ID   GLGA_BURTA              Reviewed;         533 AA.
AC   Q2T6R2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 76.
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=BTH_II0940;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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=ABC33934.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000085; ABC33934.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_009896325.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2T6R2; -.
DR   SMR; Q2T6R2; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; ABC33934; ABC33934; BTH_II0940.
DR   KEGG; bte:BTH_II0940; -.
DR   HOGENOM; CLU_009583_18_4_4; -.
DR   OrthoDB; 83240at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001930; Chromosome II.
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..533
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000241790"
FT   REGION          497..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   533 AA;  57466 MW;  D5E03E9D51985633 CRC64;
     MFVASEAFPL AKTGGLADVC ASLPKALRAL GCDVRVLMPG YAQALDRVLR PRVVAELGEV
     LPGAAVRIIA GSMPDSGVPV WLLDCPSLYR RAGSLYCGPD DADWADNAYR FGLLCQVAAR
     VALGAAGLRW RPDVVHAHDW HGGLVALLTR GAGDARPKTV FTIHNAAFQG NFALDDAARI
     GLPADALSVD GVEFYGQLSF LKAGARYADR LTTVSPTYAG EIQTAEFGCG LEGLYAARRD
     QLSGIMNGID TELWNPATDR WLPQPYSIDD MGGKAGCKAA LQQELGLCAD ARAPLVASVC
     RLTSQKMSDI VLERLPEQLA QHPRMQFALH GRGDRALEQG FDALAAQYPR RVAVRIGYDE
     TLAHRIHAGA DILLHGARFE PCGLTQLYAM RYGTIPIVRR VGGLADSVVD LDTLAPHSED
     ATGFVFDAPT GDAMSEALRR CVNLHDARPG VWSALCRLAM ARDSSWSRSA RAYLDLYAAL
     TPRRRVEASD EARGAAAALA RADAASGRRR RAPEQSERLR QERLARQVAL ASK