ID   A0A0E0C796_9ORYZ        Unreviewed;       952 AA.
AC   A0A0E0C796;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G26980.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI01G26980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G26980.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI01G26980.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0C796; -.
DR   STRING; 40149.A0A0E0C796; -.
DR   EnsemblPlants; OMERI01G26980.1; OMERI01G26980.1; OMERI01G26980.
DR   Gramene; OMERI01G26980.1; OMERI01G26980.1; OMERI01G26980.
DR   eggNOG; ENOG502QQTU; Eukaryota.
DR   HOGENOM; CLU_007243_0_0_1; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000008021; Chromosome 1.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:RHEA.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
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; PTHR46083; -; 1.
DR   PANTHER; PTHR46083:SF2; STARCH SYNTHASE 4, CHLOROPLASTIC_AMYLOPLASTIC-RELATED; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361232};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          471..696
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          751..903
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          34..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          155..182
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        52..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   952 AA;  107757 MW;  FB8962701ED02FB7 CRC64;
     MAACGAAAAE YSALLSLPCG PITRRRFAVS CRARPPGNLS AQQKKKRGKN IAPKQLSSNA
     KLLLTTEENG QLPSTSLRTS MQPPQKSTSS EDDTNGAISQ RDEKIAAIGN EQQERSKDKH
     FESDFQLEDF GEMIQNMEKN ILLLNQARLQ AIEDVDKILT EKEALQKKVD ILETKLSKAL
     ATKGNINTDI PGDHLEKFTK EILIESALSG GNPAHLCESP LFMELTVLKE ENMLLKADTQ
     FLKAKIVEFA ETEEFLFKLE KERSLLDATV RELEARFLVA QTDIWKVVPL QYDVWMEKVQ
     NLQHMLGCLK NHVEKYAALL DRHDDLHDKI DELEASLKEG KTSEFSPYVV ELLQQKLKAA
     KSRHQAGHQE TNTHIQVYQQ LTEEFQDNLG RLIEESGRLE HSANSMPSEF WSHILLMIDG
     WFLERKIPNT DARMLREMAW KRDDRICEAY FACKGAKESD VMETFLKLTK QVGGLADVVT
     GLGKALQTKG HLVEIVLPKY DCMQLDQITN LKVLDVVIQS YFDGNLFSNN VWTGTVEGLP
     VYFIEPQHPS KFFWRAQYYG EHDDFKCYSY FSRAALELLY QSGKKIDIIH CHDWQTAFVA
     PLYWDIYATR GFSSARICFT CHNFEYQGTA PAPDLSYCGL DVEQLDRPDR MQDNAHGRIN
     VAKGGIVYSN IVTTVSPTYA LEVRSEGGRG LQDTLKMHSR KFVGILNGID TGTWNPSTDR
     FLAVQYSATD LQGKAANKAF LRKQLGLYSE DASQPLVACI TRLVPQKGLH LIRHAIYKTA
     ELEGQFVLLG SSPVPHIQRE FEGVADQFQK NNNIRLILKY DEALSHCIYA ASDMFIIPSM
     FEPCGLTQMI AMRYGSVPIV RQTGGLCDSV FDFDDETIPV ELRNGFTFAR TDEQDLSSCL
     ERAFSYYSRK PMVWKQLVQK DMQIDFSWDS PASQYENLYQ SAVAQARGAA QT
//