ID   GLGA2_SYNJB             Reviewed;         513 AA.
AC   Q2JKU0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Glycogen synthase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00484};
GN   Name=glgA2 {ECO:0000255|HAMAP-Rule:MF_00484};
GN   OrderedLocusNames=CYB_1734;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000240; ABD02691.1; -; Genomic_DNA.
DR   RefSeq; WP_011433335.1; NC_007776.1.
DR   AlphaFoldDB; Q2JKU0; -.
DR   SMR; Q2JKU0; -.
DR   STRING; 321332.CYB_1734; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   KEGG; cyb:CYB_1734; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_3; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001938; 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..513
FT                   /note="Glycogen synthase 2"
FT                   /id="PRO_0000241803"
FT   REGION          475..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   513 AA;  58218 MW;  CEBAAB84167C71CC CRC64;
     MVQAKILFAA AEAAPLAKVG GMADVVGSLP VVLRKLGQDV RIIMPLYGFL WDKFGQEPGQ
     YPRSKDPIWS KQVMGQVADI YESVLPGTDV PLYLVSHYCF APHRIYYGED EFWRFTFFAN
     AVAEFAWTYY PWKPNIIHCH DWHTGMIPAW MHQAPDIGTV FTIHNLAYQG PWRWQLERMT
     WLPWYFSAHN TMAAGILYAD QVNTVSPTYA MEIRTPLHGE GLQDLLAWKG ERLRGILNGI
     DIDRFDPRTD PDLEANFSID DLSGRAANKA TLQAKLGLTV NPDTFLMGMV ARLVEQKGID
     LLIQALDRFL DYSDAQFVLL GGSGEAYYEG RIREMAERHP GKMAYQKGYQ PKLAQLIYGG
     ADAFLMPSRF EPCGISQMIA MRYGCVPIVR RTGGLVDTVS HHIPSKGIGT GYCFDRYEAL
     DFYTCLARAW EAFQHKETWQ ALQKRGMASD FSWHRSALEY LRMYELILNL PLLPEKPPEP
     PNSPSSSPPK LKKPISSQPR SKGIPELQQR PEE
//