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Database: UniProt
Entry: G5JWJ7_9STRE
LinkDB: G5JWJ7_9STRE
Original site: G5JWJ7_9STRE 
ID   G5JWJ7_9STRE            Unreviewed;       476 AA.
AC   G5JWJ7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   ECO:0000313|EMBL:EHJ52319.1};
GN   ORFNames=STRMA_0969 {ECO:0000313|EMBL:EHJ52319.1};
OS   Streptococcus macacae NCTC 11558.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ52319.1, ECO:0000313|Proteomes:UP000003573};
RN   [1] {ECO:0000313|EMBL:EHJ52319.1, ECO:0000313|Proteomes:UP000003573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ52319.1,
RC   ECO:0000313|Proteomes:UP000003573};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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:EHJ52319.1}.
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DR   EMBL; AEUW02000001; EHJ52319.1; -; Genomic_DNA.
DR   RefSeq; WP_003080204.1; NZ_UHFV01000002.1.
DR   AlphaFoldDB; G5JWJ7; -.
DR   STRING; 764298.STRMA_0969; -.
DR   eggNOG; COG0297; Bacteria.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000003573; 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          2..236
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          290..422
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   476 AA;  54298 MW;  E222DABD434E1E3F CRC64;
     MKILFVAAEG SPFAKIGGLG DVIGALPKSL VKKGNEVSVI LPYYDSIDAK FGEEIEDLFY
     FFTNVGWRHE YVGIKHTVKD GVDFYFIDNN HYFYRGQVYG EFDDGERFAF FQLAALEAME
     KIDFIPDILH VHDYHTAMIP FLLKEKYHWI NAYQKIKTVF TIHNIEFQGQ FAPSLLGEVF
     GVGEERYWDG TLRWRDCLNW MKAAILYADR VTTVSPSYAQ EIQTPEFGKG LDQIMRMESG
     KLSGIVNGID TELLDPRTDE HLLAHFSKDD LSGKAKNKAA LQEQLGLPVR DDVALIGVVS
     RLTDQKGFNL VVNELNAMMQ MDIQLVLLGT GYAEFENAFS WFAQAYPEKM SANIMFDLTL
     AQQIYAASDI FLMPSAFEPC GLSQMMAMRY GSLPLVHEVG GLRDTVIPYN EFDKTGTGFG
     FQEFSGYWLT RTLAKALDVY YNREKDWKKL QESAMTTDFS WDTASQAYEH LYRELV
//
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