ID   GLGA_THEVB              Reviewed;         474 AA.
AC   Q8DKU2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=tll0763;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Thermosynechococcaceae; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000039; BAC08314.1; -; Genomic_DNA.
DR   RefSeq; NP_681552.1; NC_004113.1.
DR   RefSeq; WP_011056608.1; NC_004113.1.
DR   AlphaFoldDB; Q8DKU2; -.
DR   SMR; Q8DKU2; -.
DR   STRING; 197221.gene:10747354; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; BAC08314; BAC08314; BAC08314.
DR   KEGG; tel:tll0763; -.
DR   PATRIC; fig|197221.4.peg.802; -.
DR   eggNOG; COG0297; Bacteria.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000440; 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..474
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188651"
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   474 AA;  54364 MW;  46FCDB64E5B7609B CRC64;
     MRILFVAAEA APLAKVGGMG DVVGSLPKVL RRMGHDVRIF MPYYGFLPDK VEIPKDPIWI
     GHAMFQTFHV YETVLPGSDV PLYLFGHPCF NPRRIYYGED EDWRFTFFAN GAAEFAWNYW
     KPQIIHCHDW HTGMIPVWMH QDPDITTVFT IHNLAYQGPW RWRLEQITWC PWYMQGHNTM
     AAALQYADRV NTVSPTYAEQ IKTPEYGEKL EGLLSFISGK LSGILNGIDT ELFDPSSDRA
     LAQNYTADTL ERRRANKIAL QEELGLEVNS GAFLVGMVSR LVEQKGLDLL IQILDRFLAY
     TDSQFVLLGT GDRYYETQMW QIASRFPGRC SVQLLYSDVL SRRIYGGADA FIMPSRFEPC
     GISQMIALRY GCVPIVRRTG GLVDTVSHHN PEQQTGTGYC FDRYEPLDFY TCLVRAWEGY
     RYKREWHALQ QRGMREDFSW TKSALAYNAL YNSIYGLPPE TMPNPSPTLV PAVT
//