ID   SSG2_PEA                Reviewed;         752 AA.
AC   Q43093;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Granule-bound starch synthase 2, chloroplastic/amyloplastic;
DE            EC=2.4.1.21;
DE   AltName: Full=Granule-bound starch synthase II;
DE            Short=GBSS-II;
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 58-73.
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   -!- 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 {ECO:0000250}. Plastid,
CC       amyloplast {ECO:0000250}. Note=Amyloplast or chloroplast, granule-bound
CC       and soluble. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Most highly expressed in early embryos. Levels
CC       decline in later stages of development.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; X88790; CAA61269.1; -; mRNA.
DR   PIR; S61505; S61505.
DR   AlphaFoldDB; Q43093; -.
DR   SMR; Q43093; -.
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   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW   Plastid; Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1302049"
FT   CHAIN           58..752
FT                   /note="Granule-bound starch synthase 2,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011144"
FT   REGION          116..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         275
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   752 AA;  83618 MW;  E0496420CD359395 CRC64;
     MMLSLGSDAT VLPFHAKNLK FTPKLSTLNG DLAFSKGLGV GRLNCGSVRL NHKQHVRAVG
     KSFGADENGD GSEDDVVNAT IEKSKKVLAL QRELIQQIAE RKKLVSSIDS DSIPGLEGNG
     VSYESSEKSL SRDSNPQKGS SSSGSAVETK RWHCFQQLCR SKETETWAVS SVGINQGFDE
     IEKKNDAVKA SSKLHFNEQI KNKLYERPDT KDISSSIRTS SLKFENFEGA NEPSSKEVAN
     EAENFESGGE KPPPLAGTNV MNIILVSAEC APWSKTGGLG DVAGSLPKAL ARRGHRVMIV
     APHYGNYAEA HDIGVRKRYK VAGQDMEVTY FHTYIDGVDI VFIDSPIFRN LESNIYGGNR
     LDILRRMVLF CKAAVEVPWH VPCGGICYGD GNLVFIANDW HTALLPVYLK AYYRDHGLMN
     YTRSVLVIHN IAHQGRGPVE DFNTVDLSGN YLDLFKMYDP VGGEHFNIFA AGLKTADRIV
     TVSHGYAWEL KTSEGGWGLH NIINESDWKF RGIVNGVDTK DWNPQFDAYL TSDGYTNYNL
     KTLQTGKRQC KAALQRELGL PVREDVPIIS FIGRLDHQKG VDLIAEAIPW MMSHDVQLVM
     LGTGRADLEQ MLKEFEAQHC DKIRSWVGFS VKMAHRITAG SDILLMPSRF EPCGLNQLYA
     MSYGTVPVVH GVGGLRDTVQ PFNPFDESGV GWTFDRAEAN KLMAALWNCL LTYKDYKKSW
     EGIQERGMSQ DLSWDNAAQQ YEEVLVAAKY QW