Literature summary for 2.1.1.317 extracted from

Ternes, P.; Sperling, P.; Albrecht, S.; Franke, S.; Cregg, J.M.; Warnecke, D.; Heinz, E.
Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling (2006), J. Biol. Chem., 281, 5582-5592.

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Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic tree, recombinant enzyme functional expression in a Saccharomyces cerevisiae strain that is engineered to produce glucosylceramides suitable as a substrate for C9-methylation. C9-methylated sphingolipids are detected in the transformed strain expressing the candidate from Pichia pastoris, demonstrating its function as a sphingolipid C9-methyltransferase	Komagataella pastoris

Cloned (Comment)

Organism

DNA and amino acid sequence determination and analysis, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic tree, recombinant enzyme functional expression in a Saccharomyces cerevisiae strain that is engineered to produce glucosylceramides suitable as a substrate for C9-methylation. C9-methylated sphingolipids are detected in the transformed strain expressing the candidate from Pichia pastoris, demonstrating its function as a sphingolipid C9-methyltransferase

Komagataella pastoris

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a Pichia pastoris knock-out strain lacking sphingolipid C9-methyltransferase, the strain contains only non-methylated glucosylceramides	Komagataella pastoris

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	membrane-bound	Komagataella pastoris	16020	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide	Komagataella pastoris	-	S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide	-	?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide	Komagataella pastoris GS115	-	S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide	-	?

Organism

Organism	UniProt	Comment	Textmining
Komagataella pastoris	Q2QJ12	i.e. Pichia pastoris	-
Komagataella pastoris GS115	Q2QJ12	i.e. Pichia pastoris	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide	-	Komagataella pastoris	S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide	-	?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide	-	Komagataella pastoris GS115	S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide	-	?

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Komagataella pastoris

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the superfamily of S-adenosylmethionine-dependent methyltransferases and shows highest sequence similarity to plant and bacterial cyclopropane fatty acid synthases, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic profiling of SAM-dependent methyltransferases, overview	Komagataella pastoris
malfunction	a Pichia pastoris knock-out strain of the sphingolipid C9-methyltransferase lacks C9-methylated glucosylceramides	Komagataella pastoris
additional information	analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme	Komagataella pastoris