ID GLYG_RABIT Reviewed; 333 AA. AC P13280; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 153. DE RecName: Full=Glycogenin-1; DE Short=GN-1; DE Short=GN1; DE EC=2.4.1.186 {ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735}; GN Name=GYG1; Synonyms=GYG; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC RP ACTIVITY, COFACTOR, PATHWAY, AND TISSUE SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=1281472; DOI=10.1016/s0021-9258(18)35674-6; RA Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.; RT "Rabbit skeletal muscle glycogenin. Molecular cloning and production of RT fully functional protein in Escherichia coli."; RL J. Biol. Chem. 267:25759-25763(1992). RN [2] RP PROTEIN SEQUENCE OF 2-333. RC STRAIN=New Zealand white; TISSUE=Skeletal muscle; RX PubMed=2806254; DOI=10.1111/j.1432-1033.1989.tb15090.x; RA Campbell D.G., Cohen P.; RT "The amino acid sequence of rabbit skeletal muscle glycogenin."; RL Eur. J. Biochem. 185:119-125(1989). RN [3] RP PROTEIN SEQUENCE OF 35-48; 182-202; 210-227 AND 308-325, FUNCTION, RP CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR. RC TISSUE=Liver; RX PubMed=2526735; DOI=10.1111/j.1432-1033.1989.tb14914.x; RA Smythe C., Villar-Palasi C., Cohen P.; RT "Structural and functional studies on rabbit liver glycogenin."; RL Eur. J. Biochem. 183:205-209(1989). RN [4] RP PROTEIN SEQUENCE OF 35-48, AND PHOSPHORYLATION AT SER-44. RX PubMed=3151442; RA Lomako J., Whelan W.J.; RT "The occurrence of serine phosphate in glycogenin: a possible regulatory RT site."; RL BioFactors 1:261-264(1988). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, AND RP MUTAGENESIS OF TYR-195. RX PubMed=8143846; DOI=10.1016/0014-5793(94)80580-6; RA Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.; RT "Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is RT not essential for catalytic function and activity."; RL FEBS Lett. 342:38-42(1994). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, AND MUTAGENESIS OF RP TYR-195. RX PubMed=7771798; DOI=10.1006/abbi.1995.1295; RA Cao Y., Steinrauf L.K., Roach P.J.; RT "Mechanism of glycogenin self-glucosylation."; RL Arch. Biochem. Biophys. 319:293-298(1995). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=9409751; DOI=10.1016/s0014-5793(97)01299-4; RA Baque S., Guinovart J.J., Ferrer J.C.; RT "Glycogenin, the primer of glycogen synthesis, binds to actin."; RL FEBS Lett. 417:355-359(1997). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, AND MUTAGENESIS OF RP LYS-86 AND TYR-195. RX PubMed=10049511; DOI=10.1006/abbi.1998.1073; RA Lin A., Mu J., Yang J., Roach P.J.; RT "Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, RT involves an inter-subunit reaction."; RL Arch. Biochem. Biophys. 363:163-170(1999). RN [9] {ECO:0007744|PDB:1LL0, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1LL3} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, RP SUBUNIT, AND COFACTOR. RX PubMed=12051921; DOI=10.1016/s0022-2836(02)00305-4; RA Gibbons B.J., Roach P.J., Hurley T.D.; RT "Crystal structure of the autocatalytic initiator of glycogen biosynthesis, RT glycogenin."; RL J. Mol. Biol. 319:463-477(2002). RN [10] {ECO:0007744|PDB:1ZCT, ECO:0007744|PDB:1ZCU, ECO:0007744|PDB:1ZCV, ECO:0007744|PDB:1ZCY, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH MANGANESE; UDP AND RP UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, RP SUBUNIT, AND MUTAGENESIS OF ASP-160 AND ASP-163. RX PubMed=15849187; DOI=10.1074/jbc.m502344200; RA Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.; RT "Requirements for catalysis in mammalian glycogenin."; RL J. Biol. Chem. 280:23892-23899(2005). RN [11] {ECO:0007744|PDB:3V8Y, ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V90, ECO:0007744|PDB:3V91} RP X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH RP MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF THR-83. RX PubMed=22226635; DOI=10.1016/j.febslet.2011.12.028; RA Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.; RT "Structural and biochemical insight into glycogenin inactivation by the RT glycogenosis-causing T82M mutation."; RL FEBS Lett. 586:254-257(2012). RN [12] {ECO:0007744|PDB:3USQ, ECO:0007744|PDB:3USR} RP X-RAY CRYSTALLOGRAPHY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, RP MUTAGENESIS OF TYR-195, AND GLYCOSYLATION AT TYR-195. RX PubMed=22128147; DOI=10.1074/jbc.m111.287813; RA Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.; RT "Mechanisms of monomeric and dimeric glycogenin autoglucosylation."; RL J. Biol. Chem. 287:1955-1961(2012). CC -!