ID   SSY1_ARATH              Reviewed;         652 AA.
AC   Q9FNF2; Q0WV88; Q9SEI7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Starch synthase 1, chloroplastic/amyloplastic;
DE            Short=AtSS1;
DE            Short=SSS;
DE            EC=2.4.1.21;
DE   AltName: Full=Soluble starch synthase I;
DE   Flags: Precursor;
GN   Name=SS1; OrderedLocusNames=At5g24300; ORFNames=MOP9.12;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-652.
RA   Lue W.L., Wang S.M., Yu T.S., Chen J.;
RT   "Characterization of Arabidopsis soluble starch synthase gene.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=16045475; DOI=10.1111/j.1365-313x.2005.02462.x;
RA   Delvalle D., Dumez S., Wattebled F., Roldan I., Planchot V., Berbezy P.,
RA   Colonna P., Vyas D., Chatterjee M., Ball S., Merida A., D'Hulst C.;
RT   "Soluble starch synthase I: a major determinant for the synthesis of
RT   amylopectin in Arabidopsis thaliana leaves.";
RL   Plant J. 43:398-412(2005).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=17217470; DOI=10.1111/j.1365-313x.2006.02968.x;
RA   Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V.,
RA   Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.;
RT   "The phenotype of soluble starch synthase IV defective mutants of
RT   Arabidopsis thaliana suggests a novel function of elongation enzymes in the
RT   control of starch granule formation.";
RL   Plant J. 49:492-504(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=21624979; DOI=10.1093/jxb/err172;
RA   Szydlowski N., Ragel P., Hennen-Bierwagen T.A., Planchot V., Myers A.M.,
RA   Merida A., d'Hulst C., Wattebled F.;
RT   "Integrated functions among multiple starch synthases determine both
RT   amylopectin chain length and branch linkage location in Arabidopsis leaf
RT   starch.";
RL   J. Exp. Bot. 62:4547-4559(2011).
CC   -!- FUNCTION: Involved in the synthesis of short glycan chains within
CC       amylopectin in leaves. Is required to generate chains up to about a
CC       degree of polymerization of 10 (DP10). {ECO:0000269|PubMed:16045475,
CC       ECO:0000269|PubMed:21624979}.
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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16045475}. Plastid, amyloplast
CC       {ECO:0000269|PubMed:16045475}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, buds and
CC       flowers. {ECO:0000269|PubMed:16045475, ECO:0000269|PubMed:17217470}.
CC   -!- INDUCTION: Circadian-regulation with the lowest levels at the end of
CC       the dark period. {ECO:0000269|PubMed:16045475}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have reduced starch content in leaves.
CC       {ECO:0000269|PubMed:16045475}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; AB006701; BAB10396.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93282.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93283.1; -; Genomic_DNA.
DR   EMBL; AY128273; AAM91082.1; -; mRNA.
DR   EMBL; AK226881; BAE98960.1; -; mRNA.
DR   EMBL; AF121673; AAF24126.1; -; Genomic_DNA.
DR   RefSeq; NP_001190378.1; NM_001203449.1.
DR   RefSeq; NP_197818.1; NM_122336.5.
DR   AlphaFoldDB; Q9FNF2; -.
DR   SMR; Q9FNF2; -.
DR   BioGRID; 17772; 1.
DR   STRING; 3702.Q9FNF2; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   iPTMnet; Q9FNF2; -.
DR   PaxDb; 3702-AT5G24300-1; -.
DR   ProteomicsDB; 228340; -.
DR   EnsemblPlants; AT5G24300.1; AT5G24300.1; AT5G24300.
DR   EnsemblPlants; AT5G24300.2; AT5G24300.2; AT5G24300.
DR   GeneID; 832497; -.
DR   Gramene; AT5G24300.1; AT5G24300.1; AT5G24300.
DR   Gramene; AT5G24300.2; AT5G24300.2; AT5G24300.
DR   KEGG; ath:AT5G24300; -.
DR   Araport; AT5G24300; -.
DR   TAIR; AT5G24300; SS1.
DR   eggNOG; ENOG502QTWM; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   InParanoid; Q9FNF2; -.
DR   OMA; TWCPWYM; -.
DR   OrthoDB; 141134at2759; -.
DR   PhylomeDB; Q9FNF2; -.
DR   BioCyc; ARA:AT5G24300-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G24300-MONOMER; -.
DR   BRENDA; 2.4.1.21; 399.
DR   UniPathway; UPA00152; -.
DR   PRO; PR:Q9FNF2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNF2; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0009011; F:starch synthase activity; IDA:UniProtKB.
DR   GO; GO:0010021; P:amylopectin biosynthetic process; IDA:TAIR.
DR   GO; GO:0009960; P:endosperm development; IEA:EnsemblPlants.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   Genevisible; Q9FNF2; AT.
PE   2: Evidence at transcript level;
KW   Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Reference proteome;
KW   Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..652
FT                   /note="Starch synthase 1, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011137"
FT   BINDING         156
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        78..85
FT                   /note="LGFQLTPP -> MNSIFPCT (in Ref. 5; AAF24126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="Q -> E (in Ref. 5; AAF24126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="Y -> H (in Ref. 5; AAF24126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        584
FT                   /note="T -> A (in Ref. 5; AAF24126)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   652 AA;  72099 MW;  91E5069DCD1B2B5B CRC64;
     MASLQISGSV KFEPFVGFNR IRHFRPIASL GFPRFRRRFS IGRSLLLRRS SSFSGDSRES
     DEERFITDAE RDGSGSVLGF QLTPPGDQQT VSTSTGEITH HEEKKEAIDQ IVMADFGVPG
     NRAVEEGAAE VGIPSGKAEV VNNLVFVTSE AAPYSKTGGL GDVCGSLPIA LAGRGHRVMV
     ISPRYLNGTA ADKNYARAKD LGIRVTVNCF GGSQEVSFYH EYRDGVDWVF VDHKSYHRPG
     NPYGDSKGAF GDNQFRFTLL CHAACEAPLV LPLGGFTYGE KSLFLVNDWH AGLVPILLAA
     KYRPYGVYKD ARSILIIHNL AHQGVEPAAT YTNLGLPSEW YGAVGWVFPT WARTHALDTG
     EAVNVLKGAI VTSDRIITVS QGYAWEITTV EGGYGLQDLL SSRKSVINGI TNGINVDEWN
     PSTDEHIPFH YSADDVSEKI KCKMALQKEL GLPIRPECPM IGFIGRLDYQ KGIDLIQTAG
     PDLMVDDIQF VMLGSGDPKY ESWMRSMEET YRDKFRGWVG FNVPISHRIT AGCDILLMPS
     RFEPCGLNQL YAMRYGTIPV VHGTGGLRDT VENFNPYAEG GAGTGTGWVF TPLSKDSMVS
     ALRLAAATYR EYKQSWEGLM RRGMTRNYSW ENAAVQYEQV FQWVFMDPPY VS
//