GLGA_GRABC
ID GLGA_GRABC Reviewed; 480 AA.
AC Q0BPL3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=GbCGDNIH1_2341;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(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; CP000394; ABI63239.1; -; Genomic_DNA.
DR RefSeq; WP_011633041.1; NC_008343.2.
DR AlphaFoldDB; Q0BPL3; -.
DR SMR; Q0BPL3; -.
DR STRING; 391165.GbCGDNIH1_2341; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR EnsemblBacteria; ABI63239; ABI63239; GbCGDNIH1_2341.
DR KEGG; gbe:GbCGDNIH1_2341; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_4_5; -.
DR OMA; TWCPWYM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001963; 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..480
FT /note="Glycogen synthase"
FT /id="PRO_1000014361"
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 480 AA; 52021 MW; 87FF3F3A763A72D3 CRC64;
MRVLNVASEA YPWIKTGGLA DVAGALPAAL AEHDVDMRTL LPAYAGLRQR PETRPVHHYA
DLFGGAASIL EARLTGGLTL YLLDAPHLYD RPGGPYTDAN GRDWADNAER FAAFCRAAAD
IALGILPDWT PDIVHAHDWQ AGLVPAYLAL SEASPRPPVL FTIHNLAFQG VVPRDRLAAL
LLPPDSFSVD GVEYYGQIGL LKAGLHYADA LTTVSPSYAR EIQTDTGGMG LGGLLRDRAA
VLNGLLNGID MTEWNPAHDP HVKAHFDRHS LEHRTINREA LRTRFGLDSS AGPLFGIVSR
LTGQKGIDLV LNALPFLISQ QAQLVVLGSG DKGLEQGLLQ AAQTHPRQIA VFSGYDEALS
RQIFSGADAM LIPSRFEPCG LTQLYAMRYG AVPIVSRVGG LADTIIDANT AACEAGVATG
LMFQPDGEDS LIEPLSRAIR LFHQAEIWER LQHRGMETDS SWTLRSTAYV ALYTRLLSLR