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Database: UniProt
Entry: D7M325_ARALL
LinkDB: D7M325_ARALL
Original site: D7M325_ARALL 
ID   D7M325_ARALL            Unreviewed;       655 AA.
AC   D7M325;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN   ORFNames=ARALYDRAFT_489289 {ECO:0000313|EMBL:EFH48362.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001478};
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; GL348718; EFH48362.1; -; Genomic_DNA.
DR   RefSeq; XP_002872103.1; XM_002872057.1.
DR   AlphaFoldDB; D7M325; -.
DR   STRING; 81972.D7M325; -.
DR   EnsemblPlants; fgenesh2_kg.6__2423__AT5G24300.1; fgenesh2_kg.6__2423__AT5G24300.1; fgenesh2_kg.6__2423__AT5G24300.1.
DR   Gramene; fgenesh2_kg.6__2423__AT5G24300.1; fgenesh2_kg.6__2423__AT5G24300.1; fgenesh2_kg.6__2423__AT5G24300.1.
DR   eggNOG; ENOG502QTWM; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   OrthoDB; 141134at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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:0009011; F:starch synthase activity; IEA:EnsemblPlants.
DR   GO; GO:0010021; P:amylopectin biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0009960; P:endosperm development; IEA:EnsemblPlants.
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:SF11; 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   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          147..404
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          459..608
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   655 AA;  72228 MW;  5F9988D5AD244CEF CRC64;
     MASLQISGSV KFEPLVGFNR IRYFRPIGSL GIPRFRRRFS IGRPLLLRRS SSFSGDKIGE
     SVGDEKGFIT DAERDGSGSV LGFQLTPTGD QEIFSTSTGE ITHQEEKKEA IDETVMADFG
     VPGNRAVEEG AVEVGIPSGK AEVVNNLVFV TSEAAPYSKT GGLGDVCGSL PIALAGRGHR
     VMVVSPRYLN GTAADNNYAR AKDLGIRITV NCFGGSQEVS FYHEYRDGVD WVFVDHKSYH
     RPGNPYGDSK GAFGDNQFRF TLLCHAACEA PLVLPLGGFT YGEKSLFLVN DWHAGLVPIL
     LAAKYRPYGV YKDARSILII HNLAHQGVEP AATYTNLGLP SEWYGAVGWV FPTWARTHAL
     DTGEAVNVLK GAIVTSDRII TVSQGYAWEI TTVEGGYGLQ DLLSSRKSVI NGITNGINVD
     EWNPSTDEHI PFHYSADDFS EKVKCKMALQ KELGLPIRPE CPMIGFIGRL DYQKGIDLIQ
     TAGPDLMVDD IQFVMLGSGD PKYESWMRSM EETYRDKFRG WVGFNVPISH RITAGCDILL
     MPSRFEPCGL NQLYAMRYGT IPVVHGTGGL RDTVENFNPY AEGGAGAGTG WVFTPLSKDS
     MVSALRLAAA TYREYKESWE GLMRRGMTRN YSWENAAVQY EQVFQWVFMD PPYVS
//
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