ID   GLGA_CERS5              Reviewed;         478 AA.
AC   A4WRM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   10-JUN-2026, entry version 94.
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=Rsph17025_1135;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000661; ABP70036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WRM2; -.
DR   SMR; A4WRM2; -.
DR   STRING; 349102.Rsph17025_1135; -.
DR   KEGG; rsq:Rsph17025_1135; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_4_5; -.
DR   BioCyc; RSPH349102:G1G8M-1163-MONOMER; -.
DR   UniPathway; UPA00164; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0009011; F:alpha-1,4-glucan glucosyltransferase (ADP-glucose donor) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004373; F:alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity; IEA:InterPro.
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; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   NCBIfam; NF001899; PRK00654.1-2; 1.
DR   PANTHER; PTHR45825:SF11; ALPHA AMYLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   Pfam; PF13692; Glyco_trans_1_4; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..478
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000014382"
FT   BINDING         20
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   478 AA;  51183 MW;  3C24927FAECF1D64 CRC64;
     METARGRVLS VASECVPLLK TGGLADVVGA LPGALAAEGW EMRVLMPCYR PLRWRLEQME
     EVFSEEDLFG GRGRVMAGEV AGRRMLLLDA PHLYDREGGP YAGPWGDWGD NAQRFAALSW
     IAARIAREGL SDGWRPEVLH AHDWQAGFAP AYLAYWGSGG VRSVLTVHNI AFQGWAPAAL
     LPSLRLPASE FHPAALEYYG GLSSLKAGLV TADHITTVSP TYACELMRPE FGMGLQGVIA
     ARAGQVSGIL NGVDTDIWSP EAEERPYTAR SLKAKAENRA VLSGAFKLDV PGPLAILVSR
     LTYQKGIDLI PEVLPDFIAA GGGLAVLGTG DAALEGAMRE LEVRFSGRVG VRIGYDEGLS
     HLMFAGGDAV LVPSRFEPCG LTQMYGLRYG AIPVVALTGG LADTIINANP AALTAGCATG
     LTFHPTEPPA FAEALRRLIH LYADHALWEK VQKNAMRHPV GWQTSAAAYA ALYRELVA
//