ID   GLGA_CHLMU              Reviewed;         474 AA.
AC   Q9PLC3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=TC_0181;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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}.
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DR   EMBL; AE002160; AAF39055.1; -; Genomic_DNA.
DR   PIR; A81732; A81732.
DR   RefSeq; WP_010229734.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PLC3; -.
DR   SMR; Q9PLC3; -.
DR   STRING; 243161.TC_0181; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; AAF39055; AAF39055; TC_0181.
DR   GeneID; 1246306; -.
DR   KEGG; cmu:TC_0181; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_3_0; -.
DR   OMA; TWCPWYM; -.
DR   OrthoDB; 83240at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000800; 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   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   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR02095; glgA; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..474
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188603"
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   474 AA;  53234 MW;  823FDE6E12F35B1E CRC64;
     MKITHTAIEF APVIKAGGLG DALYGLAKAL AVNHTTEVVI PLYPKLFTSL HEQDLFATQK
     IPYFFAGEQE ATAFSYFYEG IKVTLLKLDS QPELFEEAET IYTNDDAFRF CAFSAAAAAY
     IQKEGADIVH LHDWHVGLVA GLLKQQPCPQ LQKIVLTLHN FGYRGYTTRE VLEASSLNEF
     YLSHYQLFRD PQTCVLLKGA LYCSDFVTTV SPTYAKEILQ DYSDYEIHDA ITARQHHLKG
     ILNGIDYTIL DPETDPHLAK NYSKVLFEDP KAFFEAKAEN KKALYETLGL SLDKSPCMCI
     ISRIAEQKGP EFMKQAILHA LENAYTLIII GTCYGGQIHK EFSNLQESLA DSPNVRILLT
     YSDVLARQIF AAADMICIPS MFEPCGLTQM IGMRYGTVPV VRATGGLADT VTDGVNGFSF
     SNPHDFHEFR NMLSKAIATY RDDQDKWQQI VRSCLEFSSD LETAANKYLE IYQQ