SSY1_ORYSJ
ID SSY1_ORYSJ Reviewed; 641 AA.
AC Q0DEC8; B7F2B2; O24206; Q40739; Q5WA90; Q7Y044;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Soluble starch synthase 1, chloroplastic/amyloplastic {ECO:0000305};
DE EC=2.4.1.21 {ECO:0000305};
DE AltName: Full=Starch synthase I {ECO:0000303|PubMed:20018713};
DE Flags: Precursor;
GN Name=SS1 {ECO:0000303|PubMed:20018713};
GN Synonyms=SSS1 {ECO:0000303|PubMed:7610165};
GN OrderedLocusNames=Os06g0160700 {ECO:0000312|EMBL:BAS96282.1},
GN LOC_Os06g06560 {ECO:0000305};
GN ORFNames=P0681F10.13 {ECO:0000312|EMBL:BAD67625.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 114-131, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Seed;
RX PubMed=7518089; DOI=10.1104/pp.103.2.565;
RA Baba T., Nishihara M., Mizuno K., Kawasaki T., Shimada H., Kobayashi E.,
RA Ohnishi S., Tanaka K., Arai Y.;
RT "Identification, cDNA cloning, and gene expression of soluble starch
RT synthase in rice (Oryza sativa L.) immature seeds.";
RL Plant Physiol. 103:565-573(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7610165; DOI=10.1104/pp.108.2.677;
RA Tanaka K., Ohnishi S., Kishimoto N., Kawasaki T., Baba T.;
RT "Structure, organization and chromosomal location of the gene encoding a
RT form of rice soluble starch synthase.";
RL Plant Physiol. 108:677-683(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20018713; DOI=10.1073/pnas.0912396106;
RA Tian Z., Qian Q., Liu Q., Yan M., Liu X., Yan C., Liu G., Gao Z., Tang S.,
RA Zeng D., Wang Y., Yu J., Gu M., Li J.;
RT "Allelic diversities in rice starch biosynthesis lead to a diverse array of
RT rice eating and cooking qualities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21760-21765(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nanjing 37;
RA Junwang X., Zhen Z.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16443699; DOI=10.1104/pp.105.071845;
RA Fujita N., Yoshida M., Asakura N., Ohdan T., Miyao A., Hirochika H.,
RA Nakamura Y.;
RT "Function and characterization of starch synthase I using mutants in
RT rice.";
RL Plant Physiol. 140:1070-1084(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21417378; DOI=10.1021/bm200019q;
RA Hanashiro I., Higuchi T., Aihara S., Nakamura Y., Fujita N.;
RT "Structures of starches from rice mutants deficient in the starch synthase
RT isozyme SSI or SSIIIa.";
RL Biomacromolecules 12:1621-1628(2011).
RN [11]
RP FUNCTION.
RX PubMed=21730357; DOI=10.1093/jxb/err125;
RA Fujita N., Satoh R., Hayashi A., Kodama M., Itoh R., Aihara S.,
RA Nakamura Y.;
RT "Starch biosynthesis in rice endosperm requires the presence of either
RT starch synthase I or IIIa.";
RL J. Exp. Bot. 62:4819-4831(2011).
CC -!- FUNCTION: Involved in starch synthesis in endosperm amyloplasts
CC (PubMed:16443699, PubMed:21417378, PubMed:21730357). Plays a role in
CC the elongation of amylopectin chains (PubMed:16443699, PubMed:21417378,
CC PubMed:21730357). Synthesizes preferentially amylopectin chains with a
CC degree of polymerization (DP) of 7 to 11 by elongating chains with a DP
CC of 4 to 7 (PubMed:16443699). Generates distincly chains with a DP of 8
CC to 12 chains from short chains with a DP of 6 to 7 (PubMed:16443699).
CC {ECO:0000269|PubMed:16443699, ECO:0000269|PubMed:21417378,
CC ECO:0000269|PubMed:21730357}.
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:0000305};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Leaves and immature seeds.
CC {ECO:0000269|PubMed:7518089}.
