ID   GLGA_SALPA              Reviewed;         477 AA.
AC   Q5PM09;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=SPA3386;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79199.1; -; Genomic_DNA.
DR   RefSeq; WP_001197669.1; NC_006511.1.
DR   AlphaFoldDB; Q5PM09; -.
DR   SMR; Q5PM09; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; AAV79199; AAV79199; SPA3386.
DR   KEGG; spt:SPA3386; -.
DR   HOGENOM; CLU_009583_18_4_6; -.
DR   OMA; TWCPWYM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008185; 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..477
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000230262"
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;  52946 MW;  004D2E49B6AA380D CRC64;
     MQVLHVCSEM FPLLKTGGLA DVIGALPAAQ IADGVDVRVL LPGFPDIRRG IPDAHVVSRR
     DTFAGKISLL FGHYNGVGIY LIDAPHLYER PGSPYHDTNL YAYTDNVLRF ALLGWVGCEM
     ACGLDPFWRP DVVHAHDWHA GLAPAYLAAR GRPAKSVFTV HNLAYQGMFY AKHMDDIELP
     WSFFNMHGLE FNGQLSFLKA GLYYADHITA VSPTYAREIT EPQFAYGMEG LLRQRHLEGR
     LSGILNGVDE KIWNPESDLL LASRYTRDTL EEKAENKRQL QIAMGLKVND KVPLFAVVSR
     LTNQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEHPGQVG VQIGYHEAFS
     HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG LADTVSDSSL ENLADGIASG
     FVFEDSNAWS LLRAIRRAFV LWSRPSLWRF VQRQAMAMDF SWQVAAKSYR ELYYRLK