ID GLGA_BACCQ Reviewed; 476 AA. AC B9J2G5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Glycogen synthase {ECO:0000255|HAMAP-Rule:MF_00484}; DE EC=2.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00484}; DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000255|HAMAP-Rule:MF_00484}; GN Name=glgA {ECO:0000255|HAMAP-Rule:MF_00484}; GN OrderedLocusNames=BCQ_4682; OS Bacillus cereus (strain Q1). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=19060151; DOI=10.1128/jb.01629-08; RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., RA Xue Y., Zhu Y., Jin Q.; RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 RT with industrial applications."; RL J. Bacteriol. 191:1120-1121(2009). CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)- CC alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA- CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, CC ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00484}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. CC Bacterial/plant glycogen synthase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00484}. 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; CP000227; ACM15108.1; -; Genomic_DNA. DR AlphaFoldDB; B9J2G5; -. DR SMR; B9J2G5; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR KEGG; bcq:BCQ_4682; -. DR HOGENOM; CLU_009583_18_2_9; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000441; Chromosome. DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro. DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR HAMAP; MF_00484; Glycogen_synth; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR011835; GS/SS. DR InterPro; IPR013534; Starch_synth_cat_dom. DR NCBIfam; TIGR02095; glgA; 1. DR PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1. DR PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1. DR Pfam; PF08323; Glyco_transf_5; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Glycogen biosynthesis; Glycosyltransferase; Transferase. FT CHAIN 1..476 FT /note="Glycogen synthase" FT /id="PRO_1000135645" FT BINDING 15 FT /ligand="ADP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:57498" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00484" SQ SEQUENCE 476 AA; 54998 MW; 5A2F6CF2627E8E41 CRC64; MNILFAVSEC VPFVKSGGLA DVAGALPKEL KKLGVEVRII LPNYSLIPQK LRDGCTLHKV INVPLGWRNQ YCGILKGEQD GITYYLIDNE YYFKRDSLYG HYDDGERFSY FSKAVLECIP HLDFEVDVLH SHDWHTAMVN FLLREKYQDN PLYEHIKTVY TIHNLQFQGV FPPEVMYDLL ELGDEYFHSE QLEFYGNVNF MKGGIIASDQ ITAVSPTYKE EIQYEFFGEK LDGLLRKYND KLSGIVNGID TSVYNPETDS YITAQYDADS LYEKNENKRA LQRYFGLPEK EDTPIISMVT RLTKQKGLDL VRTVFREIME EDVQCIILGS GDSEYEQFFE WMAYEYPEKV KVYIGFNEEL AHQVYAGSDL FLMPSLFEPC GLGQLIALAY GTIPIVRETG GLNDTVQSYD EETGEGNGFS FTNFNAHDML HTVRRAIEFY HDKPVWEQLV KQAMTEDYSW EKSALAYKKL YKSLME //