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Database: UniProt
Entry: A0A101W9R1_9FIRM
LinkDB: A0A101W9R1_9FIRM
Original site: A0A101W9R1_9FIRM 
ID   A0A101W9R1_9FIRM        Unreviewed;       482 AA.
AC   A0A101W9R1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=APF77_19575 {ECO:0000313|EMBL:KUO68977.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO68977.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO68977.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO68977.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO68977.1}.
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DR   EMBL; LOES01000235; KUO68977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101W9R1; -.
DR   STRING; 1734399.APF77_19575; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000057710; 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          5..239
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          293..440
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   482 AA;  55109 MW;  B8C9A763CAC6BB1D CRC64;
     MNNLNVLFAA SEAVPFAKTG GLADVAGTLP KELISLGADV RLIMPKYKAI SQSFVDRMEY
     IGYVYVDLAW RHQYCAVLKL EHEGVTAYFI DNEFYFNRDV LYGHFDEAEQ FAFFSKAVLK
     VLPLVGFKPD IIHCNDWQTG ILSVLLKAQF GHEEFYRNIR TVYTIHNLKY QGIFNKEILG
     DILGLGWEHF NSEGLEFHDN VNYMKAGIAY SDVITTVSKT YAEEIRHDFF GENLNGMINK
     RNDRLYGILN GIDYQENNPA TDDRIFKSFD AEDIEGKYEN KKMLQQTLGL PQDKDIPLIS
     IVSRLVDQKG FDLIACVLEE LLRLDMQLVV LGTGDKKYEE MFGNASSRYP GKVSANLKYD
     GLLAQRIYAG SDMFLMPSLY EPCGLSQLFS LRYGTVPIVR ETGGLNDTIE LYNEFTGEGT
     GFTFANYNAH EMLDAIRCAM SFYGQKDVWE AIIRNGMKQD FSWNKSAREY MELYERVLAL
     RK
//
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