ID A0A3M8R183_9PROT Unreviewed; 481 AA.
AC A0A3M8R183;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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 ECO:0000313|EMBL:RNF62306.1};
GN ORFNames=EC580_07370 {ECO:0000313|EMBL:RNF62306.1};
OS Acidithiobacillus sulfuriphilus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1867749 {ECO:0000313|EMBL:RNF62306.1, ECO:0000313|Proteomes:UP000271650};
RN [1] {ECO:0000313|EMBL:RNF62306.1, ECO:0000313|Proteomes:UP000271650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ-2 {ECO:0000313|EMBL:RNF62306.1,
RC ECO:0000313|Proteomes:UP000271650};
RA Falagan C., Moya-Beltran A., Quatrini R., Johnson D.B.;
RT "Acidithiobacillus sulfuriphilus sp. nov.: an extremely acidophilic sulfur-
RT oxidizing chemolithotroph isolated from a neutral pH environment.";
RL Submitted (OCT-2018) 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:RNF62306.1}.
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DR EMBL; RIZI01000162; RNF62306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8R183; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000271650; 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:UP000271650};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 3..240
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 297..443
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 16
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 481 AA; 53530 MW; 752CBE1D46B02435 CRC64;
MLRILFALSE MAPYSKTGGL ADVGSALPAA IAGLGVDIRV LVPAYHPFAE GAHLQWRGRV
TAPCTGETVE LWSPEERPQV LLLRYPPYYE RPGGPYQDPS GVDWPDNDQR FALLNRVAVE
IAQGRVPALD WRADIVHVND WQTGLVPYLL HLESRAGAPR PAVLFTIHNL AYQGRFDPGA
LQRLHLPPDG FHWQGTEFYG TFSFMKTALI YSDRIGTVSP TYAREIQEPE LGMGLEGVLR
TRSQGLFGIL NGIDTQSWNP GSDPYLPARF QRQDKGGKAL CKAQLQMEMG LYPAPETFLL
AMISRLVTQK GVDLVLDILP DLLRRGVQFV LLGSGEQPFE EAFRRLAAGQ RGQMAVRIAF
DEGLAHRIEA GADAFLMPSR FEPCGLNQMY SLRYGTLPIV RRTGGLADTV VDAEHFGGPP
PNGFVFVPVD RDALLAAVLR AESHFRQPAA WRYLQDNAMA LDFSWERAAR AYLEIYQQML
Q
//
