CEGT_GIBZE
ID CEGT_GIBZE Reviewed; 528 AA.
AC I1RPI4; A0A0E0SQR3;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000250|UniProtKB:Q16739};
DE EC=2.4.1.80 {ECO:0000305|PubMed:17908205};
DE AltName: Full=GLCT-1;
DE AltName: Full=Glucosylceramide synthase {ECO:0000303|PubMed:17908205};
DE Short=GCS {ECO:0000303|PubMed:17908205};
DE AltName: Full=UDP-glucose ceramide glucosyltransferase {ECO:0000303|PubMed:17908205};
DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase;
GN Name=GCS1 {ECO:0000303|PubMed:17908205}; ORFNames=FGRRES_05955, FGSG_05955;
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, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=17908205; DOI=10.1111/j.1365-2958.2007.05955.x;
RA Ramamoorthy V., Cahoon E.B., Li J., Thokala M., Minto R.E., Shah D.M.;
RT "Glucosylceramide synthase is essential for alfalfa defensin-mediated
RT growth inhibition but not for pathogenicity of Fusarium graminearum.";
RL Mol. Microbiol. 66:771-786(2007).
CC -!- FUNCTION: Catalyzes the final step in the biosynthesis of the membrane
CC lipid glucosylceramide (GluCer), the transfer of glucose to ceramide
CC (Probable). Glucosylceramides play important roles in growth,
CC differentiation and pathogenicity. Contribution to fungal pathogenesis
CC is host-dependent (PubMed:17908205). {ECO:0000269|PubMed:17908205,
CC ECO:0000305|PubMed:17908205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-
CC glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80;
CC Evidence={ECO:0000305|PubMed:17908205};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:17908205}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9R0E0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS
CC active site, involved in catalysis and UDP-sugar binding.
CC {ECO:0000250|UniProtKB:Q9R0E0}.
CC -!- DISRUPTION PHENOTYPE: Results in complete loss of glucosylceramides
CC (GluCers) in mutant cells. Shows a significant change in the conidial
CC morphology and displays a dramatic polar growth defect, and its mycelia
CC are resistant to cell wall degrading enzymes. Shows increased
CC resistance to plant defensins MsDef1 and RsAFP2, but not MsDef4.
CC {ECO:0000269|PubMed:17908205}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; DS231665; ESU11990.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF88776.1; -; Genomic_DNA.
DR RefSeq; XP_011324566.1; XM_011326264.1.
DR AlphaFoldDB; I1RPI4; -.
DR STRING; 5518.FGSG_05955P0; -.
DR EnsemblFungi; ESU11990; ESU11990; FGSG_05955.
DR GeneID; 23553106; -.
DR KEGG; fgr:FGSG_05955; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G19155; -.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_1_0_1; -.
DR InParanoid; I1RPI4; -.
DR UniPathway; UPA00222; -.
DR PHI-base; PHI:1002; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; PTHR12726; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Golgi apparatus; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..528
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_0000434808"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..402
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..528
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 503..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 154
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 308
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 349..353
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 528 AA; 59553 MW; 0CAEDF50C1BEFDE8 CRC64;
MYSFIECIAG ALFVLGCVVV TLVVIGVRAL LYNFRNRPAP PLSSQLGQNA PHVTIIRPVK
GLEPRLYDCI AASFRQDYPQ DKVSIRLCLE DDTDPAYPVL QKVIEDFPTI DARIMLEKED
HVLSETVNMG PNPKIRNLSR AYREAKGDIV WIIDCNIWMA KGVLGRMVDK LMGYRVGGAA
KPYKFVHQLP IVVDLMDFST SLAAEGRSLL DASPEEDHPT EDLGAEEFPK VMSHGGGRID
EMFMTTSHAK FYSAINTLRA APCAVGKSNM FRKSQLDQAT DAILNPKLDQ SKNLPTGVDY
FSHNICEDHL IGEALWTTDF PGYKSHGLVW GDIAVQPVSG MSVQAYTARR SRWLRARKYT
VLSATILEPF TECFLFATYM SLAMTTIPVL SQNLGIPKTW NATAIAWFTI TTLWMLIDYI
GYLRLHSGVT MEVDEHTPYF AKGFKNTGGI KRRPFLEFLA AWIGREGLAF PVWAYAVVFG
NTVNWRGRLF YIHWDTTVDA VEPREERTRE VRTPELERGP SRNKHRVD
