ID   GLGA_PARUW              Reviewed;         500 AA.
AC   Q6MAS9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=pc1596;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(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; BX908798; CAF24320.1; -; Genomic_DNA.
DR   RefSeq; WP_011176142.1; NC_005861.2.
DR   AlphaFoldDB; Q6MAS9; -.
DR   SMR; Q6MAS9; -.
DR   STRING; 264201.pc1596; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   KEGG; pcu:PC_RS07650; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_3_0; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000529; 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; PTHR46083; -; 1.
DR   PANTHER; PTHR46083:SF1; GLYCOGEN SYNTHASE 2-RELATED; 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..500
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188627"
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   500 AA;  58201 MW;  52FD3869D894BC30 CRC64;
     MHIIHIASEL APLAKVGGLA DVVLGLCREL SWKGHDVDII IPKYDCMDSE QIRDLTVDYF
     ELPSFYNGEW FFNTVWMGWV ENLKVYFIEP HHPRFFFNRG CFYGCEDDLE RFLYFSRTAL
     EFLYKKSILP DIIHLHDWQT AVIAPLYKDM YQKLGYTKPK ILFTIHNMEY QGKCAAHDLN
     YIGLDGNRYQ QHSFMQDNLY PHLINLLKGG IVYSDFVTTV SPNYAKEVLT PKEGRGLEAT
     LVEYQHKFKG ILNGIDYSYW NPEIDRFLPA HYSLREMPKN KKDRNTVDKK GFIKKILREK
     LYLAEEHRPI IGCITRLVPQ KGIDLIKHTI RHIVEKKGQF ILLGSSPIPS INDEFHRLKH
     QYTDHPHIHL ILHHSEELAH LIYAGSDMFI VPSLFEPCGL TQIIALKYGT VPIVRRTGGL
     ADTIIDVDHT DQQPDKKNGY VFDDPDANGI DSAIDRAIHC WFEEPEKWRQ LMLNGMKMDF
     SWNQSSDCYL KIYQAISAKN
//