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Database: UniProt
Entry: B2CP02_LOTJA
LinkDB: B2CP02_LOTJA
Original site: B2CP02_LOTJA 
ID   B2CP02_LOTJA            Unreviewed;       614 AA.
AC   B2CP02;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305 {ECO:0000313|EMBL:ACB30385.1};
RN   [1] {ECO:0000313|EMBL:ACB30385.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pan X., Yan H., Jiang H., Li M., Wu G.;
RT   "Two genes encoding granule bound starch synthase I in legumes and its
RT   phylogenetic relationship to GBSSI genes from other angiosperms.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; EU532433; ACB30385.1; -; mRNA.
DR   AlphaFoldDB; B2CP02; -.
DR   SMR; B2CP02; -.
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: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:SF15; 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|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   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          90..349
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          405..528
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   614 AA;  67257 MW;  71DF2D92B8A4FBB5 CRC64;
     MAAVAASSNL VSSSSYIHHR SILSYESKAA STGLRSLRQT NTHNGLRILN LVDELLNRTP
     IQVKAVQARR KGLQGKNVRP TGVIICGMNL IFLGTEVGPW SKTGGLGDVL GGLPPALAAN
     GHRVMTIAPR YDQYKDAWDT SVTIEVKVGD KTEKVGFFHC HKRGVDRVFV DHPIFLEKVW
     GKSGTKLYGP TAGEDYQDNQ LRFSLFCQAA LEAPRVLNLT SNKYFSGPYG EDVIFIANDW
     HTALIPCYLK SMYQSIGIYK NARVVYCIHN IAYQGRFAFA DFQLLNLPDQ FKSSFDFLDG
     HVKPVIGRKT NWMKAGILES DLVLTVSPYY AEELVSGPDK GVELDNIIRR TGITGIVNGM
     DVQEWNPSTD KYLTVKYNAS TVVEGKALLK EALQAEVGLP VDRNIPLIGF IGRLEEQKGS
     DILVAAIPQF IKENIQIVAL GTGKKQMEKQ LEQLEIAYPD KARGVAKFNV PLAHMIIAGA
     DFILIPSRFE PCGLIQLQAM RYGTVPIVAS TGGLVDTVKE GFTGFQMGSF NVECEAVDPA
     DVDALAKTVK RALAVHGTLA FTEIIKNCMA QDLSWKGPAK RWEEVLLSLG VPGSEAGIEG
     EEIAPQAKEN LATP
//
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