ID   SSG1_ANTMA              Reviewed;         608 AA.
AC   O82627;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Granule-bound starch synthase 1, chloroplastic/amyloplastic;
DE            EC=2.4.1.21;
DE   AltName: Full=Granule-bound starch synthase I;
DE            Short=GBSS-I;
DE   Flags: Precursor;
GN   Name=WAXY; Synonyms=GBSS;
OS   Antirrhinum majus (Garden snapdragon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=4151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Leaf;
RX   PubMed=10364391; DOI=10.1104/pp.120.2.401;
RA   Merida A., Rodriguez-Galan J.M., Vincent C., Romero J.M.;
RT   "Expression of the granule-bound starch synthase I (Waxy) gene from
RT   snapdragon is developmentally and circadian clock regulated.";
RL   Plant Physiol. 120:401-410(1999).
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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC       Note=Amyloplast or chloroplast, granule-bound.
CC   -!- TISSUE SPECIFICITY: In leaves, flowers and fruits. Observed in all
CC       floral whorls at early developmental stages, but restricted to carpel
CC       before anthesis.
CC   -!- INDUCTION: Expressed with a circadian rhythm with peak expression at
CC       the end of the day.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; AJ006293; CAA06958.1; -; mRNA.
DR   EMBL; AJ006294; CAA06959.1; -; Genomic_DNA.
DR   AlphaFoldDB; O82627; -.
DR   SMR; O82627; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   UniPathway; UPA00152; -.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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-EC.
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..78
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           79..608
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011124"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  66361 MW;  6527D53D565B6E0C CRC64;
     MATVTASQLV SHVHGGATSS PDTKTNLAQV GLRNQQFTHN GLRSINMVDK LQMRNNAKQS
     RSLVKKTDNG SPLGKIICGT GMNLVFVLAE VGPWSKTGGL GDVVGGLPPA MAGNGHRVMT
     VSPRYDQYKD AWDTSVVVEI KVGDSIETVR FFHCYKRGVD RVFVDHPIFL EKVWGKTKSK
     IYGPNAGTDY QDNQLRFSLL CQAALEAPRV LNLTSSKYFS GPYGEDVVFV ANDWHTALLP
     CYLKSMYQSK GMYLHAKVAF CIHNIAYQGR FGSSDFCLLN LPDQFKSSFD FFDGYEKPVK
     GRKINWMKAG ILESDRVVTV SPYYAMELVS GAEKGVELDN VIAKTSITGI VNGMDTQEWN
     PATDKHIDTN YDITTVMDAK PLLKEALQAA VGLPVDKNIP VIGFIGRLEE QKGSDILVAA
     ISKFVGLDVQ IIILGTGKKK FEQQIQELEV LYPDKARGVA KFNVPLAHMI TAGADFMLVP
     SRFEPCGLIQ LHAMRYGTIP ICASTGGLVD TVTEGFTGFH MGAFNVECAT VDPADVQKIA
     TTVERALAAY GSVAYKEMIQ NCMAQDLSWK GPAKNWEKML LSLGVSGSEP GVDGEEIAPL
     AKENVATP