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 27-MAR-2024, entry version 86.
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; Pseudomonadota; 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 KEGG; spt:SPA3386; -.
DR HOGENOM; CLU_009583_18_4_6; -.
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 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; 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
//
