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
//