C9MT2_GIBZE
ID C9MT2_GIBZE Reviewed; 521 AA.
AC I1RNL0; A0A0E0SN67;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Sphingolipid C9-methyltransferase 2 {ECO:0000303|PubMed:19028992};
DE Short=C-9-MT2 {ECO:0000303|PubMed:19028992};
DE EC=2.1.1.317 {ECO:0000269|PubMed:19028992};
GN Name=MT2 {ECO:0000303|PubMed:19028992}; ORFNames=FGRRES_05593, FGSG_05593;
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 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. However, C-9
CC methylation of GlcCers is not essential for the sensitivity of
CC 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: Produces 65 to 75% nonmethylated and 25 to 35%
CC methylated GlcCers. Exhibits severe growth defects and produces
CC abnormal conidia. Also exhibits drastically reduced disease symptoms in
CC wheat and much-delayed disease symptoms in Arabidopsis thaliana. A
CC double-knockout with its paralog MT1 is not viable.
CC {ECO:0000269|PubMed:19028992}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; DS231665; ESU11573.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF87880.1; -; Genomic_DNA.
DR RefSeq; XP_011324149.1; XM_011325847.1.
DR AlphaFoldDB; I1RNL0; -.
DR SMR; I1RNL0; -.
DR STRING; 5518.FGSG_05593P0; -.
DR PRIDE; I1RNL0; -.
DR EnsemblFungi; ESU11573; ESU11573; FGSG_05593.
DR GeneID; 23552770; -.
DR KEGG; fgr:FGSG_05593; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18285; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR InParanoid; I1RNL0; -.
DR UniPathway; UPA00222; -.
DR PHI-base; PHI:2409; -.
DR Proteomes; UP000070720; Chromosome 3.
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..521
FT /note="Sphingolipid C9-methyltransferase 2"
FT /id="PRO_0000434801"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 225..226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 262..270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 288..293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 318..319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
SQ SEQUENCE 521 AA; 59853 MW; 20CACB24727E394F CRC64;
MAEKSGVTGL DFEFVKTPAF PKPDFDKLEN VGVPTTRYPA IKNAPLPADG SGSDTFNNYV
LISILTIVPW WLSWKVGGGF KTTLFFAIIV DLPMLAAWWL TISAISPRKN EKVRLPNRGV
EHYLEFKKEA DRAKYRGTNK IPMETFYEMY FDGDVDFKGD CLEVMEQRHD WVSFRFTIGL
IKFFLFGMMP EVIMHTRSQD EEQVRDHYDR GDDFYGWFLG PRMIYTSGII SDINREETLE
ELQDNKLTVV CEKIGLTKGD SMLDIGCGWG TLARFASEQY GANVTGVTLG RNQTAWGNSS
MRKVGIPEEQ SRIVCKDYRD IPVPVGGYKK ITSLEMSEHV GIRHFSSFLK QVHDMLDDDG
VFFLQYAGIR KAWQYEDLTW GLFMNKYIFP GADASTPLGW VVDKLEGTGF EIKHIDTIGV
HYSATLWRWY RNWMDNRDKV EAKYGKRWFR IWEFFLAYST IISRQGSATC FQITMVKNIN
STHRIDGVET QFNLHGALDN CRADLQSWAA KNNVKTPSEL L
