ID GLGA_SYNE7 Reviewed; 465 AA. AC Q935Y7; Q31K71; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 3. DT 27-MAR-2024, entry version 103. 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=Synpcc7942_2518; ORFNames=sea0009; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Holtman C.K., Socias T., Mohler B.J., Chen Y., Min H., Golden S.S., RA Youderian P.; RT "Synechococcus elongatus PCC7942 genome sequence, cosmid 7H1."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Golden S., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; U30252; AAL03921.2; -; Genomic_DNA. DR EMBL; CP000100; ABB58548.1; -; Genomic_DNA. DR RefSeq; WP_011378498.1; NZ_JACJTX010000001.1. DR AlphaFoldDB; Q935Y7; -. DR SMR; Q935Y7; -. DR STRING; 1140.Synpcc7942_2518; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR PaxDb; 1140-Synpcc7942_2518; -. DR GeneID; 76401243; -. DR KEGG; syf:Synpcc7942_2518; -. DR eggNOG; COG0297; Bacteria. DR HOGENOM; CLU_009583_18_2_3; -. DR OrthoDB; 9808590at2; -. DR BioCyc; SYNEL:SYNPCC7942_2518-MONOMER; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000889800; 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; Reference proteome; KW Transferase. FT CHAIN 1..465 FT /note="Glycogen synthase" FT /id="PRO_0000188653" FT BINDING 15 FT /ligand="ADP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:57498" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00484" FT CONFLICT 33..34 FT /note="LG -> SA (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" FT CONFLICT 38 FT /note="R -> G (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="P -> R (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="N -> T (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" FT CONFLICT 251..252 FT /note="DK -> IA (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="K -> R (in Ref. 1; AAL03921)" FT /evidence="ECO:0000305" SQ SEQUENCE 465 AA; 53347 MW; F49F080B462B922B CRC64; MRILFVAAEC APFAKVGGMG DVVGSLPKVL KALGHDVRIF MPYYGFLNSK LDIPAEPIWW GYAMFNHFAV YETQLPGSDV PLYLMGHPAF DPHRIYSGED EDWRFTFFAN GAAEFSWNYW KPQVIHCHDW HTGMIPVWMH QSPDISTVFT IHNLAYQGPW RWKLEKITWC PWYMQGDSTM AAALLYADRV NTVSPTYAQQ IQTPTYGEKL EGLLSFISGK LSGILNGIDV DSYNPATDTR IVANYDRDTL DKRLNNKLAL QKEMGLEVNP DRFLIGFVAR LVEQKGIDLL LQILDRFLSY SDAQFVVLGT GERYYETQLW ELATRYPGRM STYLMYDEGL SRRIYAGSDA FLVPSRFEPC GITQMLALRY GSVPIVRRTG GLVDTVFHHD PRHAEGNGYC FDRYEPLDLY TCLVRAWESY QYQPQWQKLQ QRGMAVDLSW KQSAIAYEQL YAEAIGLPID VLQEA //