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Literature summary extracted from

  • Oswal, N.; Sahni, N.S.; Bhattacharya, A.; Komath, S.S.; Muthuswami, R.
    Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family (2008), BMC Evol. Biol., 8, 168.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.4.1.198 analysis 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 Methanosarcina barkeri
2.4.1.198 analysis 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 Drosophila melanogaster
2.4.1.198 analysis 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 Homo sapiens
2.4.1.198 analysis 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 Rattus norvegicus
2.4.1.198 analysis 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 Saccharomyces cerevisiae
2.4.1.198 analysis 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 Methanothermobacter thermautotrophicus
2.4.1.198 analysis 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 Cryptosporidium parvum
2.4.1.198 analysis 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 Arabidopsis thaliana
2.4.1.198 analysis 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 Pyrococcus furiosus
2.4.1.198 analysis 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 Giardia intestinalis
2.4.1.198 analysis 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 Entamoeba histolytica
2.4.1.198 analysis 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 Trypanosoma brucei
2.4.1.198 analysis 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 Dictyostelium discoideum
2.4.1.198 analysis 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 Thermoplasma acidophilum
2.4.1.198 analysis 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 Schizosaccharomyces pombe
2.4.1.198 analysis 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 Caenorhabditis elegans
2.4.1.198 analysis 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 Mycobacterium sp.
2.4.1.198 analysis 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 Candida albicans
2.4.1.198 analysis 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 Plasmodium falciparum
2.4.1.198 analysis 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 Oryza sativa
2.4.1.198 analysis 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 Clostridium tetani
2.4.1.198 analysis 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 Clostridium beijerinckii
2.4.1.198 analysis 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 Leishmania major
2.4.1.198 analysis 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 Bacteroides thetaiotaomicron
2.4.1.198 analysis 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 Paramecium tetraurelia
2.4.1.198 analysis 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 Cutibacterium acnes
2.4.1.198 analysis 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 Halalkalibacterium halodurans
2.4.1.198 analysis 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 Desulfitobacterium hafniense
2.4.1.198 analysis 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 Aeropyrum pernix
2.4.1.198 analysis 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 Methanosarcina acetivorans
2.4.1.198 analysis 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 Actinobacillus succinogenes
2.4.1.198 analysis 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 [Mannheimia] succiniciproducens
2.4.1.198 analysis 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 Alkaliphilus metalliredigens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.198 Actinobacillus succinogenes