CC -!- DISRUPTION PHENOTYPE: Decrease in average length of amylopectin chains
CC (PubMed:21417378). Reduced content of amylopectin chains with a degree
CC of polymerization (DP) of 8 to 12, but increased content of chains with
CC a DP of 6 to 7 and a DP of 16 to 19 (PubMed:16443699).
CC {ECO:0000269|PubMed:16443699, ECO:0000269|PubMed:21417378}.
CC -!- MISCELLANEOUS: Three forms of soluble starch synthase were purified:
CC RSS1, RSS2 and RSS3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49850.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA03739.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA07396.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D16202; BAA03739.1; ALT_FRAME; mRNA.
DR EMBL; D38221; BAA07396.1; ALT_FRAME; Genomic_DNA.
DR EMBL; GQ150941; ACY56156.1; -; Genomic_DNA.
DR EMBL; GQ150946; ACY56161.1; -; Genomic_DNA.
DR EMBL; GQ150942; ACY56157.1; -; Genomic_DNA.
DR EMBL; GQ150943; ACY56158.1; -; Genomic_DNA.
DR EMBL; GQ150944; ACY56159.1; -; Genomic_DNA.
DR EMBL; GQ150945; ACY56160.1; -; Genomic_DNA.
DR EMBL; AF165890; AAD49850.1; ALT_FRAME; mRNA.
DR EMBL; AB026295; BAD67625.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18795.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96282.1; -; Genomic_DNA.
DR EMBL; AK109458; BAG98759.1; -; mRNA.
DR PIR; JQ2322; JQ2322.
DR RefSeq; XP_015644241.1; XM_015788755.1.
DR AlphaFoldDB; Q0DEC8; -.
DR SMR; Q0DEC8; -.
DR STRING; 4530.OS06T0160700-01; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q0DEC8; -.
DR PRIDE; Q0DEC8; -.
DR EnsemblPlants; Os06t0160700-01; Os06t0160700-01; Os06g0160700.
DR GeneID; 9269493; -.
DR Gramene; Os06t0160700-01; Os06t0160700-01; Os06g0160700.
DR KEGG; osa:9269493; -.
DR eggNOG; ENOG502QTWM; Eukaryota.
DR HOGENOM; CLU_009583_18_2_1; -.
DR InParanoid; Q0DEC8; -.
DR OMA; TWCPWYM; -.
DR OrthoDB; 732319at2759; -.
DR PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q0DEC8; OS.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009960; P:endosperm development; IMP:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..113
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7518089"
FT CHAIN 114..641
FT /note="Soluble starch synthase 1,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000011138"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT CONFLICT 46..47
FT /note="QR -> HG (in Ref. 1; BAA03739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 70952 MW; EF851A03C7349076 CRC64;
MATAAGMGIG AACLVAPQVR PGRRLRLQRV RRRCVAELSR DGGSAQRPLA PAPLVKQPVL
PTFLVPTSTP PAPTQSPAPA PTPPPLPDSG VGEIEPDLEG LTEDSIDKTI FVASEQESEI
MDVKEQAQAK VTRSVVFVTG EASPYAKSGG LGDVCGSLPI ALALRGHRVM VVMPRYMNGA
LNKNFANAFY TEKHIKIPCF GGEHEVTFFH EYRDSVDWVF VDHPSYHRPG NLYGDNFGAF
GDNQFRYTLL CYAACEAPLI LELGGYIYGQ KCMFVVNDWH ASLVPVLLAA KYRPYGVYRD
ARSVLVIHNL AHQGVEPAST YPDLGLPPEW YGALEWVFPE WARRHALDKG EAVNFLKGAV
VTADRIVTVS QGYSWEVTTA EGGQGLNELL SSRKSVLNGI VNGIDINDWN PSTDKFLPYH
YSVDDLSGKA KCKAELQKEL GLPIRPDVPL IGFIGRLDYQ KGIDLIKLAI PDLMRDNIQF
VMLGSGDPGF EGWMRSTESG YRDKFRGWVG FSVPVSHRIT AGCDILLMPS RFEPCGLNQL
YAMQYGTVPV VHGTGGLRDT VENFNPFAEK GEQGTGWAFS PLTIEKMLWA LRMAISTYRE
HKSSWEGLMK RGMSSDFTWD HAASQYEQIF EWAFMDQPYV M
