Literature summary for 2.4.1.198 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.

Search for more literature for 2.4.1.198

Application

Application	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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.
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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

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

Substrates and Products (Substrate)

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

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