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Database: UniProt
Entry: Q7G050_AEGTA
LinkDB: Q7G050_AEGTA
Original site: Q7G050_AEGTA 
ID   Q7G050_AEGTA            Unreviewed;       604 AA.
AC   Q7G050;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN   Name=wx-TtD {ECO:0000313|EMBL:AAF06938.1};
OS   Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=37682 {ECO:0000313|EMBL:AAF06938.1};
RN   [1] {ECO:0000313|EMBL:AAF06938.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yan L., Bhave M., Fairclough R., Konic C., Rahman S., Appels R.;
RT   "The genes encoding granule-bound starch synthases at the waxy loci of the
RT   A, B and D progenitors of common wheat.";
RL   Genome 0:0-0(1999).
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         Evidence={ECO:0000256|ARBA:ARBA00036544};
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727, ECO:0000256|RuleBase:RU361232}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU361232}. Plastid, amyloplast
CC       {ECO:0000256|RuleBase:RU361232}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|RuleBase:RU361232}.
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DR   EMBL; AF110375; AAF06938.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7G050; -.
DR   SMR; Q7G050; -.
DR   UniPathway; UPA00152; -.
DR   ExpressionAtlas; Q7G050; baseline.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0043531; F:ADP binding; IEA:EnsemblPlants.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0019863; F:IgE binding; IEA:EnsemblPlants.
DR   GO; GO:0033840; F:NDP-glucose-starch glucosyltransferase activity; IEA:RHEA.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF3; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Amyloplast {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW   Chloroplast {ECO:0000256|RuleBase:RU361232};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361232};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          79..338
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          391..517
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   604 AA;  66269 MW;  6F69B3AB6594AE49 CRC64;
     MAALVTSQLA TSGTVLGITD RFRRAGFQGV RPRSPADAAL GMRTVGASAA PTQSRKAHRG
     TRRCLSMVVR ATGSGGMNLV FVGAEMAPWS KTGGLGDVLG GLPPAMAANG HRVMVISPRY
     DQYKDAWDTS VVSEIKVVDK YERVRYFHCY KRGVDRVFVD HPCFLEKVRG KTKEKIYGPD
     AGTDYEDNQQ RFSLLCQAAL EVPRILNLDN NPYFSGPYGE DVVFVCNDWH TGLLACYLKS
     NYQSNGIYRA AKVAFCIHNI SYQGRFSFDD FAQLNLPDRF KSSFDFIDGY DKPVEGRKIN
     WMKAGILQAD KVLTVSPYYA EELISGEARG CELDNIMRLT GITGIVNGMD VSEWDPTKDK
     FLAVNYDITT ALEGKALNKE ALQAEVGLPV DRKVPLVAFI GRLEEQKGPD VMIAAIPEIL
     KEEDVQIVLL GTGKKKFERL LKSIEEKFPS KVRAVVRFNA PLAHQMMAGA DVLAVTSRFE
     PCGLIQLQGM RYGTPCACAS TGGLVDTIVE GKTGFHMGRL SVDCNVVEPA DVKKVVTTLK
     RAVKVVGTPA YHEMVKNCMI QDLSWKGPAK NWEDVLLELG VEGSEPGVIG EEIAPLAMEN
     VAAP
//
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