ID   ALG5E_TRIVA             Reviewed;         325 AA.
AC   A2DSR8;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Dolichyl-phosphate beta-glucosyltransferase ALG5E {ECO:0000303|PubMed:18552282};
DE            Short=DolP-glucosyltransferase;
DE            EC=2.4.1.117 {ECO:0000269|PubMed:18552282};
GN   Name=ALG5E {ECO:0000303|PubMed:18552282};
GN   ORFNames=TVAG_347770 {ECO:0000303|PubMed:17218520};
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-98 / G3;
RX   PubMed=17218520; DOI=10.1126/science.1132894;
RA   Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA   Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA   Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA   Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA   Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA   Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA   Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA   Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA   Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA   Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA   Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA   Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA   Johnson P.J.;
RT   "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT   vaginalis.";
RL   Science 315:207-212(2007).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18552282; DOI=10.1128/ec.00061-08;
RA   Grabinska K.A., Ghosh S.K., Guan Z., Cui J., Raetz C.R., Robbins P.W.,
RA   Samuelson J.;
RT   "Dolichyl-phosphate-glucose is used to make O-glycans on glycoproteins of
RT   Trichomonas vaginalis.";
RL   Eukaryot. Cell 7:1344-1351(2008).
CC   -!- FUNCTION: Dolichyl-phosphate beta-glucosyltransferase involved in the
CC       glycosylation of glycoproteins through the synthesis of dolichyl beta-
CC       D-glucosyl phosphate which serves as a sugar donor for transfer of
CC       three glucose residues to the Man-9-GlcNAc-2-PP-dolichol precursor to
CC       N-glycans. {ECO:0000269|PubMed:18552282}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC         D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC         COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC         Evidence={ECO:0000269|PubMed:18552282};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:18552282}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P40350}; Single-pass type II membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; DS113241; EAY16467.1; -; Genomic_DNA.
DR   RefSeq; XP_001328690.1; XM_001328655.1.
DR   AlphaFoldDB; A2DSR8; -.
DR   SMR; A2DSR8; -.
DR   STRING; 5722.XP_001328690.1; -.
DR   GeneID; 4774490; -.
DR   KEGG; tva:TVAG_347770; -.
DR   VEuPathDB; TrichDB:TVAG_347770; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   InParanoid; A2DSR8; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001542; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd04188; DPG_synthase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR035518; DPG_synthase.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..325
FT                   /note="Dolichyl-phosphate beta-glucosyltransferase ALG5E"
FT                   /id="PRO_0000431409"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        6..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..215
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  36962 MW;  7161CAA46B53E407 CRC64;
     MNFWNFLEIL LFIGIVAAGL IVAVMIKTAE DTTLFDRTQL PEDNPQKLNY YVQPPPNGDE
     KVPFPTVFEP AKVYTTFVVP AYNEEKRIPK MLDETVEYLK SREAKDKSFT WEIVVVNDGS
     KDKTKEVVLN YAKDYPNIFL LNQPVNMGKG AAIQAGCLHA RGELVLMVDA DGATKINEFE
     ALETEIKKLM KNNNQAIVVG SRAQNEKANR TPIRKFLGLG MHVLIVLSGV RGIHDTQCGF
     KLFSREACKM LFMNQHVQRW CFDPELLVIG RRLGMKISEI PVEWNEIEGS KMKISGMIKM
     AIDLIDIAIF HRVGAWTIRD RRINK