ID GLGA_SHIFL Reviewed; 477 AA.
AC Q83PV4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=SF3452, S4311;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44912.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19269.1; -; Genomic_DNA.
DR RefSeq; NP_709205.1; NC_004337.2.
DR RefSeq; WP_001197654.1; NZ_WPGW01000010.1.
DR AlphaFoldDB; Q83PV4; -.
DR SMR; Q83PV4; -.
DR STRING; 198214.SF3452; -.
DR PaxDb; 198214-SF3452; -.
DR GeneID; 1026461; -.
DR KEGG; sfl:SF3452; -.
DR KEGG; sfx:S4311; -.
DR PATRIC; fig|198214.7.peg.4072; -.
DR HOGENOM; CLU_009583_18_2_6; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..477
FT /note="Glycogen synthase"
FT /id="PRO_0000188645"
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 477 AA; 52781 MW; C9B18973AD08414E CRC64;
MQVLHVCSEM FPLLKTGGLA DVIGALPAAQ IADGVDARVL LPAFPDIRRG VTDAQVVSRR
DTFAGHITLL FGHYNGVGIY LIDAPHLYDR PGSPYHDTNL FAYTDNVLRF ALLGWVGAEM
ASGLDPFWRP DVVHVHDWHA GLAPAYLAAR GRPAKSVFTV HNLAYQGMFY AHHMNDIQLP
WSFFNIHGLE FNGQISFLKA GLYYADHITA VSPTYAREIT EPQFAYGMEG LLQQRHREGR
LSGVLNGVDE KIWSPETDLL LASRYTRDTL EDKAENKSQL QIAMGLKVDD KVPLFAVVSR
LTSQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEYPGQVG VQIGYHEAFS
HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG LADTVSDCSL ENLADGVASG
FVFEDSNAWS LLRAIRRAFV LWSRPSLWRF VQRQAMAMDF SWQVAAKSYR ELYYRLK
//
