ID J3L3K7_ORYBR Unreviewed; 975 AA.
AC J3L3K7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB01G38130.1};
RN [1] {ECO:0000313|EnsemblPlants:OB01G38130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB01G38130.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB01G38130.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) 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; J3L3K7; -.
DR STRING; 4533.J3L3K7; -.
DR EnsemblPlants; OB01G38130.1; OB01G38130.1; OB01G38130.
DR Gramene; OB01G38130.1; OB01G38130.1; OB01G38130.
DR eggNOG; ENOG502QQTU; Eukaryota.
DR HOGENOM; CLU_007243_0_0_1; -.
DR OMA; LDQHDDL; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000006038; 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:UP000006038};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 481..719
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 775..921
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 127..182
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 316..343
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 368..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 109917 MW; 2773BF863ACDAC96 CRC64;
MAACGAAAAA DYSALLPLRC GPGTRRRFAV SCRARPGNLS TQQKKKRGKN IAPKQLSSNT
KLLLTTEENG QLPNTSLRTS MQSHQKSTSS EDDTTGAIGQ RDEKFADIGN EQQERSKDKH
FESGVQLEDL GEMIQNMEKN ILLLNQAHLQ AIEDVGRILT EKEALQKKVN ILEMKLSKTL
AAEGDINTDV LGNHLEKFTI EMLIESALTG GNPVHLRESP LYMELTVLKE ENMLLKADAQ
FLKAKIIELA QAEEFLFKLE KERSLLDASI REHESRFLVA QTDIWKVAPL QYDVWMEKVE
NLQHILGCLT NDVNKYVALL DQHDDLQDKI DELEASVREG RTSEFSPYVV ELLQQKLKAA
KSHRQEGHQE TNSHIQVYQQ LIEEFQENLG KLMEESGRLE YSANGMPSEF WSHILLMIDG
WFLERKISNT DANMLREMTW KRDDRICEAY FACSGAKEGD VMEGFLKLTL SGNSQCSSAL
HIVHIAAEMA PVAKVGGLAD VVAGLGKALQ TNGHLVEIIL PKYDCMQLDQ ITNLKVLDVV
IQSYFDGNLF SNNVWTGTVE GLPVYFIEPQ HPSKFFWRAQ YYGEHDDFKR YSYFSRAALE
LLYQSGKKID IIHCHDWQTA FVAPLYWDIY ATRGFSSARI CFTCHNFEYQ GTAPAPDLSY
CGLDVEKLDR PDRMQDNAHG RINVAKGGIV YSNIVTTVSP TYALEVRSEG GHGLQDTLKT
HSRKFVGILN GIDTETWNPS TDRFLAVQYS ATDLQGKAAN KAFLRKQLGL YSEDAPQPLV
GCITRLVPQK GLHLIRHAIY KTAELGGQFV LLGSSPVPHI QREFEGVADQ FQNNNNIRLI
LKYDEALSHC IYAASDMFII PSMFEPCGLT QMIAMRYGSV PIVRKTGGLS DSVFDFDDET
LPAELRNGFT FARTDEQDLT SCLERAFRYY SRKPMVWKQL VQKDMQIDFS WVSPASQYEN
LYHSAVAQAR GVAQT
//
