ID   SSG1_PEA                Reviewed;         603 AA.
AC   Q43092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
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;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 76-88.
RC   STRAIN=cv. BC1/RR; TISSUE=Embryo;
RX   PubMed=1302049; DOI=10.1111/j.1365-313x.1992.00193.x;
RA   Dry I., Smith A., Edwards A., Bhattacharyya B., Dunn P., Martin C.;
RT   "Characterization of cDNAs encoding two isoforms of granule-bound starch
RT   synthase which show differential expression in developing storage organs of
RT   pea and potato.";
RL   Plant J. 2:193-202(1992).
CC   -!- FUNCTION: May be responsible for the synthesis of amylose.
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: Expressed in pods and leaves. No expression in
CC       flowers or stipules.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of embryonic development
CC       with highest levels in later developmental stages.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; X88789; CAA61268.1; -; mRNA.
DR   PIR; S61504; S61504.
DR   AlphaFoldDB; Q43092; -.
DR   SMR; Q43092; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PRIDE; Q43092; -.
DR   UniPathway; UPA00152; -.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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: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   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW   Plastid; Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..75
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1302049"
FT   CHAIN           76..603
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011133"
FT   BINDING         91
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   603 AA;  66362 MW;  817252FDD12CCAA0 CRC64;
     MATITGSSMP TRTACFNYQG RSAESKLNLP QIHFNNNQAF PVLGLRSLNK LHVRTARATS
     GSSDTSEKSL GKIVCGMSLV FVGAEVGPWS KTGGLGDVLG GLPPVLAGNG HRVMTVSPRY
     DQYKDAWDTN VLVEVKVGDK IETVRFFHCY KRGVDRVFVD HPLFLERVWG KTGSKLYGPK
     TGIDYRDNQL RFSLLCQAAL EAPRVLNLNS SKYFSGPYGE DVIFVANDWH SALIPCYLKS
     MYKSRGLYKN AKVAFCIHNI AYQGRNAFSD FSLLNLPDEF RSSFDFIDGY NKPCEGKKIN
     WMKAGILESD QVFTVSPHYA KELISGEDRG VELDNIIRST GIIGIVNGMD NREWSPQTDR
     YIDVHYNETT VTEAKPLLKG TLQAEIGLPV DSSIPLIGFI GRLEEQKGSD ILVEAIAKFA
     DENVQIVVLG TGKKIMEKQI EVLEEKYPGK AIGITKFNSP LAHKIIAGAD FIVIPSRFEP
     CGLVQLHAMP YGTVPIVSST GGLVDTVKEG YTGFHAGPFD VECEDVDPDD VDKLAATVKR
     ALKTYGTQAM KQIILNCMAQ NFSWKKPAKL WEKALLNLEV TGNVAGIDGD EIAPLAKENV
     ATP