ID B7JDE8_BACC0 Unreviewed; 498 AA.
AC B7JDE8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:ACK88363.1};
GN OrderedLocusNames=BCAH820_4977 {ECO:0000313|EMBL:ACK88363.1};
OS Bacillus cereus (strain AH820).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK88363.1, ECO:0000313|Proteomes:UP000001363};
RN [1] {ECO:0000313|EMBL:ACK88363.1, ECO:0000313|Proteomes:UP000001363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820 {ECO:0000313|EMBL:ACK88363.1,
RC ECO:0000313|Proteomes:UP000001363};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001283; ACK88363.1; -; Genomic_DNA.
DR AlphaFoldDB; B7JDE8; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR KEGG; bcu:BCAH820_4977; -.
DR HOGENOM; CLU_009583_18_2_9; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001363; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 24..259
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 310..460
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 37
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 498 AA; 57481 MW; 23957BB3B4013FC1 CRC64;
MKTRREEAAR EVVEAFRAVG QQVNILFAVS ECVPFVKSGG LADVAGALPK ELKKLGVEVR
IILPNYSLIP QKLRDGCTLH KVINVPLGWR NQYCGILKGE QDGITYYLID NEYYFKRDSL
YGHYDDGERF SYFSKAVLEC IPHLDFEVDV LHSHDWHTAM VNFLLREKYQ DNPLYEHIKT
VYTIHNLQFQ GVFPPEVMYD LLELGDEYFH SEQLEFYGNV NFMKGGIIAS DQITAVSPTY
KEEIQYEFFG EKLDGLLRKY NDKLSGIVNG IDTSVYNPET DSYITAQYDA DSLYEKNENK
RALQRYFGLP EKEDTPIISM VTRLTKQKGL DLVRTVFREI MEEDVQCIIL GSGDSEYEQF
FEWMAYEYPE KVKVYIGFNE ELAHQVYAGS DLFLMPSLFE PCGLGQLIAL AYGTIPIVRE
TGGLNDTVQS YDEETGEGNG FSFTNFNAHD MLHTVLRAIE FYHDKPVWDR LVKQAMTEDY
SWEKSALAYK KLYKSLME
//
