ID   GLGA_BACCQ              Reviewed;         476 AA.
AC   B9J2G5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=BCQ_4682;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(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; CP000227; ACM15108.1; -; Genomic_DNA.
DR   RefSeq; WP_012644674.1; NC_011969.1.
DR   AlphaFoldDB; B9J2G5; -.
DR   SMR; B9J2G5; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; ACM15108; ACM15108; BCQ_4682.
DR   KEGG; bcq:BCQ_4682; -.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   OMA; TWCPWYM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000441; 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_1000135645"
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;  54998 MW;  5A2F6CF2627E8E41 CRC64;
     MNILFAVSEC VPFVKSGGLA DVAGALPKEL KKLGVEVRII LPNYSLIPQK LRDGCTLHKV
     INVPLGWRNQ YCGILKGEQD GITYYLIDNE YYFKRDSLYG HYDDGERFSY FSKAVLECIP
     HLDFEVDVLH SHDWHTAMVN FLLREKYQDN PLYEHIKTVY TIHNLQFQGV FPPEVMYDLL
     ELGDEYFHSE QLEFYGNVNF MKGGIIASDQ ITAVSPTYKE EIQYEFFGEK LDGLLRKYND
     KLSGIVNGID TSVYNPETDS YITAQYDADS LYEKNENKRA LQRYFGLPEK EDTPIISMVT
     RLTKQKGLDL VRTVFREIME EDVQCIILGS GDSEYEQFFE WMAYEYPEKV KVYIGFNEEL
     AHQVYAGSDL FLMPSLFEPC GLGQLIALAY GTIPIVRETG GLNDTVQSYD EETGEGNGFS
     FTNFNAHDML HTVRRAIEFY HDKPVWEQLV KQAMTEDYSW EKSALAYKKL YKSLME