ID   ALG5D_TRIVA             Reviewed;         327 AA.
AC   A2E3C6;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Dolichyl-phosphate beta-glucosyltransferase ALG5D {ECO:0000303|PubMed:18552282};
DE            Short=DolP-glucosyltransferase;
DE            EC=2.4.1.117 {ECO:0000269|PubMed:18552282};
GN   Name=ALG5D {ECO:0000303|PubMed:18552282};
GN   ORFNames=TVAG_221700 {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS113295; EAY12817.1; -; Genomic_DNA.
DR   RefSeq; XP_001325040.1; XM_001325005.1.
DR   AlphaFoldDB; A2E3C6; -.
DR   SMR; A2E3C6; -.
DR   STRING; 5722.XP_001325040.1; -.
DR   GeneID; 4770785; -.
DR   KEGG; tva:TVAG_221700; -.
DR   VEuPathDB; TrichDB:TVAG_221700; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   InParanoid; A2E3C6; -.
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; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..327
FT                   /note="Dolichyl-phosphate beta-glucosyltransferase ALG5D"
FT                   /id="PRO_0000431408"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..327
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   327 AA;  37953 MW;  46ABE280AEBD0047 CRC64;
     MEKQLAELSV YILIIFLILG FIMAILMRFG DDTTLFDLTQ LPKNNPKKLN YYVQPAKNPN
     ENVPFKTIFD KPQVYVSFIV PAYNEEKRLP KMLEETIEYL EQRRYKDNNF TWEIVVVNDG
     SKDRTAHVVL EYAERYSNIF LLNQPHNMGK GAAIQAGCLH ARGQLVLMVD ADGATKISDF
     GLLENEIKKL MKNNKEAIVV GSRTLNEDKS KVHRTFIRKI LGLGMHILIV ISGVHGIKDT
     QCGFKLFTRD ACKMLFMNQH VQRWCFDPEL LVIARRRKMK VSEISVEWNE IEGSKMKISG
     MIKMAIDLLR IAVFYRLNIW TIRDRKF