Literature summary for 2.3.1.1 extracted from

Xu, Y.; Glansdorff, N.; Labedan, B.
Bioinformatic analysis of an unusual gene-enzyme relationship in the arginine biosynthetic pathway among marine gamma proteobacteria: implications concerning the formation of N-acetylated intermediates in prokaryotes (2006), BMC Genomics, 7, 4.

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Organism

Organism	UniProt	Comment	Textmining
Aliivibrio fischeri	-	-	-
Colwellia psychrerythraea	-	-	-
Idiomarina loihiensis	-	-	-
Moritella abyssi	-	-	-
Moritella profunda	-	-	-
Pseudoalteromonas haloplanktis	-	-	-
Vibrio parahaemolyticus	-	-	-
Vibrio vulnificus	-	-	-

Synonyms

Synonyms	Comment	Organism
ArgA	-	Idiomarina loihiensis
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Aliivibrio fischeri
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Moritella profunda
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Moritella abyssi
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Pseudoalteromonas haloplanktis
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Vibrio vulnificus
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Idiomarina loihiensis
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fusedto a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Vibrio parahaemolyticus
ArgH(A)	acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fusedto a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli	Colwellia psychrerythraea

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Release 2023.1 (January 2023)