GLGA_STRS7
ID GLGA_STRS7 Reviewed; 476 AA.
AC C0MH77;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=SZO_11710;
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAW99616.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MH77; -.
DR SMR; C0MH77; -.
DR EnsemblBacteria; CAW99616; CAW99616; SZO_11710.
DR KEGG; seq:SZO_11710; -.
DR PATRIC; fig|40041.11.peg.1236; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_2_9; -.
DR OMA; TWCPWYM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001368; 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..476
FT /note="Glycogen synthase"
FT /id="PRO_1000206434"
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 476 AA; 53641 MW; F411923BCD9DA7F0 CRC64;
MKIMFVAAEG APFAKTGGLG DVIGALPKSL VKNGHEVFVI LPYYDVVDQA FGHQVEDVLY
FYTQVGWRRQ YVGIKKLVKD KVTFYFIDNQ AYFFRGRIYG DWDDGERFAY FQLAAIEAME
KIGVIPDILH VHDYHTAMIP FLLKEKYHWI QAYQAIRTVF TIHNIAFQGQ FDPGMLGDLF
GVGIGRYEDG TLRWHDCLNW MKAAVLYADR VTTVSPSYAH EIQTPAFGQG LDQVMRMEAG
KLSGIVNGID TDLFNPARDP HLPASFSAED LSGKAATKQV LQERLGLPVR ADVPLIGMVS
RLTDQKGFQL VLEELSHILQ QDVQLVLLGT GDPDYEAAFS WFAKAYPEKL SANITFDLPL
AQQIYGACDL FLMPSAFEPC GLSQMMAMRY GAIPIVHEIG GLKDTVASYN AYEKTGTGFG
FDQFSGFWLT QTLLFALDIY HNHKEDWQTI QQHAMTKDFS WDTASLAYLD LYKSLL