SSY23_ORYSJ
ID SSY23_ORYSJ Reviewed; 810 AA.
AC Q0DDE3; Q5DWW9; Q5DWX1; Q67X47; Q6TDS3; Q944W5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; OrderedLocusNames=Os06g0229800, LOC_Os06g12450;
GN ORFNames=P0525F01.23;
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 71-78, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS VAL-737 AND PHE-781, AND
RP MUTAGENESIS OF ASP-88; SER-604; MET-737 AND LEU-781.
RC STRAIN=cv. Kinmaze, and cv. Nipponbare;
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 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 [4]
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 [5]
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 [6]
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}.
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DR EMBL; AF419099; AAL16661.1; -; mRNA.
DR EMBL; AB115915; BAD90591.1; -; mRNA.
DR EMBL; AB115916; BAD90592.1; -; mRNA.
DR EMBL; AP003509; BAD37272.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19130.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96901.1; -; Genomic_DNA.
DR RefSeq; XP_015644246.1; XM_015788760.1.
DR AlphaFoldDB; Q0DDE3; -.
DR SMR; Q0DDE3; -.
DR STRING; 4530.OS06T0229800-01; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q0DDE3; -.
DR PRIDE; Q0DDE3; -.
DR EnsemblPlants; Os06t0229800-01; Os06t0229800-01; Os06g0229800.
DR GeneID; 4340567; -.
DR Gramene; Os06t0229800-01; Os06t0229800-01; