GLGA2_GEOMG
ID GLGA2_GEOMG Reviewed; 484 AA.
AC Q39QT6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glycogen synthase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00484};
GN Name=glgA2 {ECO:0000255|HAMAP-Rule:MF_00484}; OrderedLocusNames=Gmet_3175;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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; CP000148; ABB33388.1; -; Genomic_DNA.
DR RefSeq; WP_004513892.1; NC_007517.1.
DR AlphaFoldDB; Q39QT6; -.
DR SMR; Q39QT6; -.
DR STRING; 269799.Gmet_3175; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR EnsemblBacteria; ABB33388; ABB33388; Gmet_3175.
DR KEGG; gme:Gmet_3175; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_2_7; -.
DR OMA; TWCPWYM; -.
DR OrthoDB; 83240at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000007073; 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 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 Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
PE 3: Inferred from homology;
KW Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..484
FT /note="Glycogen synthase 2"
FT /id="PRO_0000230242"
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 484 AA; 53848 MW; 949EE76DFB6096BD CRC64;
MKILQVASEV APLAKTGGLA DVVAALPKEL RRMGHDVRVA IPFYKEVSSG NLPVRKARKS
AEVALGGELH KGYLRQTALG EVPVYLVENR DLFGRDHLYG PPEGDYPDNP LRFAFFCRSV
LQFLKRMDFR PDVIHCHDWQ SALIPIILKY ELGHDPFFNR TAVIFTIHNL AYQGVFPADA
LAQTGLDPSL FSVDRIEFYG RINLLKGAIL AADAITTVSE TYCHEILSPG QGCGLEGVLE
RRQADLAGIL NGLDSEEWNP SLDRRIFRNY SSKSLAGKGA DKRELQRELG LKAGASIPII
GMVGRIVEQK GIDLVIDLLP RFAAEELQLV ILGTGDLRLM HQLHEFRNKG VKNVSINLGF
KEPLAPKIYA GCDMFLMPSR FEPCGLSQLI ALSYGTVPIV RRTGGLADTV IDVTANPREG
NGFSFTEFSA DACWDAVQRA LAAYRDREGW RKIMRRGMLR DVSWRSAAGK YEELYRTCAD
NRRG
