ID U6GNX1_9EIME Unreviewed; 257 AA. AC U6GNX1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 08-NOV-2023, entry version 20. DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136}; DE EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136}; DE EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136}; DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136}; GN ORFNames=EPH_0033360 {ECO:0000313|EMBL:CDI80304.1}; OS Eimeria praecox. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria. OX NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI80304.1}; RN [1] {ECO:0000313|EMBL:CDI80304.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Houghton {ECO:0000313|EMBL:CDI80304.1}; RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S., RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D., RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P., RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M., RA Tomley F., Pain A.; RT "Genomic analysis of the causative agents of coccidiosis in chickens."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDI80304.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Houghton {ECO:0000313|EMBL:CDI80304.1}; RA Aslett M.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol CC diphosphate. {ECO:0000256|RuleBase:RU367136}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519, CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510, CC ChEBI:CHEBI:132511; EC=2.4.1.257; CC Evidence={ECO:0000256|RuleBase:RU367136}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc- CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D- CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA- CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132; CC Evidence={ECO:0000256|RuleBase:RU367136}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|RuleBase:RU367136}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367136}. CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC {ECO:0000256|RuleBase:RU367136}. 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; HG691828; CDI80304.1; -; Genomic_DNA. DR AlphaFoldDB; U6GNX1; -. DR EnsemblProtists; CDI80304; CDI80304; EPH_0033360. DR VEuPathDB; ToxoDB:EPH_0033360; -. DR OrthoDB; 1377at2759; -. DR UniPathway; UPA00378; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR027054; ALG2. DR InterPro; IPR001296; Glyco_trans_1. DR PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1. DR PANTHER; PTHR45918:SF1; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1. DR Pfam; PF00534; Glycos_transf_1; 2. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|RuleBase:RU367136}; KW Transferase {ECO:0000256|RuleBase:RU367136, ECO:0000313|EMBL:CDI80304.1}. FT DOMAIN 68..133 FT /note="Glycosyl transferase family 1" FT /evidence="ECO:0000259|Pfam:PF00534" FT DOMAIN 154..206 FT /note="Glycosyl transferase family 1" FT /evidence="ECO:0000259|Pfam:PF00534" SQ SEQUENCE 257 AA; 28581 MW; E0288172C3A02602 CRC64; MRDTLSCMRI VNSVPDNTRL TFVFLIAFFI RKAKPRVLYP PVSTEVEAFQ LKGGSSDSDA SFSELERFDL SAPFVVSLNR FEEKKDVELA IKAVARLPRQ IKCNLIVAGG FDPRLPECND YFQRLVKLSK ELNFRVLGCE DVVDTNTPAL DNSVPCEAMF VGCLPVACNT GGPRETIVDR ETGFLCPPTP ESFSAALKHI LLLSLENPEE LAALRSKAQI HATNRFSPDV FRRSLKAIIE DVTGPWDGSS SERPKKV //