GLGA2_SYNJB
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 03-AUG-2022, entry version 88.
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}; OrderedLocusNames=CYB_1734;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified 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 OMA; TWCPWYM; -.
DR OrthoDB; 83240at2; -.
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 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; 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