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Database: UniProt
Entry: A0A1F5SQ96_9BACT
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ID   A0A1F5SQ96_9BACT        Unreviewed;       493 AA.
AC   A0A1F5SQ96;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=A2242_00760 {ECO:0000313|EMBL:OGF28898.1};
OS   Candidatus Falkowbacteria bacterium RIFOXYA2_FULL_47_9.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1797995 {ECO:0000313|EMBL:OGF28898.1, ECO:0000313|Proteomes:UP000178925};
RN   [1] {ECO:0000313|EMBL:OGF28898.1, ECO:0000313|Proteomes:UP000178925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGF28898.1}.
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DR   EMBL; MFGC01000004; OGF28898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5SQ96; -.
DR   STRING; 1797995.A2242_00760; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000178925; 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          7..246
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          299..458
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   BINDING         20
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   493 AA;  56796 MW;  CBB2AA20E4030012 CRC64;
     MNNHKLQIIH IVSEVDPFSK TGGLADVARS LPKAQKRLGH DVCVITPFYS QIIDVKKYKL
     ELFEKDIKVV LNSQDTAVVN FYRGYLMHGL PVYFIENKKY FSQRKILYGS SHENARFMLF
     DVAALRLITM LNLQPDIIHC HDWQAGLIPY YVKTKFHYVA NLTKTKTLYT IHNLAFQLGR
     NWWEVPVEQK DYGKSKLPRL DDPAIEHVNF AKRAIMNADA LNAVSENYAQ EILTKKFGQD
     LQRILQNRRD KLFGIQNGID YRAYNPATDA GLEKTYSCKN FSVKKMNKAR LQKLFGLPLN
     QHIPIIAMTS RIVFQKGFAL ILKIAEHLAR LNAQFIFIGA GDKTYVAKLQ RTAKKYPEKI
     AVIPSHEQNQ KYETLVYAGA DMLLLPSHHE PCGLNQMIAM RYGCVPIVHR VGGLFDTVED
     YRVTSGTGFV FDRFDAFELY GGIVRALEIF NNKRRWKELV ARDMRQSNSW EIPAKKYIDL
     YRKMLNGNAK SNS
//
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