ID   SSG1_MANES              Reviewed;         608 AA.
AC   Q43784;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
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; Synonyms=GBSS;
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. M.COL 22; TISSUE=Tuberous root;
RX   PubMed=8260633; DOI=10.1007/bf00021811;
RA   Salehuzzaman S.N., Jacobsen E., Visser R.G.F.;
RT   "Isolation and characterization of a cDNA encoding granule-bound starch
RT   synthase in cassava (Manihot esculenta Crantz) and its antisense expression
RT   in potato.";
RL   Plant Mol. Biol. 23:947-962(1993).
CC   -!- FUNCTION: Responsible for the synthesis of amylose in reserve starch.
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: Synthesized in a number of different organs, but
CC       most abundantly in tubers.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; X74160; CAA52273.1; -; mRNA.
DR   PIR; S43341; S43341.
DR   AlphaFoldDB; Q43784; -.
DR   SMR; Q43784; -.
DR   STRING; 3983.cassava4.1_003884m; -.
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: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   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_0000011130"
FT   REGION          587..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;  66968 MW;  C9C970CD3011BDDB CRC64;
     MATVIAAHFV SRSSHLSIHA LETKANNLSH TGPWTQTITP NGLRSLNTMD KLQMKTQSKA
     VKKVSATGNG RPAAKIICGH GMNLIFVGAE VGPWSKTGGL GDVLGGLPPA MAARGHRVMT
     VSPRYDQYKD AWDTSVSVEI KIGDRIETVR FFHSYKRGVD RVFVDHPMFL EKVWGKTGSK
     IYGPRAGLDY QDNQLRFSLL CLAALEAPRV LNLNSSKNFS GPYGEEVAFI ANDWHTALLP
     CYLKAIYQPM GIYKHAKVAF CIHNIAYQGR FAFSDFPRLN LPDKFKSSFD FIDGYEKPVK
     GRKINWMKAG ILESDRVLTV SPYYAQEVIS GVERGVELDN FIRKTGIAGI INGMDVQEWN
     PVTDKYIDIH YDATTVMDAK PLLKEALQAE VGLPVDRNVP LIGFIGRLEE QKGSDIFVAA
     ISQLVEHNVQ IVILGTGKKK FEKQIEHLEV LYPDKARGVA KFNVPLAHMI TAGADFMLVP
     SRFEPCGLIQ LHAMRYGTVP IVASTGGLVD TVKEGYTGFQ MGALHVECDK IDSADVAAIV
     KTVARALGTY ATAALREMIL NCMAQDLSWK GPARMWEKML LDLEVTGSEP GTEGEEIAPL
     AKENVPTP