ID A0A084CPE3_9GAMM Unreviewed; 503 AA.
AC A0A084CPE3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycogen synthase {ECO:0000256|ARBA:ARBA00019935, ECO:0000256|HAMAP-Rule:MF_00484};
DE EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588, ECO:0000256|HAMAP-Rule:MF_00484};
DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|ARBA:ARBA00031722, ECO:0000256|HAMAP-Rule:MF_00484};
GN Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484,
GN ECO:0000313|EMBL:KEY91672.1};
GN ORFNames=CF67_01107 {ECO:0000313|EMBL:KEY91672.1};
OS Candidatus Photodesmus blepharus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photodesmus.
OX NCBI_TaxID=1179155 {ECO:0000313|EMBL:KEY91672.1, ECO:0000313|Proteomes:UP000053784};
RN [1] {ECO:0000313|EMBL:KEY91672.1, ECO:0000313|Proteomes:UP000053784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppalp.1 {ECO:0000313|EMBL:KEY91672.1,
RC ECO:0000313|Proteomes:UP000053784};
RA Hendry T.A., de Wet J.R., Dunlap P.V.;
RT "Selection and divergence in the genomes of co-occurring obligate luminous
RT symbionts with specific hosts.";
RL Submitted (MAR-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|ARBA:ARBA00004964, 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:KEY91672.1}.
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DR EMBL; JGVK01000001; KEY91672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084CPE3; -.
DR STRING; 1179155.CF67_01107; -.
DR eggNOG; COG0297; Bacteria.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000053784; 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:UP000053784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 23..254
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 318..458
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 35
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 503 AA; 57298 MW; AF50D93BF28EA749 CRC64;
MFFKLFGLED GEKTKLSKKN LSILFAVSEV NGLAKSGGLA DFAKSLTESL VKLGQDVRLV
LPDYRKIVDN FNREVVLSTR LEHWPHTAYS VAKLSMQGVP IYCIRCSKYF DRSDMYEENN
EAYTDNGERF AFFSAACLDI LPKLAFCPNI VHANDWQTGF VAYFLKKRYA ETEYFQSMRC
VISIHNAAFK GMFTYEELQY LPEFRLRCVP EAEISSTHVT MLKAGIVCAD KINAVSPTYA
EELKTELGSH GMQNEFRSRS KDFIGILNGC DYSVWNPEID KYLPKNYRAT YQSMSFGKKV
CKQALQCEMG LPVKNVAMYG MVCRLTNQKG LHYLLPILDN FLEFDVQLVI IGVGDPFWVD
QLRTISTLHC TKFAFLEIYD DRLAHLIEAG SDFFLMPSEF EPCGLNQMYS MAYGTLPIVR
GVGGLKDSVK NYDSDSIEAT GFVFDKPSSE ALLVTISRSL ILYIQNPKEI DRLKLNAMKQ
RFFWSDSARK YIAMYRSALS ESA
//
