ID   GLGA_GEOTN              Reviewed;         485 AA.
AC   A4IS20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   02-SEP-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=GTNG_2779;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae;
OC   Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO68124.1; -; Genomic_DNA.
DR   RefSeq; WP_011888027.1; NC_009328.1.
DR   AlphaFoldDB; A4IS20; -.
DR   SMR; A4IS20; -.
DR   KEGG; gtn:GTNG_2779; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_9; -.
DR   UniPathway; UPA00164; -.
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; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   NCBIfam; NF001898; PRK00654.1-1; 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; 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..485
FT                   /note="Glycogen synthase"
FT                   /id="PRO_1000014360"
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   485 AA;  56262 MW;  1DFF45594E5A12DA CRC64;
     MKVLFAVSEC APFAKSGGLA DVAGALPKEL RRLGIDARVM LPKYETIAPE WKKKMKKVAE
     LIVPVGWRRQ YCGVEELRHD GVIYYFIDNE YYFKRPQLYG HYDDGERFAY FCRAVLEVLP
     EIQFQPDVIH CHDWHTGMVP FLLREQYRHE LFYVDMRTVF TIHNLQFQGL FPRGILEDLL
     NLDGRYFTVD HLEFYGCVSF MKGALVASDL ITTVSPTYKE EIQTAYYGER LDGLLRARRD
     DLLGILNGID DEFYNPEADP FLTATYSVHT RERKQLNKRA LQRQFGLPEW DDVPLIAMVT
     RMTAQKGLDL VTCVFHEMMS EDMQLVVLGT GDWRFEQFFS QMAAAYPGKV GVYIGFHEPL
     AHQIYAGADL FLMPSLFEPC GLSQMIALRY GTIPIVRETG GLNDTVQSYN EITKEGNGFS
     FTNFNAHDML YTIRRALSFY RQPSVWEQLT ERAMRGDYSW RRSANQYKQA YEQLIKKEEH
     TLVHG
//