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Information on EC 2.1.1.317 - sphingolipid C9-methyltransferase
for references in articles please use BRENDA:EC2.1.1.317
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.317 sphingolipid C9-methyltransferase
IUBMB Comments
The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
sphingolipid c9-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase
The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
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
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Q2QJ12
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Q2QJ12
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
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
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Q2QJ12
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Q2QJ12
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Q2QJ12
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
evolution
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C-9-methylated glucosylceramides (GlcCers) are sphingolipids unique to fungi
evolution
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C-9-methylated glucosylceramides (GlcCers) are sphingolipids unique to fungi
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evolution
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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
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malfunction
Q2QJ12
a Pichia pastoris knock-out strain of the sphingolipid C9-methyltransferase lacks C9-methylated glucosylceramides
malfunction
-
the Candida albicans mts1 disruptant had a decreased hyphal growth rate compared to the wild-type strain. The mts1 disruptant grows similarly to wild-type in medium containing SDS or fluconazole. The membrane structure of the mts1 disruptant is not disturbed, mutant phenotype, overview
malfunction
-
the DELTAFgmt2 mutant exhibits severe growth defects and produces abnormal conidia, while the DELTAFgmt1 mutant grows like the wild-type strain. The DELTAFgmt2 mutant is less virulent on different host plants tested than the previously characterized DELTAFggcs1 mutant, which lacks GlcCer synthase activity and produces no GlcCer at all. Moreover, the DELTAFgmt1 and DELTAFgmt2 mutants retain sensitivity to the antifungal plant defensins MsDef1 and RsAFP2
malfunction
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DELTAsmt1 mutants lacking the sphingolipid C9 methyltransferase gene (SMT1) are attenuated in virulence and have a growth defect at 37 °C, in neutral/alkaline pH and 5 % CO2 environments
malfunction
Q5B192, Q5AWF5
increased levels of unmethylated glucosylceramide are observed in smtA mutants. DELTAsmtA and wild-type cells show a similar 9-methyl-glucosylceramide content
malfunction
Q5B192, Q5AWF5
increased levels of unmethylated glucosylceramide are observed in smtB mutants. DELTAsmtB cells show activity reduced by 50%. The compromised 9-methyl-glucosylceramide production in the DELTAsmtB strain is not accompanied by reduced filamentation or defects in cell polarity
malfunction
-
the DELTAFgmt2 mutant exhibits severe growth defects and produces abnormal conidia, while the DELTAFgmt1 mutant grows like the wild-type strain. The DELTAFgmt2 mutant is less virulent on different host plants tested than the previously characterized DELTAFggcs1 mutant, which lacks GlcCer synthase activity and produces no GlcCer at all. Moreover, the DELTAFgmt1 and DELTAFgmt2 mutants retain sensitivity to the antifungal plant defensins MsDef1 and RsAFP2
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malfunction
-
a Pichia pastoris knock-out strain of the sphingolipid C9-methyltransferase lacks C9-methylated glucosylceramides
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metabolism
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the enzyme is part of the C-9-methylated glucosylceramides biosynthesis pathway, overview
metabolism
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the enzyme is part of the C-9-methylated glucosylceramides biosynthesis pathway, overview
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physiological function
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C9-methylated glucosylceramide is a fungus-specific sphingolipid. This lipid is a major membrane component in the cell and is thought to play important roles in the growth and virulence of several fungal species. The enzyme is involved in hyphal elongation. The C9-methyl group of a long-chain base in glucosylceramides plays an important role in the hyphal elongation of Candida albicans independent of lipid membrane disruption
physiological function
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sphingolipid C-9 methyltransferases seem to be essential in the organism, they are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Isozyme FgMT2 encodes a sphingolipid C-9 methyltransferase that is capable of methylating C-9-methylated glucosylceramides in the absence of the FgMT1-encoded enzyme and that isozyme FgMT2 is the predominant sphingolipid C-9 methyltransferases for methylating C-9-methylated glucosylceramides
physiological function
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the enzyme adds a methyl group to position nine of the sphingosine backbone of ceramide. The sphingolipid glucosylceramide and factors involved in the fungal GlcCer pathways are an integral part of fungal virulence, especially in fungal replication at 37 °C, in neutral/alkaline pH and 5 % CO2 environments (e.g. alveolar spaces)
physiological function
-
sphingolipid C-9 methyltransferases seem to be essential in the organism, they are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Isozyme FgMT2 encodes a sphingolipid C-9 methyltransferase that is capable of methylating C-9-methylated glucosylceramides in the absence of the FgMT1-encoded enzyme and that isozyme FgMT2 is the predominant sphingolipid C-9 methyltransferases for methylating C-9-methylated glucosylceramides
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additional information
Q2QJ12
analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
additional information
-
analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
additional information
-
the C-9 methyl group is not a critical structural feature of the GlcCer receptor required for the antifungal action of plant defensins
additional information
-
the C-9 methyl group is not a critical structural feature of the GlcCer receptor required for the antifungal action of plant defensins
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additional information
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analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
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Show AA Sequence and Transmembrane Helices (2037 entries)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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construction of a mts1 disruptant mutant strain MTS105 that lacks (E,E)-9-methylsphinga-4,8-dienine in its glucosylceramides and contains (E)-sphing-4-enine and (E,E)-sphinga-4,8-dienine. Reintroducing the MTS1 gene into the mts1 disruptant restores the synthesis of (E,E)-9-methylsphinga-4,8-dienine in the glucosylceramides
additional information
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construction of enzyme knockout mutants of genes FgMT1 and FgMT2 by gene replacements, penotypes, overview. The DELTAFgmt1 mutant produces C-9-methylated GlcCer like the wild-type strain, whereas the DELTAFgmt2 mutant produces 65 to 75% nonmethylated and 25 to 35% methylated GlcCer. No DELTAFgmt1DELTAFgmt2 double-knockout mutant producing only nonmethylated GlcCer can be recovered,. The DELTAFgmt2 mutant exhibits drastically reduced disease symptoms when expressed in Triticum aestivum and much-delayed disease symptoms when expressed in Arabidopsis thaliana
additional information
-
construction of enzyme knockout mutants of genes FgMT1 and FgMT2 by gene replacements, penotypes, overview. The DELTAFgmt1 mutant produces C-9-methylated GlcCer like the wild-type strain, whereas the DELTAFgmt2 mutant produces 65 to 75% nonmethylated and 25 to 35% methylated GlcCer. No DELTAFgmt1DELTAFgmt2 double-knockout mutant producing only nonmethylated GlcCer can be recovered,. The DELTAFgmt2 mutant exhibits drastically reduced disease symptoms when expressed in Triticum aestivum and much-delayed disease symptoms when expressed in Arabidopsis thaliana
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additional information
Q2QJ12
construction of a Pichia pastoris knock-out strain lacking sphingolipid C9-methyltransferase, the strain contains only non-methylated glucosylceramides
additional information
-
construction of a Pichia pastoris knock-out strain lacking sphingolipid C9-methyltransferase, the strain contains only non-methylated glucosylceramides
additional information
-
construction of a Pichia pastoris knock-out strain lacking sphingolipid C9-methyltransferase, the strain contains only non-methylated glucosylceramides
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Q2QJ12
genes FgMT1 and FgMT2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in and complementation of an enzyme knockout mutant strain C-9-MT-null of Pichia pastoris
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramamoorthy, V.; Cahoon, E.; Thokala, M.; Kaur, J.; Li, J.; Shah, D.
Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum
Eukaryot. Cell
8
217-229
2009
Fusarium graminearum, Fusarium graminearum PH-1
brenda
Ternes, P.; Sperling, P.; Albrecht, S.; Franke, S.; Cregg, J.M.; Warnecke, D.; Heinz, E.
Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling
J. Biol. Chem.
281
5582-5592
2006
Komagataella pastoris (Q2QJ12), Komagataella pastoris, Komagataella pastoris GS115 (Q2QJ12)
brenda
Oura, T.; Kajiwara, S.
Candida albicans sphingolipid C9-methyltransferase is involved in hyphal elongation
Microbiology
156
1234-1243
2010
Candida albicans
brenda
Singh, A.; Rella, A.; Schwacke, J.; Vacchi-Suzzi, C.; Luberto, C.; Del Poeta, M.
Transmembrane transporter expression regulated by the glucosylceramide pathway in Cryptococcus neoformans
BMC Res. Notes
8
861
2015
Cryptococcus neoformans
brenda
Fernandes, C.; de Castro, P.; Singh, A.; Fonseca, F.; Pereira, M.; Vila, T.; Atella, G.; Rozental, S.; Savoldi, M.; Del Poeta, M.; Goldman, G.; Kurtenbach, E.
Functional characterization of the Aspergillus nidulans glucosylceramide pathway reveals that LCB DELTA8-desaturation and C9-methylation are relevant to filamentous growth, lipid raft localization and Psd1 defensin activity
Mol. Microbiol.
102
488-505
2016
Aspergillus nidulans (Q5B192), Aspergillus nidulans (Q5AWF5)
brenda
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