ID   LPG1_LEIDO              Reviewed;         434 AA.
AC   Q05889;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Galactofuranosyl glycosyltransferase;
DE            EC=2.4.1.-;
GN   Name=LPG1;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ld4;
RX   PubMed=8378337; DOI=10.1073/pnas.90.18.8609;
RA   Ryan K.A., Garraway L.A., Descoteaux A., Turco S.J., Beverley S.M.;
RT   "Isolation of virulence genes directing surface glycosyl-
RT   phosphatidylinositol synthesis by functional complementation of
RT   Leishmania.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8609-8613(1993).
CC   -!- FUNCTION: Glycosyltransferase that may be responsible for the addition
CC       of galactofuranosyl residues to the nascent lipophosphoglycan (LPG)
CC       chain. It could alternatively be involved in the synthesis of the
CC       galactofuranosyl donor.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       II membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle with a two-
CC       fold decrease in amastigotes (LPG is 1000-fold less abundant in
CC       amastigotes than in promastigotes).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; L11348; AAA03083.1; -; Unassigned_DNA.
DR   AlphaFoldDB; Q05889; -.
DR   CAZy; GT40; Glycosyltransferase Family 40.
DR   VEuPathDB; TriTrypDB:LdBPK_250010.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_250005000; -.
DR   VEuPathDB; TriTrypDB:LDHU3_25.0020; -.
DR   UniPathway; UPA00196; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..434
FT                   /note="Galactofuranosyl glycosyltransferase"
FT                   /id="PRO_0000059105"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        39..434
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   434 AA;  51016 MW;  BBE33A0EAE5079B8 CRC64;
     MAPPRWHHDR RRMAIFVRVG LYTLLFLMGY VVPLIIFYNR SRADTFEDTP RSGEAFISDE
     NFFHCIAERL SYKEQHPARI PYVLIPVTMD YQDIKQLFCN ITVPMTYIMF INNGMFRPLR
     SLLDRLAVDL RDYVDQNLFI IHHPENIAYA SAVNEGLRHA LNFSVAKVPW VFITNADVRF
     APGLIDEFVS QANEKTQGQL ERIRRLDQEI IAEARTLRNV PNRRFAFRSS QHPIITASSL
     PYRIRTMPPE EMKKQFADTY GIFYTDHKDF MATFALSRLA IATVGFFDEN YYPAYGEDHD
     YVWRMAALGY QKYFSEPGKF VHFENANLNV GGSARNRGIF KNTAYFLQSV KFGRMNYQPF
     RLQYRRAKWF PDGVTIYQDT GRNPLPFNGT IPLDMWVLDT DRRRSIWEIG ENIRCHRDYK
     PYSMKLLDFP VDPS