ALG5B_TRIVA
ID ALG5B_TRIVA Reviewed; 333 AA.
AC A2EK20;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase ALG5B {ECO:0000303|PubMed:18552282};
DE Short=DolP-glucosyltransferase;
DE EC=2.4.1.117 {ECO:0000269|PubMed:18552282};
GN Name=ALG5B {ECO:0000303|PubMed:18552282};
GN ORFNames=TVAG_174740 {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; DS113410; EAY07004.1; -; Genomic_DNA.
DR RefSeq; XP_001319227.1; XM_001319192.1.
DR AlphaFoldDB; A2EK20; -.
DR SMR; A2EK20; -.
DR STRING; 5722.XP_001319227.1; -.
DR GeneID; 4764889; -.
DR KEGG; tva:TVAG_174740; -.
DR VEuPathDB; TrichDB:TVAG_174740; -.
DR eggNOG; KOG2977; Eukaryota.
DR InParanoid; A2EK20; -.
DR OMA; MVNTDAV; -.
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..333
FT /note="Dolichyl-phosphate beta-glucosyltransferase ALG5B"
FT /id="PRO_0000431406"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..333
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 333 AA; 37915 MW; E85E86D3435F7D4E CRC64;
MIAEIADILG DICLLIFVFA LIYAICSSVV SDETLYDRTL LASTDPRKLE YFIEPSHDEQ
PQLFPTIFDE PEVYATFVVP AYNEERRIPS MLNETLQFLD TRRDENPNFS YEIIVVDDGS
KDKTAEVVLD FANSHPEIRL LKQPVNMGKG AAVAAGCSHA RGQYILMVDA DGATKIDEFN
ELEKKMLQLQ QVNREAIVVG SRAHLEGQDK ANRTPIRKFL GLSFHLLILL SGVRGINDTQ
CGFKLFSREA SRYLFPNQHI ERWCFDPELL VIGRKRKMQI AEVPVEWNEI EGSKMKVTSM
IKMAIDLLRI ALFHGMGIWT VKLKQAVYDQ ELI
