ID   GLGA_PARDP              Reviewed;         467 AA.
AC   A1BAE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Pden_4426;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
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; CP000490; ABL72490.1; -; Genomic_DNA.
DR   RefSeq; WP_011750652.1; NC_008687.1.
DR   AlphaFoldDB; A1BAE6; -.
DR   SMR; A1BAE6; -.
DR   STRING; 318586.Pden_4426; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; ABL72490; ABL72490; Pden_4426.
DR   GeneID; 75503805; -.
DR   KEGG; pde:Pden_4426; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_4_5; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000361; Chromosome 2.
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..467
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000014371"
FT   BINDING         16
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   467 AA;  49189 MW;  51A08DB13360B472 CRC64;
     MTRVLSVASE CVPLVKTGGL ADVAGALPAA LAGQGVGMRV LLPGYPAVLG AAAKTPVLRE
     IPDLFGGPAR IRRGALGKAV LYILDAPHLF DRPGGIYLGP DGRDWPDNPQ RFAALCKAAA
     LIAAEGVEDW RPQVLHLHDW QAGLTPIYLR QAGVRDVRTL LTIHNIAFQG LAPAHMLSAL
     QLPAHLFNPS GFEYWGRISA LKAGIVFADK VSTVSPTYAE ELMTPEFGMG MEGVLADRAG
     DFTGILNGID LDAWKPPYAT PQGKAPHRAA LRKEFGLPET DGPLCVVVSR LTGQKGLDLL
     IEALPALLEN GGQLAVLGSG DPGLEAAFAK AAARHAGVAL RLGYDEALSR RMIAGGDAIL
     VPSRFEPCGL TQLYGLRFGT LPLVALTGGL ADTVINASVA GLAAGVATGV QFHPVDARTL
     SRALTRLCAL WHQPAAWQRM MDNAMAHPVG WDASARAYAE LFEAMAA
//