ID   GLGA_CLOAB              Reviewed;         477 AA.
AC   Q97GX6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=CA_C2239;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80196.1; -; Genomic_DNA.
DR   PIR; A97176; A97176.
DR   RefSeq; NP_348856.1; NC_003030.1.
DR   RefSeq; WP_010965537.1; NC_003030.1.
DR   AlphaFoldDB; Q97GX6; -.
DR   SMR; Q97GX6; -.
DR   STRING; 272562.CA_C2239; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   GeneID; 44998718; -.
DR   KEGG; cac:CA_C2239; -.
DR   PATRIC; fig|272562.8.peg.2440; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000814; 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..477
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188607"
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   477 AA;  55070 MW;  974122C6A46FAAD6 CRC64;
     MKILFASSES YPFIKTGGLG DVSYALPKAL RKIGIDARVI IPKYSDIPEY FRYNTHHIAS
     FGVPVGWRSQ YGGLEYYEYD GVPFYFIDND YYFKRSGLYG YYDDGERFAY FSRGVLQAIT
     YMQDFNPDII QCNDWQTAII PVLLKDHYRN YRNYNHIKTI FTIHNLKYQG VFGKSVLGEL
     LCLNEGYYNE NALKFYDGIS FMKGGILFSD KLSTVSRTYA EEIKDPYYGE HLDGLLRSRS
     YDLWGIVNGI DYDILNPETD KDLFFNFDSS TLYNKTKNKI ELQKMLNLPV SENIPMIGIV
     SRLVSQKGLD LISCVLEDLL QDGIQLVVLG TGDAKYENMF KYFAWKYPNK LSANIQFNNS
     LAQKIYGASD MFLMPSKFEP CGIGQLIALR YGSLPIVRET GGLKDTVRPF NPITGEGNGF
     SFTNYNAHDM LHVIRNAEYF YYNEKYNWNK LVQTAMNDDN SWSKSAEIYR NLYMSVL
//