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Database: UniProt
Entry: W0J309_9BACT
LinkDB: W0J309_9BACT
Original site: W0J309_9BACT 
ID   W0J309_9BACT            Unreviewed;       491 AA.
AC   W0J309;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=OPIT5_13955 {ECO:0000313|EMBL:AHF91146.1};
OS   Opitutaceae bacterium TAV5.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF91146.1, ECO:0000313|Proteomes:UP000003813};
RN   [1] {ECO:0000313|EMBL:AHF91146.1, ECO:0000313|Proteomes:UP000003813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAV5 {ECO:0000313|EMBL:AHF91146.1};
RX   PubMed=25744998;
RA   Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA   Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA   Rodrigues J.L.;
RT   "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT   Potential Facultative Methylotroph of the Wood-Feeding Termite
RT   Reticulitermes flavipes.";
RL   Genome Announc. 3:0-0(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}.
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DR   EMBL; CP007053; AHF91146.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0J309; -.
DR   STRING; 794903.OPIT5_13955; -.
DR   KEGG; obt:OPIT5_13955; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_0; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000003813; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000003813};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          5..244
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          303..443
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   491 AA;  54021 MW;  C1AE0D20BBF1D9DF CRC64;
     MSSLRILFVS PEVEPFVKVG GLADMAGSLP KALAALGHDV RIVCPAYGCV KIGTNWRARQ
     DPLGVDVGAA AEWARTWETT LPGATVPVPV YFLEHQRFFG RPEVYTGPWG AHEDNDLRFT
     FFSRAALTLC LQLGWIPDVI HCHDWTTGFV PVYLNTLYRD TPLGRTASMF TIHNLEHQGL
     FGRRAFDYSR LPAAEFRADS VEAFGGVNMM KAGLYHATKL TTVSPTYAHE IRTPEGGCGL
     HDVLAFRGAD LMGILNGIDT SSWSPEIDMS LPATYSAANF TGKAVCKAAL QRELGLKVDP
     HVAVFGIVSR FASQKGLDLV AEALPHIVRR MHVQFVILGA GDPGLEYMFR GMGDEFRGQV
     GTYIGYSPGL ARLVQAGSDF FVMPSRAEPC GLTQLYAMRY GTPPVVRATG GLIDTVEQYD
     EATGEGTGFL FNDTSAAALY NTVGWACSTY YDRPHHVRQL RRAGMAKDFS WRRSAELYVD
     AYHWAIAARR E
//
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