SSY23_ORYSI
ID SSY23_ORYSI Reviewed; 810 AA.
AC P0C586; Q5DWW9; Q5DWX1; Q67X47; Q6TDS3; Q944W5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Soluble starch synthase 2-3, chloroplastic/amyloplastic;
DE EC=2.4.1.21;
DE AltName: Full=Soluble starch synthase II-3;
DE AltName: Full=Starch synthase IIa;
DE Flags: Precursor;
GN Name=SSII-3; Synonyms=ALK;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Shuangke Zao;
RA Gao Z., Zeng D., Cui X., Zhou Y., Yan M., Huang D., Li J., Qian Q.;
RT "Map-based cloning of the ALK gene, which controls the gelatinization
RT temperature of rice.";
RL Sci. China, Ser. C, Life Sci. 46:661-668(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLU-88; GLY-604;
RP VAL-737 AND LEU-781.
RC STRAIN=cv. IR36, and cv. Kasalath;
RX PubMed=16027975; DOI=10.1007/s11103-005-6507-2;
RA Nakamura Y., Francisco P.B. Jr., Hosaka Y., Sato A., Sawada T., Kubo A.,
RA Fujita N.;
RT "Essential amino acids of starch synthase IIa differentiate amylopectin
RT structure and starch quality between japonica and indica rice varieties.";
RL Plant Mol. Biol. 58:213-227(2005).
RN [3]
RP PROTEIN SEQUENCE OF 71-78, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14740212; DOI=10.1007/s00425-003-1189-y;
RA Jiang H.W., Dian W.M., Liu F., Wu P.;
RT "Molecular cloning and expression analysis of three genes encoding starch
RT synthase II in rice.";
RL Planta 218:1062-1070(2004).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15232694; DOI=10.1007/s00425-004-1314-6;
RA Hirose T., Terao T.;
RT "A comprehensive expression analysis of the starch synthase gene family in
RT rice (Oryza sativa L.).";
RL Planta 220:9-16(2004).
CC -!- FUNCTION: Plays an important role during endosperm starch synthesis.
CC Determines the type of amylopectin structure of starch grain.
CC Synthesizes long B1 amylopectin chains by elongating short A and B1
CC chains, independently of the other soluble starch synthases. Barely
CC active in japonica subspecies. {ECO:0000269|PubMed:14740212,
CC ECO:0000269|PubMed:16027975}.
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, amyloplast. Plastid, chloroplast.
CC Note=Amyloplast or chloroplast, granule-bound and soluble.
CC -!- TISSUE SPECIFICITY: Expressed most exclusively in endosperm.
CC {ECO:0000269|PubMed:14740212, ECO:0000269|PubMed:15232694}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing caryopsis at 5 to 15 days
CC after flowering. Expressed exclusively in the endosperm at 5 to 10 days
CC after flowering. {ECO:0000269|PubMed:14740212}.
CC -!- MISCELLANEOUS: Increased activity due to variations in subspecies
CC indica is associated with the synthesis of the L-type amylopectin,
CC which contains much lower proportion of short amylopectin chains than
CC the S-type amylopectin found in most japonica varieties. The difference
CC in amylopectin chain composition explains why starch from japonica
CC subspecies has a lower gelatinisation temperature than starch from
CC indica subspecies.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ99280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY423717; AAQ99280.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB115917; BAD90593.1; -; mRNA.
DR EMBL; AB115918; BAD90594.1; -; mRNA.
DR AlphaFoldDB; P0C586; -.
DR SMR; P0C586; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PRIDE; P0C586; -.
DR UniPathway; UPA00152; -.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW Plastid; Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 17..810
FT /note="Soluble starch synthase 2-3,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000295651"
FT REGION 43..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT MUTAGEN 88
FT /note="E->D: Reduced activity; when associated with F-781.
FT Loss of activity; when associated with M-737. Loss of
FT activity; when associated with S-604 and F-781."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 604
FT /note="G->S: Loss of activity; when associated with M-737
FT and/or F-781."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 737
FT /note="V->M: Loss of activity. Loss of activity; when
FT associated with D-88 and/or S-604 and/or F-781."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 781
FT /note="L->F: Reduced activity. Reduced activity; when
FT associated with D-88. Loss of activity; when associated
FT with S-604 and/or M-737."
FT /evidence="ECO:0000269|PubMed:16027975"
SQ SEQUENCE 810 AA; 88327 MW; A08DE310DC90B319 CRC64;
MSSAVVASST TFLVALASSA SRGGPRRGRV VGVAAPPALL YDGRAGRLAL RAPPPPRPRP
RRRDAGVVRR ADDGENEAAV ERAGEDDEEE EEFSSGAWQP PRSRRGGVGK VLKRRGTVPP
VGRYGSGGDA ARVRGAAAPA PAPTQDAASS KNGALLSGRD DDTPASRNGS VVTGADKPAA
ATPPVTITKL PAPDSPVILP SVDKPQPEFV IPDATAPAPP PPGSNPRSSA PLPKPDNSEF
AEDKSAKVVE SAPKPKATRS SPIPAVEEET WDFKKYFDLN EPDAAEDGDD DDDWADSDAS
DSEIDQDDDS GPLAGENVMN VIVVAAECSP WCKTGGLGDV AGALPKALAR RGHRVMVVVP
RYGDYAEAQD VGIRKYYKAA GQDLEVKYFH AFIDGVDFVF IDAPLFRHRQ DDIYGGNRQE
IMKRMILFCK AAVEVPWHVP CGGVPYGDGN LVFLANDWHT ALLPVYLKAY YRDNGMMQYT
RSVLVIHNIA YQGRGPVDEF PYMELPEHYL DHFKLYDPVG GEHANIFGAG LKMADRVVTV
SPGYLWELKT TEGGWGLHDI IRENDWKMNG IVNGIDYREW NPEVDVHLQS DGYANYTVAS
LDSGKPRCKA ALQRELGLEV RDDVPLIGFI GRLDGQKGVD IIGDAMPWIA GQDVQLVLLG
SGRRDLEVML QRFEAQHNSK VRGWVGFSVK MAHRITAGAD VLVMPSRFEP CGLNQLYAMA
YGTVPVVHAV GGLRDTVSAF DPFEDTGLGW TFDRAEPHKL IEALGHCLET YRKYKESWRG
LQVRGMSQDL SWDHAAELYE EVLVKAKYQW
