ID   SSG1_IPOBA              Reviewed;         608 AA.
AC   Q42857; Q93VD9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=SS67;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RA   Kimura T., Ideta O., Saito A.;
RT   "Identification of the gene encoding granule-bound starch synthase I in
RT   sweet potato (Ipomoea batatas (L.) Lam.).";
RL   Plant Biotechnol. 17:247-252(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tainong 57; TISSUE=Tuberous root;
RA   Wang S.J., Yeh K.W., Tsai C.Y.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required 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   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA86423.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB071604; BAB68126.1; -; mRNA.
DR   EMBL; AB071976; BAB68525.1; -; Genomic_DNA.
DR   EMBL; U44126; AAA86423.1; ALT_FRAME; mRNA.
DR   PIR; T10906; T10906.
DR   AlphaFoldDB; Q42857; -.
DR   SMR; Q42857; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   BRENDA; 2.4.1.242; 2773.
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..76
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           77..608
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011128"
FT   BINDING         96
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        91
FT                   /note="V -> E (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="D -> E (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="L -> P (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="N -> K (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        549
FT                   /note="M -> I (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="D -> E (in Ref. 2; AAA86423)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   608 AA;  66689 MW;  C93CDA49A1F50C03 CRC64;
     MATITASHFV SHVCGGATSG ESKVGLGQLA LRSQAVTHNG LRPVNKIDML QLRTSAKKPS
     KNGRENEGGM AAGTIVCKQQ GMNLVFVGCE VGPWCKTGGL GDVLGGLPPA LAARGHRVMT
     VCPRYDQYKD AWDTCVVVEL QVGDRIEPVR FFHSYKRGVD RVFVDHPMFL EKVWGKTGSM
     LYGPKAGKDY KDNQLRFSLL CQAALEAPRV LNLNSSNYFS GPYGEDVVFV ANDWHTALLP
     CYLKTMYQSR GIYMNAKVAF CIHNIAYQGR FAFSDFSLLN LPDEYKGSFD FIDGYDKPVK
     GRKINWMKAG IREADRVFTV SPNYAKELVS CVSKGVELDN HIRDCGITGI CNGMDTQEWN
     PATDKYLAVK YDITTVMQAK PLLKEALQAA VGLPVDRNIP LIGFIGRLEE QKGSDILYAA
     ISKFISMDVQ ILILGTGKKK FEQQIEQLEV MYPDKARGVA KFNVPLAHMI TAGADFMLIP
     SRFEPCGLIQ LHAMRYGTPC ICASTGGLVD TVKEGYTGFH MGAFNVDCET VDPEDVLKVI
     TTVGRALAMY GTLAFTEMIK NCMSQELSWK GPAKNWETVL LSLGVAGSEP GVEGDEIAPL
     AKENVATP