C9MT1_GIBZE
ID C9MT1_GIBZE Reviewed; 513 AA.
AC I1RJD6; A0A098DK74; A0A0E0S5T2;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Sphingolipid C9-methyltransferase 1 {ECO:0000303|PubMed:19028992};
DE Short=C-9-MT1 {ECO:0000303|PubMed:19028992};
DE EC=2.1.1.317 {ECO:0000269|PubMed:19028992};
GN Name=MT1 {ECO:0000303|PubMed:19028992}; ORFNames=FGRRES_03951, FGSG_03951;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
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 the growth, differentiation
CC and pathogenicity. The methyl group at the C9-position distinguishes
CC fungal glucosylceramides from those of plants and animals, and may thus
CC play a role in host-pathogen interactions enabling the host to
CC recognize the fungal attack and initiate specific defense responses.
CC However, C-9 methylation of GlcCers is not essential for the
CC sensitivity of F.graminearum to plant defensins MsDef1 and RsAFP2.
CC {ECO:0000269|PubMed:19028992}.
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:19028992};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:19028992}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:C4R7Z3}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: In contrast to the knockout of its paralog MT2,
CC has no effect on methylation of GluCers and exhibits no growth defects.
CC However, a double-knockout with its paralog MT2 is not viable.
CC {ECO:0000269|PubMed:19028992}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; DS231664; ESU09214.1; -; Genomic_DNA.
DR EMBL; HG970333; CEF78857.1; -; Genomic_DNA.
DR RefSeq; XP_011321713.1; XM_011323411.1.
DR AlphaFoldDB; I1RJD6; -.
DR SMR; I1RJD6; -.
DR STRING; 229533.I1RJD6; -.
DR EnsemblFungi; ESU09214; ESU09214; FGSG_03951.
DR GeneID; 23551227; -.
DR KEGG; fgr:FGSG_03951; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G14109; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR InParanoid; I1RJD6; -.
DR UniPathway; UPA00222; -.
DR PHI-base; PHI:2408; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Sphingolipid C9-methyltransferase 1"
FT /id="PRO_0000434800"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 228..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 265..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 291..296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 321..322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
SQ SEQUENCE 513 AA; 58009 MW; 4B769EEB92E6E1B4 CRC64;
MAIKQNGRAH LSSDIDFIRT PEAPVDSLST GKNPGVPSTN SPAIKNAPLP ADGPGYEQWS
NGFLVAALLG IPQWLSWKLG GGLKTAIFLS IFTTIPVLAV IWTVMSRYSP RINHDVKLPG
RPVEFYLTFK SDSHRARWTG THKIPMATFF ELYFTGQVDL NGDALEVFEY RHDWATFNFT
SETFRYILFT FFPDVVLHLR SQDEEQVRTN YDSGNDHYAW FLGPRMIYTS GIISDPTREE
TLEEMQDNKL AIVCEKISLK EGDTLLDIGC GWGTLAKFAS LNYGAKVTGV TLARNQVQWG
NDGLQQAGIP EEQSRLLCCD YRDIPEDQKF NKITQLEMAE HVGVRRLTGF FRQCYDMLEN
DGSMYVQVSG FRKAWQYEDF IWGLFLNKYI FPGADASTPL SYYVGCLESA GFEVKSVDTI
GVHYSGTLWR WYRNWLGNAD KVKAKYGVRW FRIWEIFLAY STIGSRQGSA TCYQIVVVKN
LNSNHRIDGV YSQYGLHGAL AAAKAAGKNM LPK
