ID A0A073CP59_PLAAG Unreviewed; 483 AA.
AC A0A073CP59;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KEI65775.1};
GN ORFNames=A19Y_0590 {ECO:0000313|EMBL:KEI65775.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI65775.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI65775.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI65775.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(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}.
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DR EMBL; CM002803; KEI65775.1; -; Genomic_DNA.
DR RefSeq; WP_042151900.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CP59; -.
DR STRING; 388467.A19Y_0590; -.
DR GeneID; 77286855; -.
DR PATRIC; fig|388467.6.peg.535; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_2_3; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000027395; 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:UP000027395};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 2..215
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 267..406
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 461..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 483 AA; 55159 MW; 4CB5CB9B9A98D92D CRC64;
MRILFVAAEA APLAKVGGMG DVVGALPQVL RAMGHDVRIF MPYYGFLADK IKVPKDPIWW
GNAMYQRFAV FETVFPKTDV PLYLFGHPSF MPRRVYYGED EEWRFTLFSS GAAEFAWNYW
KPHIIHCHDW HTGMIPVWMQ ETPDIATIFT IHNLAYQGPW RWYLERITWC PWYMQGHNTM
AAAVQAADRV TTVSPTYAEQ IQTAAYGENL EGLLSFVSGK MTGILNGIDT NSYNPATDPY
IPERFTADSL ENRRANKVAI QEEVGLEVNS NTFLMGMVTR LVDQKGIDLV IQIMDQFLSY
SDSQLIVLGT GDRYYETQLW HMASRYPGRM TTQLLFNDAL SRRIYAGCDA FIMPSRFEPC
GISQMLAMRY GCIPIVRRTG GLVDTVSYND PINYHGTGYC FDRYEPLDFY TSMVRASEAF
RFKDQWRELQ RRAMGQNFSW ENSAKEYIQL YNNVMDGYGG VSNEPAPEPA PPQPPPPTPG
VVV
//
