ID   GLGA_PARC0              Reviewed;         508 AA.
AC   A1TRG5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Aave_2986;
OS   Paracidovorax citrulli (strain AAC00-1) (Acidovorax citrulli).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; CP000512; ABM33553.1; -; Genomic_DNA.
DR   RefSeq; WP_011796063.1; NC_008752.1.
DR   AlphaFoldDB; A1TRG5; -.
DR   SMR; A1TRG5; -.
DR   STRING; 397945.Aave_2986; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   GeneID; 79792667; -.
DR   KEGG; aav:Aave_2986; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_4_4; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002596; 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..508
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000014336"
FT   REGION          483..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   508 AA;  54360 MW;  76C98385279F7D48 CRC64;
     MKILFATSEC APLVKTGGLG DVSAALPPAI AALGHEVMLL MPAYADMPLQ GNITGWHSLP
     AEGPWPAAQL LRVDRGGHEV PLLLLSCPQL YARGGSPYAS AQGDHPDNAL RFGLLAHVAA
     RIGTPQSPCG WTADIVHAND WPTALAPLYL RQFRDAAGPR GDAVARSMVT VHNLAFQGVF
     PMDWAQRLGI EDRHLGIEGA EFWGQLSMLK AGLQYADAIT TVSPTYAREI QTPELGFGLD
     GVLRARAGRL QGILNGIDTA LWNPSQDTLI PAPFSADRLE GKAACKAALR RTLGLAQDGD
     RMLFGLVGRM TEQKGIDWVI GGAERLLRQG GQLAILGSGD PALESALRAL AKRHPRHMHV
     TVGFDESLAH GIEAGSDSFL MPSRFEPCGL NQMYSQAYGT PPVVTPTGGL ADSVTDADDP
     AGNGTGFVLR GSSQAAFDQA VGRALHLWKT APDAWRRLQR NGMQRDFGWT ASARAYVQAY
     GAARNRAETR PQTASALSYR EPRPAAEY
//