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Database: UniProt
Entry: A0A0D3CGL2_BRAOL
LinkDB: A0A0D3CGL2_BRAOL
Original site: A0A0D3CGL2_BRAOL 
ID   A0A0D3CGL2_BRAOL        Unreviewed;       675 AA.
AC   A0A0D3CGL2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN   Name=106295327 {ECO:0000313|EnsemblPlants:Bo5g086820.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g086820.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo5g086820.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo5g086820.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   RefSeq; XP_013586654.1; XM_013731200.1.
DR   AlphaFoldDB; A0A0D3CGL2; -.
DR   STRING; 109376.A0A0D3CGL2; -.
DR   EnsemblPlants; Bo5g086820.1; Bo5g086820.1; Bo5g086820.
DR   GeneID; 106295327; -.
DR   Gramene; Bo5g086820.1; Bo5g086820.1; Bo5g086820.
DR   KEGG; boe:106295327; -.
DR   eggNOG; ENOG502QQX3; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   OMA; LGMTHPR; -.
DR   OrthoDB; 141134at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000032141; Chromosome C5.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009569; C:chloroplast starch grain; IEA:EnsemblPlants.
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; 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|RuleBase:RU361232};
KW   Chloroplast {ECO:0000256|RuleBase:RU361232};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361232}; Plastid {ECO:0000256|RuleBase:RU361232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          152..410
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          463..592
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   675 AA;  73915 MW;  617587A6A73A3C5D CRC64;
     MEIASIGNST TVITPRVKFG QSSFHSPLYI NGPPSSSFSP HLSRSLITSS SVERVSLSRK
     MASVTASHFV SLVNNNHGGA SGSEANANLS QINFKCQSTT HCGLRSFNMV DRLQRRCQAK
     AVSAKSSKGL QQNAPKAKRV GKIVCEKGMS MIFIGAEVGP WSKTGGLGDV LGGLPPALAA
     RGHRVMTVCP RYDQYKDAWD TCVVVQIKVG DKVEEVRFFH CYKRGVDRVF VDHPLFLAKV
     VGKTGSKIYG PITGVDYTDN QLRFSLLCQA ALEAPRVLNL NSSKYFSGPY GEDVVFVAND
     WHTALLPCYL KSMYQSRGIY MNAKVVFCIH NIAYQGRFAF DDFSLLNLPD SFKSSFDFMD
     GYEKPLKGRK INWMKAAILE AWRVLTVSPY YAQELISGID RGVELHSYLR MKTVSGIING
     MDVQEWNPAT DKYIDIKYDI TTVTEAKPLI KEALQAAVGL PVDRDVPVIG FIGRLEEQKG
     SDILVEAISK FMGLNVQMVI LGTGKKKMEA QILELEEKFP GKAVGVAKFN VPLAHMITAG
     ADFIIVPSRF EPCGLIQLHA MRYGTVPIVA STGGLVDTVK DGYTGFHIGR FNVKCEVVDP
     DDVIATAKAV ARAVAVYGTP AMKEMVKNCM DQDFSWKGPA RLWEKVLLSL DVAGSEAGVE
     GEEIAPLAKE NVATP
//
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