ID A0A059ADI6_EUCGR Unreviewed; 790 AA.
AC A0A059ADI6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN ORFNames=EUGRSUZ_J01349 {ECO:0000313|EMBL:KCW51888.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW51888.1};
RN [1] {ECO:0000313|EMBL:KCW51888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW51888.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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; KK198762; KCW51888.1; -; Genomic_DNA.
DR RefSeq; XP_010032498.1; XM_010034196.2.
DR AlphaFoldDB; A0A059ADI6; -.
DR STRING; 71139.A0A059ADI6; -.
DR EnsemblPlants; KCW51888; KCW51888; EUGRSUZ_J01349.
DR GeneID; 104421995; -.
DR Gramene; KCW51888; KCW51888; EUGRSUZ_J01349.
DR KEGG; egr:104421995; -.
DR eggNOG; ENOG502QT35; Eukaryota.
DR InParanoid; A0A059ADI6; -.
DR OMA; RFPFFTH; -.
DR OrthoDB; 141134at2759; -.
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:SF2; STARCH SYNTHASE 2, 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 Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 300..542
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 604..737
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 175..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 87994 MW; 5432983C4039D601 CRC64;
MASLGSLQFL SEPKAESSLL LYCINRRRPR SGSCGYWPRK SPVPLHLRGL SCGFSRSRDA
EDGWLKCSFC RGRMSGLYDR GQFLSVRAAG MGSAEGDDGD SLETEDKLQA TIEKSKRVLA
MQRDLLNQIA ERRKLVSTIK NSTISATEAE TAYENGMSTS SHQDVASTSD NYTTFEDNVL
GQTNGQSFSG SPLHSTKEAP ESVLTKEPDK AERNLESQFS SKVTPSSSDS PEHSNNISSV
SVQSTEMPSF LSSTLEVEPL EVEQNESLKE SSLQNVDNET ADPVSEDMEP PPLAGPNVMN
IILVAAECAP WSKTGGLGDV AGSLPKALAR RGHRVMVVAP RYGNYAEAQQ IGERKRYKVD
GQDHEVSYFQ AYIDGVDFVF IDSPMFRHIE NNIYGGNRVD ILKRMVLFCK AAVEVPWHVP
CGGICYGDGN LVFIANDWHT ALLPVYLKAY YRDNGLMSFT RSILVIHNIA HQGRGPVDDF
SFVDLPPHYI DLFKLYDPLG GDHFNIFAAG LKTADRVVTV SHGYAWELKT SEGGWGLHNI
INEMDWKLRG IVNGIDTKEW SPQYDVHLKS DGYTNYSLEN LQTGKAQCKE AFQRELGLPV
HPNVPLLGFI GRLDHQKGVD LIAEAVPWLM GQDVQLVMLG TGRQDLEQML RQFEGQHRDK
IRGWVGFSVK MAHRITAASD ILLMPSRFEP CGLNQLYAMS YGTIPVVHAV GGLRDTVEPF
DPFNNTGLGW TFDSAEANKL INALGYCLMT YRQYKESWEG IQRRGMTKDL SWDNAARNYE
EVLVAAKYQW
//
