GLGA_RHOBA
ID GLGA_RHOBA Reviewed; 507 AA.
AC Q7UPY2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=RB6654;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294144; CAD74926.1; -; Genomic_DNA.
DR RefSeq; NP_867380.1; NC_005027.1.
DR RefSeq; WP_011121026.1; NC_005027.1.
DR AlphaFoldDB; Q7UPY2; -.
DR SMR; Q7UPY2; -.
DR STRING; 243090.RB6654; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR EnsemblBacteria; CAD74926; CAD74926; RB6654.
DR KEGG; rba:RB6654; -.
DR PATRIC; fig|243090.15.peg.3224; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_5_0; -.
DR InParanoid; Q7UPY2; -.
DR OMA; TWCPWYM; -.
DR OrthoDB; 83240at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001025; 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..507
FT /note="Glycogen synthase"
FT /id="PRO_0000188640"
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 507 AA; 56321 MW; A07EAB782F891BCA CRC64;
MNIVYLTTEA VPFAKTGGLA DVCGTLPKVV AAQGHRCAVI MPAFSSIERS LQPIETTDIS
FAVPMSDQKL IGCRLLKSHL PKDPNDPEDS AEVPVYFIDQ PQYFRRPSLY GDANGDYHDN
AERFIFYCRA AIIAMTRLGY PVDLVHCNDW QSALVPALLR AASDNVAKTQ PIATMLSIHN
MAYQGNFGFD AFPWTGLSWD HFRPESFEYY NQLNFLKTGV VTSDVVSTVS PTYALEIQTP
EYGCGLDSIL QGIPQPVAGI INGIDTNIWN PETDPHLKRN YSVVDWADAK IDNKLALQAE
VGLPQDPDVP LLGLIGRLAD QKGWDLILPV LKQHLAEARP TQWVVLGSGD PKIEEQLREL
TEQHPEQLAA YIGFSDALAH RIEASSDMFI MPSHYEPCGL NQLYSLRYGT PCVVTKTGGL
ADTIVDATPE NVAANLATGF HLNDSSAGAL DHAINRALQL RYHSPEKWKN LVEFGMSQDW
TWRKSADQYI QLYARTISLN RRRRSGS