ID GLGA_HYDCU Reviewed; 491 AA. AC Q31IB5; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 88. 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=Tcr_0512; OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira OS crunogena). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Hydrogenovibrio. OX NCBI_TaxID=317025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25203 / XCL-2; RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383; RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., RA Tinkham L.E., Zeruth G.T.; RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena RT XCL-2."; RL PLoS Biol. 4:1-17(2006). 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; CP000109; ABB41108.1; -; Genomic_DNA. DR AlphaFoldDB; Q31IB5; -. DR SMR; Q31IB5; -. DR STRING; 317025.Tcr_0512; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR KEGG; tcx:Tcr_0512; -. DR eggNOG; COG0297; Bacteria. DR HOGENOM; CLU_009583_18_4_6; -. DR OrthoDB; 9808590at2; -. DR UniPathway; UPA00164; -. 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..491 FT /note="Glycogen synthase" FT /id="PRO_0000230270" 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 491 AA; 55113 MW; AC8B7E96F5DDEB20 CRC64; MKILFATSEA HPLIKTGGLA DVSGSLPDAY HHLKQKVRMV MPAYGDIWEK VSGVKQLSEL SIAACGRQLH VRIHVASAEG IDVPIWLVDI PELFHRPGNP YLALDGKDWW DNGERFAVFS KVVAEIAMNR AGLKWQPDLV QTNDWQTGLV SALLTLEAER PKTVFTIHNM AYAGLFPKSL FEGLGLPWSW WEPHDGIEFY DNMSMLKAGI QMADWVTTVS PTYAKEITFP EYAYGLEGVL IKRLDEGRLV GILNGIDHDV WNPKTDPFIR YHYSVDKGRV AAKKRNKKDM LDFWDLPKAV VDADDPVIGL VGRLVPQKGI DLVLEVLPEL IEQTNVRFVI VGTGDSLFEY QLTELAHQYP ERLMIYIGYS ESLAHKVEAG ADLFLMPSRF EPCGLNQLYS LAYGTPPIVH STGGLSDTVV NATKENLATG QATGFVFYDP SRHALKSTIL HALHLFSKKG TWQKLQKNGM RQDFSWTRSA KQYLALFKAM V //