ID A0A0G1N4N5_9BACT Unreviewed; 457 AA.
AC A0A0G1N4N5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glycogen synthase {ECO:0000256|HAMAP-Rule:MF_00484};
DE EC=2.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00484};
DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|HAMAP-Rule:MF_00484};
GN Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN ORFNames=UX23_C0001G0093 {ECO:0000313|EMBL:KKU15494.1};
OS Parcubacteria group bacterium GW2011_GWB1_45_9.
OC Bacteria.
OX NCBI_TaxID=1618879 {ECO:0000313|EMBL:KKU15494.1, ECO:0000313|Proteomes:UP000034512};
RN [1] {ECO:0000313|EMBL:KKU15494.1, ECO:0000313|Proteomes:UP000034512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
CC {ECO:0000256|ARBA:ARBA00002764, ECO:0000256|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:0000256|ARBA:ARBA00001478, ECO:0000256|HAMAP-
CC Rule:MF_00484};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00484}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily.
CC {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|HAMAP-Rule:MF_00484}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKU15494.1}.
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DR EMBL; LCLK01000001; KKU15494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1N4N5; -.
DR PATRIC; fig|1618879.3.peg.102; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000034512; Unassembled WGS sequence.
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 PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR45825:SF11; 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 {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00484};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 5..245
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 267..432
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 18
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 457 AA; 50929 MW; 9ABAEF13C5B70979 CRC64;
MGKIKIFIAA AEASPLAKVG GLADVIGSLP KTLSKLGVQI TILLPKYKTI DEKKFKLIKT
KETVKVAFGG NTETLPLWRT TLPDSKVPII LFEHKSWISR GGIYATPSAE PSGHESELQR
FGVFSSAIAE YASKNGDSST ILHCNDWHVA LAIPIMRGLL RNKKVHALIT IHNLAYQGIY
SEKIALKILG KDIFSIIPKQ AKNKGNINLF ASGILASNWT STVSPTYREE ILKPENGAGL
DWALRAKKNK FVGILNGIDY KSWPPQKRFK TEKAFLCGMV SRIAEQKGFD ILLPAMLDVL
NKDKRIKFTI LGVGEPLYVA KLKKYTKQFA GRVTFINRFD EAAAQKIYAN SDAFLIPSRF
EPSGLGQMIS MRYGTLPIAR ATGGLKDTIN NLEDGFLFGP YSRQALADCI LRAAKLFFNN
PKKWNAMRKN AARKDFSWKK SALEYKKLFS EILQHKN
//
