ID   GLGA_STRMU              Reviewed;         476 AA.
AC   Q8CWX0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=SMU_1536;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59186.1; -; Genomic_DNA.
DR   RefSeq; NP_721880.1; NC_004350.2.
DR   RefSeq; WP_002262948.1; NC_004350.2.
DR   AlphaFoldDB; Q8CWX0; -.
DR   SMR; Q8CWX0; -.
DR   STRING; 210007.SMU_1536; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   GeneID; 66819073; -.
DR   KEGG; smu:SMU_1536; -.
DR   PATRIC; fig|210007.7.peg.1368; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   OrthoDB; 9808590at2; -.
DR   PhylomeDB; Q8CWX0; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002512; 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..476
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188648"
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;  54312 MW;  A2C0C078C3E3F3B4 CRC64;
     MKILFVAAEG APFAKTGGLG DVIGALPKSL VKNNNEVSVI LPYYDVVDAK FGDQIEDLFY
     FFTNVGWRRE YVGIKHIFRD GVDFYFIDNK HYFYRGQIYG EFDDGERFAY FQLAALEAME
     KIQFIPDILH VHDYHTAMIP YLLKEKYHWI NAYHGIKTVF TIHNIEFQGQ FNPSMLGELF
     GVGDERYRDG TLRWNDCLNW MKAAVLYADR VTTVSPSYAK EIMTPEFGKG LDQIMRMESG
     KLSGVVNGID TDLFDPETDP HLAVHFSKDD LSGKAKNKAA LQERVGLPVR EDVPLVGIVS
     RLTDQKGFQL VVDQLNTMMQ LDLQIVLLGT GYADFENAFA WFGHAYPDKM SANITFDLEL
     AQQIYAASDI FLMPSAFEPC GLSQMMAMRY GTLPLVHEVG GLRDTVIPYN EFEKTGTGFG
     FQDFSGYWLT KTLEAALDVY YNRKEDWKIL QKNAMTTDFS WDTASQSYEH LYKELA
//