ID   ALG5A_TRIVA             Reviewed;         323 AA.
AC   A2DZE8;
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 ALG5A {ECO:0000303|PubMed:18552282};
DE            Short=DolP-glucosyltransferase;
DE            EC=2.4.1.117 {ECO:0000269|PubMed:18552282};
GN   Name=ALG5A {ECO:0000303|PubMed:18552282};
GN   ORFNames=TVAG_487200 {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; DS113273; EAY14277.1; -; Genomic_DNA.
DR   RefSeq; XP_001326500.1; XM_001326465.1.
DR   AlphaFoldDB; A2DZE8; -.
DR   SMR; A2DZE8; -.
DR   STRING; 5722.XP_001326500.1; -.
DR   GeneID; 4772265; -.
DR   KEGG; tva:TVAG_487200; -.
DR   VEuPathDB; TrichDB:TVAG_487200; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   InParanoid; A2DZE8; -.
DR   OMA; THWFWDT; -.
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..323
FT                   /note="Dolichyl-phosphate beta-glucosyltransferase ALG5A"
FT                   /id="PRO_0000431405"
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..323
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   323 AA;  36764 MW;  CE733C6B305D152D CRC64;
     MKFWRFVQIL FFLGVAAVGL VVAVMIANAD DTTLFDRMQL PDGDPNKLNY YIQPAPNGNE
     KVPFPTIFDP ASVYLSLVVP AYNEEKRLPK MLDETLNYLK SREEKDKSFT WEIVIVNDGS
     KDKTKEVVLN YAKEYPNIFL LNQPVNMGKG AAIQAGCLHV RGELVLMLDA DGATKIDDFE
     VLEKEIKSLM KTTNQAIVIG SRAQNEKAKR TPLRKFLSIG MHTLIVLSGV HGIRDTQCGF
     KLFTRESCKM IFMNQHVQRW CCDPEILVIA RRLGMKISEL PVEWNEIDGS KMKISGMIKM
     ATDLIKIAIF HRVGAWKIRD RRH