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Database: UniProt
Entry: A6Q9R3_SULNB
LinkDB: A6Q9R3_SULNB
Original site: A6Q9R3_SULNB 
ID   A6Q9R3_SULNB            Unreviewed;       493 AA.
AC   A6Q9R3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
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   OrderedLocusNames=SUN_1269 {ECO:0000313|EMBL:BAF72222.1};
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum.
OX   NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72222.1, ECO:0000313|Proteomes:UP000006378};
RN   [1] {ECO:0000313|EMBL:BAF72222.1, ECO:0000313|Proteomes:UP000006378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72222.1,
RC   ECO:0000313|Proteomes:UP000006378};
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF72222.1; -; Genomic_DNA.
DR   RefSeq; WP_011980955.1; NC_009663.1.
DR   AlphaFoldDB; A6Q9R3; -.
DR   STRING; 387093.SUN_1269; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   KEGG; sun:SUN_1269; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_7; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006378; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          8..244
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          291..448
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   BINDING         19
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   493 AA;  56136 MW;  24552CA159D388AC CRC64;
     MKRKIRTLFV ASEVVPFAKT GGLADVSGAL PKALARLGSD IKVVMPRYYT IDKNTLEHIP
     MALGVDMGAM GELWAGVYRT YLPDSEVEIY FIDHEAFYGR SGLYHESEAY EDNDKRFVFL
     SKAALQLCRA LNFKPDIVHA NDWHTATLPI LLKTSLHEDD FFKESASVLT VHNLQHQGVF
     GKELMNVLGV GWEHFTPMEL EAMDNVNLLK GGITFCDALT TVSKKYAREI QTPEFGFGLD
     EHLRAHAHKL YGILNGIDYT EWNPSVDKYI AVNYDVDTLE KKKKCKQDLQ KRFNLPQRED
     VPLIGFVGRF VTQKGIELIA TVIDGLLEMD IQVVMLGNGE FWAENFFSQV AAGHPDKFGC
     YIGYSNELAH QIEAGSDLFL MPSLFEPCGL NQIYSLRYGT LPIVRATGGL DDTIVNYDPQ
     TKEGNGFKFY HATPDALYHT VKWAVETYHQ EKDDFLHMQK NAMREHFSWL DSGTAYLDIY
     KALYYHQKIQ RYK
//
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