ID   GLGA_LACP3              Reviewed;         481 AA.
AC   Q036T0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=LSEI_2037;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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}.
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DR   EMBL; CP000423; ABJ70792.1; -; Genomic_DNA.
DR   RefSeq; WP_003566617.1; NC_008526.1.
DR   RefSeq; YP_807234.1; NC_008526.1.
DR   AlphaFoldDB; Q036T0; -.
DR   SMR; Q036T0; -.
DR   STRING; 321967.LSEI_2037; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; ABJ70792; ABJ70792; LSEI_2037.
DR   KEGG; lca:LSEI_2037; -.
DR   PATRIC; fig|321967.11.peg.2001; -.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   OMA; TWCPWYM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001651; 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..481
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000014367"
FT   BINDING         16
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   481 AA;  53996 MW;  079C74DEC1C6D7CB CRC64;
     MLKVLFTAAE SAPFYKTGGL GDVTYALPKA IKKQGVDIRV AIPFYEKKFP AKYLPKVKDL
     THFTLEMDGR PVYVGLKTIK LGDVTYYLID NRQYFDRDGL YGYWDDGGRF GYFQMAVIEM
     LQVIEWIPDV IHANDWHTAF IPVLLKEKYG WIKPYQQIKT QLTIHNLQFQ GWFPPSTLAT
     VFGIGREGFN DDGFGQDGSI NWLKGGINYA DLVSTVSPSY AKEIQTPAFG EHLDGTLRKQ
     SGKLVGILNG IDSEVYNPAT DQNLAYNYDA KNLAGKAKDK KALQDEMHLP KRTDPLFAMV
     SRLTRQKGAD LLVDALENFL VQNNVQVVVL GTGDQDLEED LSSLQDRFPG QLAVRIDFDE
     GLAQRIYAGA DYFMMPSAFE PSGLAQMMAM RYGTLPIVHE TGGLRDSVLA YNAETGAGDG
     FSFWDYNAGV LTNILRMAKS VYADQPKVYA KLQQHAMVKD FDWHHSAAEY LKGYQRILGK
     A