ID I1ZAJ1_AERHY Unreviewed; 486 AA.
AC I1ZAJ1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
OS Aeromonas hydrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644 {ECO:0000313|EMBL:AFJ20193.1};
RN [1] {ECO:0000313|EMBL:AFJ20193.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AH-3 {ECO:0000313|EMBL:AFJ20193.1};
RX PubMed=22563467; DOI=10.1371/journal.pone.0035707;
RA Merino S., Bouamama L., Knirel Y.A., Senchenkova S.N., Regue M.,
RA Tomas J.M.;
RT "Aeromonas Surface Glucan Attached through the O-Antigen Ligase Represents
RT a New Way to Obtain UDP-Glucose.";
RL PLoS ONE 7:e35707-e35707(2012).
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}.
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DR EMBL; JQ085284; AFJ20193.1; -; Genomic_DNA.
DR UniPathway; UPA00164; -.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 7..244
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 299..458
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 20
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 486 AA; 54926 MW; 0C37E675A565B791 CRC64;
MAINPLKILF VASEVEGLVK TGGLADVARA LPLYLAQKGH DVRIILPFYK TIKRRDEARL
IASRWLPTHP GLPDIGYRIY QMELEGVCVY LIDCPQYFDR PQLYAENNQA YGDNGERFAF
FSAAALHACE QLNFAPEIVH CNDWHTGLLP LXLKTRHAHN XFFQHTRSVI SIHNAAFQGV
FGREQFWAMP EIADYEQRVS YDYGHVNLLK CGVLYADKIN AVSPNYASEL LTHLGAHGMA
SIFQQRAADL RGILNGCDYQ DWDPAFDDFL PATYDVDNLA GKRVCKQTLQ QETGLPVADL
PIYGMVCRLT EQKGVHLLLP VLDKFLHHKV QVVIVGSGDP SLAAQLQAMA QQYPDKFAFI
NTYDDRLAHL VEAGADFFLM PSLFEPCGLN QMYSLAYGTL PLVRAVGGLK DTVVDWDADP
EHATGFCFND PTANILLDAM RRSLLYYLQD PERFARVQRN AMNTRFNWPD SVTLYEQMYQ
DALARQ
//
