ID   GLGA_STRE4              Reviewed;         476 AA.
AC   C0M712;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=SEQ_0913;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(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}.
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DR   EMBL; FM204883; CAW93423.1; -; Genomic_DNA.
DR   RefSeq; WP_012679389.1; NC_012471.1.
DR   AlphaFoldDB; C0M712; -.
DR   SMR; C0M712; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; CAW93423; CAW93423; SEQ_0913.
DR   KEGG; seu:SEQ_0913; -.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   OMA; TWCPWYM; -.
DR   OrthoDB; 83240at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001365; 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..476
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000190083"
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;  53670 MW;  B3191E133E27F6AE CRC64;
     MKIMFVAAEG APFAKTGGLG DVIGALPKSL VKNGHEVSVI LPYYDVVDQA FGQQVEDVLY
     FYTQVGWRRQ YVGIKKLVKD KVTFYFIDNQ GYFFRGRIYG DWDDGERFAY FQLAAIEAME
     KIGVIPDILH VHDYHTAMIP FLLKEKYHWI QAYQAIRTVF TIHNIAFQGQ FDPGMLGDLF
     DVGIERYEDG TLRWHDCLNW MKAAVLYADR VTTVSPSYAH EIQTPAFGQG LDQVMRMEAG
     KLSGIVNGID TDLFNPARDP HLPASFSAED LSGKAATKQA LQERLGLPVR ADVPLIGMVS
     RLTDQKGFQL VLEELPHILQ QDVQLVLLGT GDPDYEAAFS WFAKAYPEKL SANITFDLPL
     AQQIYGACDL FLMPSAFEPC GLSQMMAMRY GAIPIVHEIG GLKDTVASYN AYEKTGTGFG
     FDQFSGFWLT QTLLFALDIY HNHKEDWQTI QQHAMTKDFS WDTASLAYLD LYKSLL