ID A0A089KV32_9BACL Unreviewed; 474 AA.
AC A0A089KV32;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=R70331_16970 {ECO:0000313|EMBL:AIQ53046.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ53046.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ53046.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ53046.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009284; AIQ53046.1; -; Genomic_DNA.
DR RefSeq; WP_042177269.1; NZ_CP009284.1.
DR AlphaFoldDB; A0A089KV32; -.
DR STRING; 1536773.R70331_16970; -.
DR KEGG; paee:R70331_16970; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_2_9; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000029487; 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:UP000029487};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 3..235
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 292..449
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 474 AA; 53891 MW; 28D1ACFFD2BCDEB2 CRC64;
MKCLFAAAEA HPFVKTGGLA DVIGALPKAL KGAGVDVRVI LPKYKGIPEA YTAQMEHVAV
VDVPVGWRSQ YCGIERIIFE GIPVYFIDNE YYFGRDGIYG YMDDGERFAF YNRAVLECLP
AIDFQPDVLH CHDWHAAVIP MLLKAHYRHL EFYSGMRTVF TIHNLLYQGV FPYSVLGELL
GLDHSYYDSV EYYGNINYMK AGIVHSDHVT TVSPTYAEEI RTQYYGYGLD GLLNHRAESL
SGIVNGIDTK SYNPNTDNKI FTKYRSNLAK KAENKLGLQQ ELGLPVAPYI PMVAMVTRLV
DSKGLDLLTR VLDEILYYDD IQFVLLGTGD ETYERWFREA AWRYPTKLSS QILFNDALSR
KIYAASDIFL MPSKFEPCGI SQLLALRYGS IPVVRETGGL NDTVQSYIEE TGQGNGFTFK
DYNAHDMMFT LRRAVSLYHK PEHWKKVTKN AFAGDYSWNV SAQQYIDIYN KISE
//
