ID GLGA_SHIBS Reviewed; 477 AA. AC Q31VJ4; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 91. 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=SBO_3427; OS Shigella boydii serotype 4 (strain Sb227). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300268; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sb227; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., RA Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic agents of RT bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). 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; CP000036; ABB67914.1; -; Genomic_DNA. DR RefSeq; WP_001197645.1; NC_007613.1. DR AlphaFoldDB; Q31VJ4; -. DR SMR; Q31VJ4; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR KEGG; sbo:SBO_3427; -. DR HOGENOM; CLU_009583_18_2_6; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000007067; 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..477 FT /note="Glycogen synthase" FT /id="PRO_0000230263" 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 477 AA; 52796 MW; 0C6642CF8C97CF42 CRC64; MQVLHVCSEM FPLLKTGGLA DVIGALPAAQ IADGVDARVL LPAFPDIRRG VTDAQVVSRR DTFAGHITLL FGHYNGVGIY LIDAPHLYDR PGSPYHDTNL FAYTDNVLRF ALLGWVGAEM ASGLDPFWRP DVVHAHDWHA GLAPAYLAAR GRPAKSVFTV HNLAYQGMFY AHHMNDIQLP WSFFNIHGLE FNGQISFLKA GLYYADHITA VSPTYAREIT EPQFAYGMEG LLQQRHREGR LSGVLNGVDE KIWSPETDLL LASRYTRDTL EDKAENKRQL QIAMGLKVDD KVPLFAVVSR LTSQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEYPGQVG VQIGYHEAFS HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG LADTVSDCSL ENLADGVASG FVFEDSNAWS LLRAIRRAFV LWSRASLWRF VQRQAMAMDF SWQVAAKSYR ELYYRLK //