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Database: UniProt
Entry: A0A0G1EQ97_9BACT
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ID   A0A0G1EQ97_9BACT        Unreviewed;       447 AA.
AC   A0A0G1EQ97;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=UV59_C0009G0003 {ECO:0000313|EMBL:KKS85201.1};
OS   Candidatus Gottesmanbacteria bacterium GW2011_GWA1_43_11.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1618436 {ECO:0000313|EMBL:KKS85201.1, ECO:0000313|Proteomes:UP000034543};
RN   [1] {ECO:0000313|EMBL:KKS85201.1, ECO:0000313|Proteomes:UP000034543}
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:KKS85201.1}.
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DR   EMBL; LCFB01000009; KKS85201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1EQ97; -.
DR   STRING; 1618436.UV59_C0009G0003; -.
DR   PATRIC; fig|1618436.3.peg.520; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000034543; 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   NCBIfam; TIGR02095; glgA; 1.
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          6..211
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          264..410
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   447 AA;  50660 MW;  5F57814CC7592F23 CRC64;
     MTSMLVVHVA FECAPIYKTG GLGDVVGSLP VYEAKLAIKT LVMIPAYAWV PRLSTLPGSK
     VEVLYIDGSR LDKPNKKHDP KIQGPKYAEF CLNVISELKR RGIVPDILHC HDWHTALIPF
     LLKKRPDPFF KITKTLLTIH NIAYQGKFPV KYFLYPETQQ FTELVGDNSK RVNFLKLGMQ
     SADFISTVSP AHAQEIRKGN AGFGLSRVLR HKRGRFLGIL NGIDYNVWNP APDGYVYEKY
     TRQSVFSGKL TNKVKLQQQL GLTVNKDIPL YGFIARLSSQ KGVDLLTPLI SELPRERLQL
     VLLGTGDHKI EKMLNEFNHK NFAPWISVNL RFDEQLAHRI YAASDFFLIP SHYEPCGLTQ
     MISMVYGTIP VASAVGGLVD TIKDGRTGFL LKSTTSESLH QAIRRSLALW ENTLEYRGMV
     ARVMKQDFSW DKSATEYVRL YRRILSL
//
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