ID G6XF10_9PROT Unreviewed; 548 AA.
AC G6XF10;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=GMO_00750 {ECO:0000313|EMBL:EHH68768.1};
OS Gluconobacter morbifer G707.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH68768.1, ECO:0000313|Proteomes:UP000004949};
RN [1] {ECO:0000313|EMBL:EHH68768.1, ECO:0000313|Proteomes:UP000004949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G707 {ECO:0000313|EMBL:EHH68768.1,
RC ECO:0000313|Proteomes:UP000004949};
RA Lee W.-J., Kim E.-K.;
RT "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT gut.";
RL Submitted (OCT-2011) 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:EHH68768.1}.
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DR EMBL; AGQV01000001; EHH68768.1; -; Genomic_DNA.
DR AlphaFoldDB; G6XF10; -.
DR STRING; 1088869.GMO_00750; -.
DR PATRIC; fig|1088869.3.peg.74; -.
DR eggNOG; COG0297; Bacteria.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000004949; 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:UP000004949};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 18..249
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 302..454
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 504..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 548 AA; 59678 MW; F80931F87F934F84 CRC64;
MHAMNQPAEM PSPMFQLLSV AGEMYPFVKT GGLGDVVGSL PPALVSQGVE TRTVLPGYPA
VLRALSSRIG AVKIGNIMGH EVTVLEGHAH GAHLYVVDVP ALYQRPGNPY LGPDGQPWGD
NGIRYALFCR VAALIAAGLF PDWKPEAVMT HDWHAGLVAT YLRYMEEQTP QVAHVIHNLA
FQGLFPRDMM GVFELPEHAF QCGDIEYYGQ IGFMKAALQT ADRLISVSPT YAEEIQTPEE
GMGLDGVLRS RSNVLTGILN GVDLQDWNPL TDPSVFFPYA VGDIVGRRAN KRVFQAEFGL
PQDPDAFLLG MVSRLTTQKG ADLLATLAPR LFDQNIQLAV VGTGDEGIMQ AFAALQSRYP
KNVICHLRYS ETLGHRLHSA VDASLIPSRF EPCGLTQFHA LRYGSIPIAA RVGGLSDTIV
DANSAAVSEG VANGILFSPT TEDMLMLAIR RGLNLFRQKA VWARMQRNGA LHDVSWDGKA
AQYARLLLEM TGRPPMALEL ENSIAPRRGD PVSAQPRSGR QVARMPRGRN GEQASTMIHA
FPRTGTHA
//
