ID   SSG1B_HORVU             Reviewed;         565 AA.
AC   Q8LL05;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Granule-bound starch synthase 1b, chloroplastic/amyloplastic;
DE            EC=2.4.1.242;
DE   AltName: Full=Granule-bound starch synthase Ib;
DE   Flags: Precursor; Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 35-44.
RX   PubMed=12226499; DOI=10.1104/pp.005454;
RA   Patron N.J., Smith A.M., Fahy B.F., Hylton C.M., Naldrett M.J.,
RA   Rossnagel B.G., Denyer K.;
RT   "The altered pattern of amylose accumulation in the endosperm of low-
RT   amylose barley cultivars is attributable to a single mutant allele of
RT   granule-bound starch synthase I with a deletion in the 5'-non-coding
RT   region.";
RL   Plant Physiol. 130:190-198(2002).
CC   -!- FUNCTION: Involved in the synthesis of amylose in endosperm.
CC       {ECO:0000250}.
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 {ECO:0000250}. Plastid,
CC       amyloplast {ECO:0000250}. Note=Amyloplast or chloroplast, granule-
CC       bound. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; AF486521; AAM74054.1; -; mRNA.
DR   AlphaFoldDB; Q8LL05; -.
DR   SMR; Q8LL05; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   UniPathway; UPA00152; -.
DR   ExpressionAtlas; Q8LL05; baseline and differential.
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:0009011; F:starch synthase activity; IEA:EnsemblPlants.
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..34
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:12226499"
FT   CHAIN           35..565
FT                   /note="Granule-bound starch synthase 1b,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011127"
FT   BINDING         52
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   565 AA;  62444 MW;  E4A394EDD4F80BD7 CRC64;
     VFLSMRNKTQ LAKRRATNYE THRNSSRTSS PIVCSTGMPI IFVATEVHPW CKTGGLGDVV
     GGLPPALAAM GHRVMTIAPR YDQYKDTWDT NVLVEVIVGD RTETVRFFHC YKRGVDRVFV
     DHPMFLEKVW GKTGSKLYGP TTGTDFRDNQ LRFCLLCLAA LEAPRVLNLN NSEYFSGPYG
     ENVVFVANDW HTAVLPCYLK SMYKQNGIYE NAKVAFCIHN IAYQGRFPRA DFELLNLPES
     FMPSFDFVDG HVKPVVGRKI NWMKAGITEC DVVLTVSPHY VKELTSGPEK GVELDGVLRT
     KPLETGIVNG MDVIDWNPAT DKYISVKYNA TTVAQARALN KEILQAEVGL SVDSSIPVIV
     FIGRLEEQKG SDILIAASPE FVEENVQIIV LGTGKKKMEE ELMLLEVKYP QNARGIAKFN
     VPLAHMMFAG ADFIIIPSRF EPCGLIQLQG MSYGVVPICS STGGLVDTVR EGVTGFHMGS
     FNVEFETVDP TDVAAVGSNV TRALKQYRTP VFHAMVQNCM AQDLSWKGPA KKWEEALLSL
     GVEGSQPGIE GEEIAPLAKQ NVATP