CEGT_MAGO7
ID CEGT_MAGO7 Reviewed; 494 AA.
AC G4MS28; Q96V38;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000250|UniProtKB:Q16739};
DE EC=2.4.1.80 {ECO:0000269|PubMed:11443131};
DE AltName: Full=GLCT-1;
DE AltName: Full=Glucosylceramide synthase {ECO:0000303|PubMed:11443131};
DE Short=GCS;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase;
DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase;
GN ORFNames=MGG_10668;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=11443131; DOI=10.1074/jbc.m104952200;
RA Leipelt M., Warnecke D., Zahringer U., Ott C., Muller F., Hube B.,
RA Heinz E.;
RT "Glucosylceramide synthases, a gene family responsible for the biosynthesis
RT of glucosphingolipids in animals, plants, and fungi.";
RL J. Biol. Chem. 276:33621-33629(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Catalyzes the final step in the biosynthesis of the membrane
CC lipid glucosylceramide (GluCer), the transfer of glucose to ceramide.
CC Glucosylceramides play important roles in growth, differentiation and
CC pathogenicity. {ECO:0000269|PubMed:11443131}.
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:0000269|PubMed:11443131};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:11443131}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF364402; AAK73019.1; -; mRNA.
DR EMBL; CM001231; EHA57494.1; -; Genomic_DNA.
DR RefSeq; XP_003710106.1; XM_003710058.1.
DR AlphaFoldDB; G4MS28; -.
DR STRING; 318829.MGG_10668T0; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR EnsemblFungi; MGG_10668T0; MGG_10668T0; MGG_10668.
DR GeneID; 2682281; -.
DR KEGG; mgr:MGG_10668; -.
DR VEuPathDB; FungiDB:MGG_10668; -.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_1_0_1; -.
DR InParanoid; G4MS28; -.
DR OMA; HGSMPFH; -.
DR OrthoDB; 793389at2759; -.
DR UniPathway; UPA00222; -.
DR PHI-base; PHI:4493; -.
DR Proteomes; UP000009058; Chromosome 1.
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..494
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_0000434807"
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..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..380
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..494
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 95
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 160
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 285
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 326..330
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 494 AA; 55081 MW; E60EA8DA11083E41 CRC64;
MPLLMDGLAY AGAIWSLIVF CVQAIGLYQL FRSYSRPPPP PVSPSLTSED VPHVTVIRPV
KGLEPRLYEC LISTLQQSYP RDKLSVHLCI SSKEDPAYPV LKKVVVEYSA THDVRLFVET
EDPLLYGTTG DTRNLGPNPK IRNISHAYRE AKGDIIWIID CNIWVSKGTA GRMVDKLCGF
PAGSRPYKFV HQLPLSVDVT PPQDSGVLRT GGGRLDEMFM ATTHGKFYSA INTVGVAPCI
CGKSNMFRKS HLDRLTDPAH NPILPKETAT RPRGIDYFSA YICEDHLIGD LLWRSQVPGH
GNHGLVFGDL ALQPMMNNSV GSYIARRVRW LRVRKWTVLL ATLVEPGVES MVCCMAFAHA
LTTTPWCPNP ADWPIPHTWT ALWSIWLAAI AVWATLDYVV YHFLHSCRSI EKDADSPDFA
QGNELMKRPF GAWILAWIGR EILALPIWTR AVLLGTTVTW RGTKFKVRPD QSVVDIPNAG
AKSNGIGSTN RKVR
