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GLGA_BACCZ
ID   GLGA_BACCZ              Reviewed;         476 AA.
AC   Q632H4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 83.
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=BCE33L4618;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU15655.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000001; AAU15655.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041184963.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q632H4; -.
DR   SMR; Q632H4; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; AAU15655; AAU15655; BCE33L4618.
DR   KEGG; bcz:BCE33L4618; -.
DR   PATRIC; fig|288681.22.peg.743; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002612; 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_0000188593"
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;  54867 MW;  76E0BA0429361C2D 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 YITAQYDAGS LYEKNENKRA LQRYFGLPEK EDTPIISMVT
     RLTKQKGLDL VRTVFREIME EDVQCIILGS GDSEYEQFFE WMAYEYPEKV KVYIGFNEEL
     AHQVYAGSDL FLMPSLFEPC GLGQLIALAY GTIPIVRETG GLNDTVQSYD EETGEGNGFS
     FTNFNAHDML HTVLRAIEFY HDKPVWEQLV KQAMTEDYSW EKSALAYKKL YKGLME
 
 
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