ID A0A1G7NN70_9BACL Unreviewed; 485 AA.
AC A0A1G7NN70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN04488542_11663 {ECO:0000313|EMBL:SDF75514.1};
OS Fontibacillus panacisegetis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX NCBI_TaxID=670482 {ECO:0000313|EMBL:SDF75514.1, ECO:0000313|Proteomes:UP000198972};
RN [1] {ECO:0000313|EMBL:SDF75514.1, ECO:0000313|Proteomes:UP000198972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28129 {ECO:0000313|EMBL:SDF75514.1,
RC ECO:0000313|Proteomes:UP000198972};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNBG01000016; SDF75514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7NN70; -.
DR STRING; 670482.SAMN04488542_11663; -.
DR OrthoDB; 9802525at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000198972; 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:UP000198972};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 7..230
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 298..452
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 19
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 485 AA; 56117 MW; 8EC93DD63B17E3DD CRC64;
MGRKPTILYA TTEVFPFAKT GGLADVSAFL PKALRSEGYD IRIIMPKFKG IEDKYGHQLH
HVVTMDIEFA GRNHWYSVES ILYNGNMIYF VDAPYYFGRD RIYDYDDEME RFVFFCKAVM
ESLPVIGFQP DILQCNDWLM GFIPFFLKTK YRQLEFYKSM KSIFTIHALL YQGVFNKSNT
KSLLDLDWNY FVEQGLDYYD QVNCMKVGIM TSDVVSTVSP SYAAEISKMS PLHMEPLTES
LFKRRRDLHG ILNGIDLEEN NPATDSRLFA NYSLDHLEGK AENKKRLQES LGLPVRADVP
IVSLISRLEI TKGLYLIEKS YHELLKEDLQ FVVIGDGIPY YDYLFSNIMK AFPNKMYYST
YSEELAYKTY AGADLFLMPS YTEACGISQL IGMRYGTVPI IRETGGLRDT VEPFCEENET
GTGFTFKYAS QWVMLDTIRK AIDVYHKPDK WNKLVTNVMT RPVGWESSVK EYMRLYEQTM
GMTVS
//
