ID   SSG1_SORBI              Reviewed;         608 AA.
AC   Q43134; P81888;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Granule-bound starch synthase 1, chloroplastic/amyloplastic;
DE            EC=2.4.1.242;
DE   AltName: Full=Granule-bound starch synthase I;
DE            Short=GBSS-I;
DE   Flags: Precursor;
GN   Name=WAXY; Synonyms=WX; OrderedLocusNames=Sb03g020190;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. 12311; TISSUE=Seed;
RA   Hsing Y.C., Liu C., Yu H., Hsieh J.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 336-590.
RC   TISSUE=Leaf;
RX   PubMed=9866201; DOI=10.1093/oxfordjournals.molbev.a025893;
RA   Mason-Gamer R.J., Weil C.F., Kellogg E.A.;
RT   "Granule-bound starch synthase: structure, function, and phylogenetic
RT   utility.";
RL   Mol. Biol. Evol. 15:1658-1673(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose =
CC         [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate +
CC         H(+); Xref=Rhea:RHEA:15873, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:76533; EC=2.4.1.242;
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC       Note=Amyloplast or chloroplast, granule-bound.
CC   -!- TISSUE SPECIFICITY: Seed specific.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; U23945; AAC49804.1; -; mRNA.
DR   EMBL; AF079258; AAD02978.1; -; Genomic_DNA.
DR   PIR; T14731; T14731.
DR   RefSeq; XP_002436418.1; XM_002436373.1.
DR   AlphaFoldDB; Q43134; -.
DR   SMR; Q43134; -.
DR   STRING; 4558.Sb10g002140.1; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblPlants; EER87785; EER87785; SORBI_3010G022600.
DR   GeneID; 8068390; -.
DR   Gramene; EER87785; EER87785; SORBI_3010G022600.
DR   KEGG; sbi:8068390; -.
DR   eggNOG; ENOG502QQX3; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   OMA; EMGPAKN; -.
DR   OrthoDB; 1142473at2759; -.
DR   BRENDA; 2.4.1.242; 5768.
DR   UniPathway; UPA00152; -.
DR   ExpressionAtlas; Q43134; baseline.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0043531; F:ADP binding; IEA:EnsemblPlants.
DR   GO; GO:0102502; F:ADP-glucose-starch glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0019863; F:IgE binding; IEA:EnsemblPlants.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR02095; glgA; 1.
PE   2: Evidence at transcript level;
KW   Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Starch biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           78..608
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011135"
FT   BINDING         96
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  66074 MW;  C31333FA87D2D8A6 CRC64;
     MSTLATSQLV ATHAGLGVPD ASMFRRGGVQ GLRAAARASA AAGDALSMRT SACPAPRQQP
     AARRGGRGGR FPSLVVCATA GMNVVFVGAE MAPWSKTGGL GDVLGGLPPA MAANGHRVMV
     VSPRYDQYKD AWDTSVVSEI KMGDGYETVR FFHCYKRGVD RVFIDHPLFL ERVWGKTEEK
     IYGPDAGTDY KDNQLRFSLL CQAALEAPRI LSLNNNPYFS GPYGEDVVFV CNDWHTGPLS
     CYLKSNYQSN GIYKDAKTAF CIHNISYQGR FAFSDFPELN LPERFKSSFD FIDGYEKPVE
     GRKINWMKAG ILEADRVLTV SPYYAEELIS GIARGCELDN IMRLTGITGI VNGMDVSEWD
     PSKDKYIAVK YDVSTAVEAK ALNKEALQAE VGLPVDRKIP LVAFIGRLEE QKGPDVMAAA
     IPLLMEEDIQ IVLLGTGKKK FERMLMSAEE KYPDKVRAVV KFNAALAHHI MAGADLLAVT
     SRFEPCGLIQ LQGMRYGTPC ACASTGGLVD TIIEGKTGFH MGRLSVDCNV VEPADVKKVA
     TTLKRAIKVV GTPAYEEMVK NCMIQDLSWK GPAKNWENVL LSLGVAGGEP GIEGEEIAPL
     AKENVAAP