-
-
-
2.4.1.198 Aeropyrum pernix
-
-
-
2.4.1.198 Alkaliphilus metalliredigens
-
-
-
2.4.1.198 Arabidopsis thaliana
-
-
-
2.4.1.198 Bacteroides thetaiotaomicron
-
-
-
2.4.1.198 Caenorhabditis elegans
-
-
-
2.4.1.198 Candida albicans
-
-
-
2.4.1.198 Clostridium beijerinckii
-
-
-
2.4.1.198 Clostridium tetani
-
-
-
2.4.1.198 Cryptosporidium parvum
-
-
-
2.4.1.198 Cutibacterium acnes
-
-
-
2.4.1.198 Desulfitobacterium hafniense
-
-
-
2.4.1.198 Dictyostelium discoideum
-
-
-
2.4.1.198 Drosophila melanogaster
-
-
-
2.4.1.198 Entamoeba histolytica
-
-
-
2.4.1.198 Giardia intestinalis
-
-
-
2.4.1.198 Halalkalibacterium halodurans
-
-
-
2.4.1.198 Homo sapiens
-
-
-
2.4.1.198 Leishmania major
-
-
-
2.4.1.198 Methanosarcina acetivorans
-
-
-
2.4.1.198 Methanosarcina barkeri
-
-
-
2.4.1.198 Methanothermobacter thermautotrophicus
-
-
-
2.4.1.198 Mycobacterium sp.
-
-
-
2.4.1.198 Oryza sativa
-
-
-
2.4.1.198 Paramecium tetraurelia
-
-
-
2.4.1.198 Plasmodium falciparum
-
-
-
2.4.1.198 Pyrococcus furiosus
-
-
-
2.4.1.198 Rattus norvegicus
-
-
-
2.4.1.198 Saccharomyces cerevisiae
-
-
-
2.4.1.198 Schizosaccharomyces pombe
-
-
-
2.4.1.198 Thermoplasma acidophilum
-
-
-
2.4.1.198 Trypanosoma brucei
-
-
-
2.4.1.198 [Mannheimia] succiniciproducens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Methanosarcina barkeri UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Drosophila melanogaster UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Homo sapiens UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Rattus norvegicus UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Saccharomyces cerevisiae UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Methanothermobacter thermautotrophicus UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Cryptosporidium parvum UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Arabidopsis thaliana UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Pyrococcus furiosus UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Giardia intestinalis UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Entamoeba histolytica UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Trypanosoma brucei UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Dictyostelium discoideum UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Thermoplasma acidophilum UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Schizosaccharomyces pombe UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Caenorhabditis elegans UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Mycobacterium sp. UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Candida albicans UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Plasmodium falciparum UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Oryza sativa UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Clostridium tetani UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Clostridium beijerinckii UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Leishmania major UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Bacteroides thetaiotaomicron UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Paramecium tetraurelia UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Cutibacterium acnes UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Halalkalibacterium halodurans UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Desulfitobacterium hafniense UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Aeropyrum pernix UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Methanosarcina acetivorans UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Actinobacillus succinogenes UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
[Mannheimia] succiniciproducens UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?
2.4.1.198 UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
-
Alkaliphilus metalliredigens UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.198 PIG-A
-
Methanosarcina barkeri
2.4.1.198 PIG-A
-
Drosophila melanogaster
2.4.1.198 PIG-A
-
Homo sapiens
2.4.1.198 PIG-A
-
Rattus norvegicus
2.4.1.198 PIG-A
-
Saccharomyces cerevisiae
2.4.1.198 PIG-A
-
Methanothermobacter thermautotrophicus
2.4.1.198 PIG-A
-
Cryptosporidium parvum
2.4.1.198 PIG-A
-
Arabidopsis thaliana
2.4.1.198 PIG-A
-
Pyrococcus furiosus
2.4.1.198 PIG-A
-
Giardia intestinalis
2.4.1.198 PIG-A
-
Entamoeba histolytica
2.4.1.198 PIG-A
-
Trypanosoma brucei
2.4.1.198 PIG-A
-
Dictyostelium discoideum
2.4.1.198 PIG-A
-
Thermoplasma acidophilum
2.4.1.198 PIG-A
-
Schizosaccharomyces pombe
2.4.1.198 PIG-A
-
Caenorhabditis elegans
2.4.1.198 PIG-A
-
Mycobacterium sp.
2.4.1.198 PIG-A
-
Candida albicans
2.4.1.198 PIG-A
-
Plasmodium falciparum
2.4.1.198 PIG-A
-
Oryza sativa
2.4.1.198 PIG-A
-
Clostridium tetani
2.4.1.198 PIG-A
-
Clostridium beijerinckii
2.4.1.198 PIG-A
-
Leishmania major
2.4.1.198 PIG-A
-
Bacteroides thetaiotaomicron
2.4.1.198 PIG-A
-
Paramecium tetraurelia
2.4.1.198 PIG-A
-
Cutibacterium acnes
2.4.1.198 PIG-A
-
Halalkalibacterium halodurans
2.4.1.198 PIG-A
-
Desulfitobacterium hafniense
2.4.1.198 PIG-A
-
Aeropyrum pernix
2.4.1.198 PIG-A
-
Methanosarcina acetivorans
2.4.1.198 PIG-A
-
Actinobacillus succinogenes
2.4.1.198 PIG-A
-
[Mannheimia] succiniciproducens
2.4.1.198 PIG-A
-
Alkaliphilus metalliredigens