GT2_GIBZE
ID GT2_GIBZE Reviewed; 526 AA.
AC I1RB03;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Type 2 glycosyltransferase {ECO:0000303|PubMed:29020037};
DE EC=2.4.1.- {ECO:0000305|PubMed:29020037};
GN Name=GT2 {ECO:0000303|PubMed:29020037};
GN ORFNames=FG00702, FGRAMPH1_01T01771;
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, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29020037; DOI=10.1371/journal.ppat.1006672;
RA King R., Urban M., Lauder R.P., Hawkins N., Evans M., Plummer A.,
RA Halsey K., Lovegrove A., Hammond-Kosack K., Rudd J.J.;
RT "A conserved fungal glycosyltransferase facilitates pathogenesis of plants
RT by enabling hyphal growth on solid surfaces.";
RL PLoS Pathog. 13:E1006672-E1006672(2017).
CC -!- FUNCTION: Glycosyltransferase involved in the maintenance of the
CC outermost surface of the fungal cell wall (PubMed:29020037). Likely
CC functions in the synthesis of a currently unknown, potentially minor
CC but widespread, extracellular or outer cell wall polysaccharide which
CC plays a key role in facilitating many interactions between plants and
CC fungi by enabling hyphal growth on solid matrices (PubMed:29020037).
CC {ECO:0000269|PubMed:29020037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Secreted, cell wall
CC {ECO:0000269|PubMed:29020037}.
CC -!- INDUCTION: Expression is induced during hyphal growth.
CC {ECO:0000269|PubMed:29020037}.
CC -!- DISRUPTION PHENOTYPE: Severely impairs hyphal growth and pathogenicity
CC on wheat leaves (PubMed:29020037). Does not affect adhesion to leaf
CC surfaces (PubMed:29020037). Leads to constitutive overexpression of
CC several transmembrane and secreted proteins, including an important
CC LysM-domain chitin-binding virulence effector, LysM (PubMed:29020037).
CC {ECO:0000269|PubMed:29020037}.
CC -!- SIMILARITY: Belongs to the GT2 glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HG970332; CEF72686.1; -; Genomic_DNA.
DR RefSeq; XP_011316405.1; XM_011318103.1.
DR AlphaFoldDB; I1RB03; -.
DR STRING; 229533.I1RB03; -.
DR GeneID; 23548180; -.
DR KEGG; fgr:FGSG_00702; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01771; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_019940_4_1_1; -.
DR InParanoid; I1RB03; -.
DR PHI-base; PHI:7559; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030448; P:hyphal growth; IMP:PHI-base.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Secreted; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..526
FT /note="Type 2 glycosyltransferase"
FT /id="PRO_0000448755"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 526 AA; 60878 MW; 14B76117D40F4388 CRC64;
MSESEHQNVG RSPLGFAGPL SLSMPSFDFW YSSTFWLYLF LGLWFHRYFR LLVHCVSHWT
YKSKPIPSKP TFTSKDVTVV IPTIHNAFEE LRPSLESILA CEPAELILVT THDKRKELQK
LADSLVFPKV RVLDTPIANK RLQVCEALPK VETPITIMAD DDVTWPSTLM PWILAPFEDP
EIGGVGTCQR VRREHDGSWS TKAWNWLGAA YIERRNFEIS ATHNIDGGTS CMSGRTGAYR
SEILSSHDFL HGFKNEKWRK WILNADDDNF VTRWLVSHQW KTWIQYEKEC EIETTLENST
KFLYQCSRWA RSNWRSNWTS MVTERYIWKQ QLWCTYALHF ATFTSLAFLI DPLLLASCWW
GTADWDMQNR RYAFWSQFVF MFAFTKVVKL MGLFIRNPTD VMFLPVSVVF GYFHGLVKLY
ALITLNMTSW GSRADGDAND EQRLAPAPQP SIVLKTPPGK GSLIRYNARQ KGRQTQAQQV
SWEKSDYASY DSSTSYVPIR VHTPMATTPI DTKLYTNESS NTCWAI
