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Database: UniProt
Entry: B2KNV0_ORYRU
LinkDB: B2KNV0_ORYRU
Original site: B2KNV0_ORYRU 
ID   B2KNV0_ORYRU            Unreviewed;       610 AA.
AC   B2KNV0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN   Name=waxy {ECO:0000313|EMBL:ABU98326.1};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EMBL:ABU98326.1};
RN   [1] {ECO:0000313|EMBL:ABU98326.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Shapter F.M., Eggler P., Lee L.S., Henry R.J.;
RT   "Variation in Granule Bound Starch Synthase I (GBSSI) loci amongst
RT   Australian wild cereal relatives (Poaceae).";
RL   J. Cereal Sci. 49:4-11(2009).
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; EF600037; ABU98326.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KNV0; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
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   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, ECO:0000313|EMBL:ABU98326.1}.
FT   DOMAIN          84..345
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          398..523
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  66577 MW;  E4D5A1810CE6DEB9 CRC64;
     MSALTTSQLA TSATGFGIAD RSAPSSLLRH GFQGLKPRSP AGGDATSLSV TTSARATPKQ
     QRSVQRGSRR FPSVVVYATG AGMNVVFIGA EMAPWSKTGG LGDVLGGLPP AMAANGHRVM
     VISPRYDQYK DAWDTSVVAE IKVADRYERV RFFHCYKRGV DRVFIDHPSF LEKVWGKTGE
     KIYGPDTGVD YKDNQMRFSL LCQSAALEAP RILNLNNNPY FKGTYGEDVV FVCNDWHTGP
     LASYLKNNYQ PNGIYRNAKV AFCIHNISYQ GRFAFEDYPE LNLSERFRSS FDFIDGYDTP
     VEGRKINWMK AGILEADRVL TVSPYYAEEL ISGIARGCEL DNIMRLTGIT GIVNGMDVSE
     WDPSKDKYIT AKYDATTAIE AKALNKEALQ AEAGLPVDRK IPLIAFIGRL EEQKGPDVMA
     AAIPELMQED VQIVLLGTGK KKFEKLLKSM EEKYPGKVRA VVKFNAPLAH LIMAGADVLA
     VPSRFEPCGL IQLQGMRYGT PCACASTGGL VDTVIEGKTG FHMGRLSVDC KVVEPSDVKK
     VAATLKRAIK VVGTPAYEEM VRNCMNQDLS WKGPAKNWEN VLLGLGVAGS APGIEGDEIA
     PLAKENVAAP
//
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