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Database: UniProt
Entry: B3VDJ2_ORYSJ
LinkDB: B3VDJ2_ORYSJ
Original site: B3VDJ2_ORYSJ 
ID   B3VDJ2_ORYSJ            Unreviewed;       609 AA.
AC   B3VDJ2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:ACE88263.1};
RN   [1] {ECO:0000313|EMBL:ACE88263.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Endosperm {ECO:0000313|EMBL:ACE88263.1};
RA   Zhang J., Xia M., Cheng B.J.;
RT   "Study and Cloning of Rice (Oryza sativa L.) Starch Synthesis Key Enzyme
RT   Gene and Molecular Regulation.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; EU735072; ACE88263.1; -; mRNA.
DR   AlphaFoldDB; B3VDJ2; -.
DR   SMR; B3VDJ2; -.
DR   Allergome; 11008; Ory s GBSS_I.
DR   UniPathway; UPA00152; -.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
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   2: Evidence at transcript level;
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          84..344
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          397..522
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          29..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  66441 MW;  E28D7FF77A34E7C4 CRC64;
     MSALTTSQLA TSATGFGIAD RSAPSSLLRH GFQGLKPHSP AGGDATSLSV TTSARATPKQ
     QRSVQRGSRR FPSVVVYATG AGMNVVFVGA EMAPWSKTGG LGDVLGGLPP AMAANGHRVM
     VISPRYDQYK DAWDTSVVAE IKVADRYERV RFFHCYKRGV DRVFIDHPSF LEKVWGKTGE
     KIYGPDTGVD YKDNQMRFSL LCQAALEAPR ILNLNNNPYF KGTYGEDVVF VCNDWHTGPL
     ASYLKNNYQP NGIYRNAKVA FCIHNISYQG RFAFEDYPEL NLSERFRSSF DFIDGYDTPV
     EGRKINWMKA GILEADRVPT VSPYYAEELI SGIARGCELD NIMRLTGITG IVNGMDVSEW
     DPSKDKYITA KYDATTAIEA KALNKEALQA EAGLPVDRKI PLIAFIGRLE EQKGPDVMAA
     AIPELMQEDV QIVLLGTGKK KFEKLLKSME EKYPGKVRAV VKFNAPLAHL IMAGADVLAV
     PSRFEPCGLI QLQGMRYGTP CACASTGGLV DTVIEGKTGF HMGRLSVDCK VVEPSDVKKV
     AATLKRAIKV VGTPAYEEMV RNCMNQDLSW KGPAKNWENV LLGLGVAGSA PGIEGDEIAP
     LAKENVAAP
//
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