ID   SSG1_ORYGL              Reviewed;         609 AA.
AC   Q42968; Q9S7R1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
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;
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. GMS1;
RX   PubMed=1685658; DOI=10.1266/jjg.66.569;
RA   Umeda M., Ohtsubo H., Ohtsubo E.;
RT   "Diversification of the rice Waxy gene by insertion of mobile DNA elements
RT   into introns.";
RL   Jpn. J. Genet. 66:569-586(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 78-94.
RX   PubMed=8595054; DOI=10.1007/bf00553625;
RA   Taira T., Fujita N., Takaoka K., Uematsu M., Wadano A., Kozaki S.,
RA   Okabe S.;
RT   "Variation in the primary structure of waxy proteins (granule-bound starch
RT   synthase) in diploid cereals.";
RL   Biochem. Genet. 33:269-281(1995).
CC   -!- FUNCTION: Required for the synthesis of amylose in endosperm.
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   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; D10472; BAA01272.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q42968; -.
DR   SMR; Q42968; -.
DR   STRING; 4538.ORGLA06G0020500.1; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblPlants; ORGLA06G0020500.1; ORGLA06G0020500.1; ORGLA06G0020500.
DR   Gramene; ORGLA06G0020500.1; ORGLA06G0020500.1; ORGLA06G0020500.
DR   eggNOG; ENOG502QQX3; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   OMA; EMGPAKN; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0009501; C:amyloplast; ISS:Gramene.
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; ISS:Gramene.
DR   GO; GO:0019863; F:IgE binding; IEA:EnsemblPlants.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005982; P:starch metabolic process; ISS:Gramene.
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   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW   Plastid; Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:8595054"
FT   CHAIN           78..609
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011131"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   609 AA;  66475 MW;  C228BBFB9C407FA5 CRC64;
     MSALTTSQLA TSATGFGIAD RSAPSSLLRH GFQGLKPRSP AGGDATSLSV TTSARATPKQ
     QRSVQRGSRR FPSVVVYATG AGMNVVFVGA EMAPWSKTGG LGDVLGGLPP AMAANGHRVM
     VISPRYDQYK DAWDTSVVAE IKVADRYERV RFFHCYKRGV DRVFIDHPSF LEKVWGKTGE
     KIYGPDTGVD YKDNQMRFSL LCQAALEAPR ILNLNNNPYF KGTYGEDVVF VCNDWHTGPL
     ASYLKNNYQP NGIYRNAKVA FCIHNISYQG RFAFEDYPEL NLSERFRSSF DFIDGYDTPV
     EGRKINWMKA GILEADRVLT VSPYYAEELI SGIARGCELD NIMRLTGITG IVNGMDVSEW
     DPSKDKYITA KYDATTAIEA KALNKEALQA EAGLPVDRKI PLIAFIGRLE EQKGPDVMAA
     AIPELMQEDV QIVLLGTGKK KFEKLLKSME EKYPGKVRAV VKFNAPLAHL IMAGADVLAV
     PSRFEPCGLI QLQGMRYGTP CACASTGGLV DTVIEGKTGF HMGRLSVNCK VVEPSDVKKV
     AATLKRAIKV VGTPAYEEMV RNCMNQDLSW KGPAKNWENV LLGLGVAGSA PGIEGDEIAP
     LAKENVAAP