ID   SSY1_WHEAT              Reviewed;         647 AA.
AC   Q43654; Q9LEB9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Starch synthase 1, chloroplastic/amyloplastic;
DE            EC=2.4.1.21;
DE   AltName: Full=Starch synthase I-2;
DE            Short=SS I;
DE            Short=SS I-2;
DE   Flags: Precursor;
GN   Name=WSSI-2;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fielder; TISSUE=Immature kernel;
RA   Peng M., Hucl P., Chibbar R.N.;
RT   "Isolation, characterization and expression analysis of starch synthase I
RT   from wheat (Triticum aestivum L.).";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 147-647.
RC   STRAIN=cv. Florida; TISSUE=Endosperm;
RA   Block M., Loerz H., Luetticke S.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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, soluble.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB02197.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ292522; CAB99210.1; -; mRNA.
DR   EMBL; U48227; AAB02197.1; ALT_FRAME; mRNA.
DR   PIR; T06280; T06280.
DR   AlphaFoldDB; Q43654; -.
DR   SMR; Q43654; -.
DR   STRING; 4565.Traes_7BS_6135B1D85.1; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PRIDE; Q43654; -.
DR   eggNOG; ENOG502QTWM; Eukaryota.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q43654; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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; Reference proteome;
KW   Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..647
FT                   /note="Starch synthase 1, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011143"
FT   REGION          66..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         153
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   647 AA;  71005 MW;  D3374D7C3497DF6F CRC64;
     MAATGVGAGC LAPSVRLRAD PATAARASAC VVRARLRRVA RGRYVAELSR EGPAARPAQQ
     QQLAPPLVPG FLAPPPPAPA QSPAPTQPPL PDAGVGELAP DLLLEGIAED SIDSIIVAAS
     EQDSEIMDAK DQPQAKVTRS IVFVTGEAAP YAKSGGLGDV CGSLPIALAA RGHRVMVVMP
     RYLNGSSDKN YAKALYTAKH IKIPCFGGSH EVTFFHEYRD NVDWVFVDHP SYHRPGSLYG
     DNFGAFGDNQ FRYTLLCYAA CEAPLILELG GYIYGQNCMF VVNDWHASLV PVLLAAKYRP
     YGVYRDSRST LVIHNLAHQG VEPASTYPDL GLPPEWYGAL EWVFPEWARR HALDKGEAVN
     FLKGAVVTAD RIVTVSQGYS WEVTTAEGGQ GLNELLSSRK SVLNGIVNGI DINDWNPTTD
     KCLPHHYSVD DLSGKAKCKA ELQKELGLPV REDVPLIGFI GRLDYQKGID LIKMAIPELM
     REDVQFVMLG SGDPIFEGWM RSTESSYKDK FRGWVGFSVP VSHRITAGCD ILLMPSRFEP
     CGLNQLYAMQ YGTVPVVHGT GGLRDTVETF NPFGAKGEEG TGWAFSPLTV DKMLWALRTA
     MSTFREHKPS WEGLMKRGMT KDHTWDHAAE QYEQIFEWAF VDQPYVM