.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein