ID C9MT_KOMPG Reviewed; 489 AA.
AC C4R7Z3; Q2QJ12;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Sphingolipid C9-methyltransferase {ECO:0000303|PubMed:16339149};
DE Short=C-9-MT;
DE EC=2.1.1.317 {ECO:0000269|PubMed:16339149};
GN OrderedLocusNames=PAS_chr4_0465;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=16339149; DOI=10.1074/jbc.m512864200;
RA Ternes P., Sperling P., Albrecht S., Franke S., Cregg J.M., Warnecke D.,
RA Heinz E.;
RT "Identification of fungal sphingolipid C9-methyltransferases by
RT phylogenetic profiling.";
RL J. Biol. Chem. 281:5582-5592(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=19028992; DOI=10.1128/ec.00255-08;
RA Ramamoorthy V., Cahoon E.B., Thokala M., Kaur J., Li J., Shah D.M.;
RT "Sphingolipid C-9 methyltransferases are important for growth and virulence
RT but not for sensitivity to antifungal plant defensins in Fusarium
RT graminearum.";
RL Eukaryot. Cell 8:217-229(2009).
CC -!- FUNCTION: Catalyzes methylation of the sphingoid base component of
CC glucosylceramides (GluCers) at the C9-position. Sphingolipid C9-
CC methylation requires 4,8-desaturated ceramides as substrates.
CC Glucosylceramides play important roles in growth, differentiation and
CC pathogenicity. The methyl group at the C9-position distinguishes fungal
CC glucosylceramides from those of plants and animals, and may thus play a
CC role in host-pathogen interactions enabling the host to recognize the
CC fungal attack and initiate specific defense responses.
CC {ECO:0000269|PubMed:16339149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (4E,8E)-4-sphinga-4,8-dienine ceramide + S-adenosyl-L-
CC methionine = a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85953,
CC ChEBI:CHEBI:87033; EC=2.1.1.317;
CC Evidence={ECO:0000269|PubMed:16339149};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:16339149}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16339149}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Produces only non-methylated glucosylceramides
CC (PubMed:16339149). Shows no alteration of growth and no increase in the
CC level of resistance to plant defensins MsDef1 and RsAFP2
CC (PubMed:19028992). {ECO:0000269|PubMed:16339149,
CC ECO:0000269|PubMed:19028992}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; DQ070247; AAZ08581.1; -; Genomic_DNA.
DR EMBL; FN392322; CAY71718.1; -; Genomic_DNA.
DR RefSeq; XP_002493897.1; XM_002493852.1.
DR AlphaFoldDB; C4R7Z3; -.
DR SMR; C4R7Z3; -.
DR STRING; 644223.C4R7Z3; -.
DR EnsemblFungi; CAY71718; CAY71718; PAS_chr4_0465.
DR GeneID; 8201413; -.
DR KEGG; ppa:PAS_chr4_0465; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR InParanoid; C4R7Z3; -.
DR OMA; GFKTWLF; -.
DR OrthoDB; 5484439at2759; -.
DR BioCyc; MetaCyc:MONOMER-19158; -.
DR BRENDA; 2.1.1.317; 4827.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000314; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR45197:SF1; SPHINGOLIPID C9-METHYLTRANSFERASE A-RELATED; 1.
DR PANTHER; PTHR45197; SYNTHASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04190)-RELATED; 1.
DR Pfam; PF02353; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..489
FT /note="Sphingolipid C9-methyltransferase"
FT /id="PRO_0000434798"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 202..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 239..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 265..270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 295..296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
SQ SEQUENCE 489 AA; 56272 MW; 8A2844BE892FC7C2 CRC64;
MSQTESTKGV KITNYAAIKN APLPADGPGA KNFSNWLLLG LLTGVPLFVT RKFHGGLKTF
IFFFILFAIP ILMAYWTVLS SYSPRLNEKV QFPNRGVEHY LKFHDDQLAA RYQGQNKIPM
ETFHELYFEG KVSFKGDALD ALEYRHDWAS FRFTLSLFRF FLLGMIPEVI MHSRSQDEEQ
VRDHYDRGDD FYSWFLGDRM VYTSGLISDV NKDESLEELQ DNKLKTVCEK IQLKEGEYLL
DLGCGWGTLA AFASSQYGAK VTGITLGKNQ TKYGNDKIAS FGVDEKQSRI LCHDYRDTPL
PKDENGNTTK YDKITCLEMA EHVGVRKFRS FLQQVYDMLD DDGVFFLQYA GLRKSWQYED
LIWGLFMNKY IFPGADASTP LDFVVSALEA TGFETVSIDN IGVHYSATLY RWYKNWLSNR
DNVVNKYGIK WFKIWEYFLA SSTIISRQGS ATCYQIVLRK NLNSYDRAGY ISTQEGLQGP
ISRKTDWVK
//