- FUNCTION: Glycogenin participates in the glycogen biosynthetic process CC along with glycogen synthase and glycogen branching enzyme. It CC catalyzes the formation of a short alpha (1,4)-glucosyl chain CC covalently attached via a glucose 1-O-tyrosyl linkage to internal CC tyrosine residues and these chains act as primers for the elongation CC reaction catalyzed by glycogen synthase. {ECO:0000269|PubMed:10049511, CC ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, CC ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, CC ECO:0000269|PubMed:2526735, ECO:0000269|PubMed:7771798, CC ECO:0000269|PubMed:8143846}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D- CC glucosyl-L-tyrosyl-[glycogenin] + UDP + H(+); Xref=Rhea:RHEA:23360, CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, CC ChEBI:CHEBI:140573; EC=2.4.1.186; CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23361; CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha- CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + UDP CC + H(+); Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA- CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, CC ChEBI:CHEBI:140574; EC=2.4.1.186; CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56561; CC Evidence={ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281472, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:1281472, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, CC ECO:0000269|PubMed:8143846}; CC Note=Divalent metal ions. Required for self-glucosylation. Manganese is CC the most effective. {ECO:0000269|PubMed:12051921}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, CC ECO:0000269|PubMed:2526735}. CC -!- SUBUNIT: Part of the GYS1-GYG1 complex, a heterooctamer composed of a CC tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds CC to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may CC dissociate from GYG1 dimers to continue glycogen polymerization on its CC own (By similarity) (PubMed:12051921, PubMed:15849187, PubMed:22128147, CC PubMed:22226635). May also form a heterooctamer complex with GYS2 (via CC GYG1 C-terminus) (By similarity). {ECO:0000250|UniProtKB:P46976, CC ECO:0000250|UniProtKB:Q9R062, ECO:0000269|PubMed:12051921, CC ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, CC ECO:0000269|PubMed:22226635}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9409751}. Nucleus CC {ECO:0000269|PubMed:9409751}. Note=Localizes to glycogen granules CC (glycosomes) in the cytoplasm (By similarity). Cytosolic localization CC is dependent on the actin cytoskeleton (PubMed:9409751). CC {ECO:0000250|UniProtKB:C4R941, ECO:0000269|PubMed:9409751}. CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, brain and CC testis, and at lower levels in kidney. {ECO:0000269|PubMed:1281472}. CC -!- PTM: Self-glycosylated by the transfer of glucose residues from UDP- CC glucose to itself, forming an alpha-1,4-glycan of around 10 residues CC attached to Tyr-195. {ECO:0000269|PubMed:10049511, CC ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, CC ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:3151442}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin CC subfamily. {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; L01791; AAA31404.1; -; mRNA. DR PIR; A45094; A45094. DR RefSeq; NP_001075710.1; NM_001082241.1. DR PDB; 1LL0; X-ray; 3.43 A; A/B/C/D/E/F/G/H/I/J=1-333. DR PDB; 1LL2; X-ray; 1.90 A; A=1-333. DR PDB; 1LL3; X-ray; 1.90 A; A=1-333. DR PDB; 1ZCT; X-ray; 2.60 A; A/B=1-270. DR PDB; 1ZCU; X-ray; 2.00 A; A=1-333. DR PDB; 1ZCV; X-ray; 1.98 A; A=1-333. DR PDB; 1ZCY; X-ray; 1.99 A; A=1-333. DR PDB; 1ZDF; X-ray; 2.45 A; A=1-333. DR PDB; 1ZDG; X-ray; 2.30 A; A=1-333. DR PDB; 3USQ; X-ray; 2.40 A; A=1-271. DR PDB; 3USR; X-ray; 2.10 A; A=1-271. DR PDB; 3V8Y; X-ray; 2.15 A; A=1-271. DR PDB; 3V8Z; X-ray; 2.20 A; A=1-271. DR PDB; 3V90; X-ray; 2.00 A; A=1-271. DR PDB; 3V91; X-ray; 2.00 A; A=1-271. DR AlphaFoldDB; P13280; -. DR SMR; P13280; -. DR BioGRID; 1172081; 2. DR CORUM; P13280; -. DR FunCoup; P13280; 320. DR STRING; 9986.ENSOCUP00000028932; -. DR CAZy; GT8; Glycosyltransferase Family 8. DR GlyCosmos; P13280; 1 site, No reported glycans. DR iPTMnet; P13280; -. DR PaxDb; 9986-ENSOCUP00000028932; -. DR GeneID; 100009058; -. DR KEGG; ocu:100009058; -. DR CTD; 2992; -. DR eggNOG; KOG1950; Eukaryota. DR InParanoid; P13280; -. DR OMA; ACHVQPK; -. DR OrthoDB; 2014201at2759; -. DR BRENDA; 2.4.1.186; 1749. DR UniPathway; UPA00164; -. DR EvolutionaryTrace; P13280; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB. DR CDD; cd02537; GT8_Glycogenin; 1. DR FunFam; 3.90.550.10:FF:000025; Glycogenin-1 isoform 1; 1. DR Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1. DR InterPro; IPR002495; Glyco_trans_8. DR InterPro; IPR050587; GNT1/Glycosyltrans_8. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR11183; GLYCOGENIN SUBFAMILY MEMBER; 1. DR Pfam; PF01501; Glyco_transf_8; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2806254" FT CHAIN 2..333 FT /note="Glycogenin-1" FT /evidence="ECO:0000305" FT /id="PRO_0000215178" FT REGION 284..316 FT /note="Interaction with GYS1" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 9 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 9 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 11 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 11 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 12 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 12 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0007744|PDB:1LL2, FT ECO:0007744|PDB:1ZDG" FT BINDING 15 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 15 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 77 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 77 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 