SSY1_ARATH
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 03-AUG-2022, entry version 129.
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.AT5G24300.1; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR iPTMnet; Q9FNF2; -.
DR PaxDb; Q9FNF2; -.
DR PRIDE; Q9FNF2; -.
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; locus:2169749; AT5G24300.
DR eggNOG; ENOG502QTWM; Eukaryota.
DR HOGENOM; CLU_009583_18_2_1; -.
DR InParanoid; Q9FNF2; -.
DR OMA; TWCPWYM; -.
DR OrthoDB; 732319at2759; -.
DR PhylomeDB; Q9FNF2; -.
DR BioCyc; ARA:AT5G24300-MON; -.
DR BioCyc; MetaCyc:AT5G24300-MON; -.
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 Genevisible; Q9FNF2; AT.
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 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 Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
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
