ID A0A1E8GMB1_9LACT Unreviewed; 477 AA.
AC A0A1E8GMB1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BG261_07110 {ECO:0000313|EMBL:OFI48658.1};
OS Floricoccus tropicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Floricoccus.
OX NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI48658.1, ECO:0000313|Proteomes:UP000178622};
RN [1] {ECO:0000313|Proteomes:UP000178622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT "Draft genome sequence of a novel species of the family Streptococcaceae
RT isolated from flowers.";
RL Submitted (SEP-2016) 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:OFI48658.1}.
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DR EMBL; MKIR01000024; OFI48658.1; -; Genomic_DNA.
DR RefSeq; WP_070793050.1; NZ_MKIR01000024.1.
DR AlphaFoldDB; A0A1E8GMB1; -.
DR STRING; 1859473.BG261_07110; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000178622; 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}; Reference proteome {ECO:0000313|Proteomes:UP000178622};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 2..237
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 291..428
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 15
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 477 AA; 54889 MW; 2C1A9A094FE503EB CRC64;
MKILLVGAEA APFIKTGGLG DVLGALPKSL NKKKDVDARV ILPYYKGIPQ QFKDQAEDLF
YTYVDVGWRH MYAGVKHIYF ENVHFYFIDN EYYFNRDGVY GFYDDGERFA FFQQAVLEIL
PQLEFIPDVI HVNDYHTAMI PVLLREKYAW IDGYPYINTL LTIHNIEFQG QYDPATLGEL
FNLSMDKYND GTFQQDGCFN WLKSGLIYAN KITTVSPTYA KEIQTPEFGK GLDSILRAQN
SKLSGIVNGI DTEIFDPAKD EFLFKNYSLK TVKDKTINKL ELQKQVGLPV REDVMLVGIV
SRLTYQKGFH LVLEQMKEIL NWDIQFVILG TGYKEFEEGF SWFTENYPDK VATIINFNLE
LAQRIYGGSD LFLMPSAFEP CGLSQMMAMR YGNLPLVHEV GGLKDTVSPY NPLTGEGTGF
GFKSFDSYWL KDVLASANLL YNRDQEAWKK LQKNAMEQDF SWDTASLEYL NLYWELN
//