86 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 102 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91" FT BINDING 102 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0007744|PDB:1ZCT" FT BINDING 102 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 103 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 103 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 104 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91" FT BINDING 104 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 104 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 133 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 134 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:3V91" FT BINDING 160 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 163 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P46976" FT BINDING 164 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT BINDING 212 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, FT ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91" FT BINDING 212 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0007744|PDB:1ZCT" FT BINDING 215 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0007744|PDB:1ZCT" FT BINDING 215 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, FT ECO:0007744|PDB:3V91" FT BINDING 218 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000269|PubMed:15849187, FT ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1ZCT, FT ECO:0007744|PDB:3V8Z" FT BINDING 218 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:12051921, FT ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, FT ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, FT ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91" FT SITE 86 FT /note="Important for catalytic activity" FT /evidence="ECO:0000269|PubMed:10049511" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000250|UniProtKB:P46976" FT MOD_RES 44 FT /note="Phosphoserine; by PKA; in vitro" FT /evidence="ECO:0000269|PubMed:3151442" FT CARBOHYD 195 FT /note="O-linked (Glc...) tyrosine" FT /evidence="ECO:0000269|PubMed:8143846" FT MUTAGEN 83 FT /note="T->M: Loss of autoglucosylation." FT /evidence="ECO:0000269|PubMed:22226635" FT MUTAGEN 83 FT /note="T->S: No effect on autoglucosylation." FT /evidence="ECO:0000269|PubMed:22226635" FT MUTAGEN 86 FT /note="K->Q: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:10049511" FT MUTAGEN 160 FT /note="D->N,S: Reduced trans-glucosylation activity by at FT least 260-fold and reduced UDP-glucose hydrolytic activity FT by 4 to 14-fold." FT /evidence="ECO:0000269|PubMed:15849187" FT MUTAGEN 163 FT /note="D->N: Loss of self-glucosylation activity and FT ability to trans-glucosylate maltose. Reduces UDP-glucose FT hydrolytic activity by at least 190-fold." FT /evidence="ECO:0000269|PubMed:15849187" FT MUTAGEN 163 FT /note="D->S: Loss of self-glucosylation activity and 18 to FT 30-fold reduction in its ability to trans-glucosylate FT maltose. Reduces UDP-glucose hydrolytic activity by at FT least 190-fold." FT /evidence="ECO:0000269|PubMed:15849187" FT MUTAGEN 195 FT /note="Y->F,T: Loss of self-glucosylation. No loss of FT catalytic activity." FT /evidence="ECO:0000269|PubMed:10049511, FT ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:7771798, FT ECO:0000269|PubMed:8143846" FT CONFLICT 39 FT /note="T -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="C -> S (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="C -> L (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 3..12 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 13..28 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 45..54 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 71..76 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 81..86 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 87..91 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 112..116 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 119..124 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 131..139 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 143..155 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:1ZCY" FT HELIX 163..170 FT /evidence="ECO:0007829|PDB:1LL2" FT TURN 171..176 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 209..212 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1LL3" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:3USR" FT TURN 226..229 FT /evidence="ECO:0007829|PDB:1LL2" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:3USR" FT HELIX 243..252 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 253..257 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 258..261 FT /evidence="ECO:0007829|PDB:1LL2" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:1ZCV" SQ SEQUENCE 333 AA; 37397 MW; 7C27F7B428F67571 CRC64; MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA LEIVFDEVIT VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFEREEL SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HVASEQGSFD GGDQGLLNTF FNSWATTDIR KHLPFIYNLS SISIYSYLPA FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM THPQFLNVWW DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ //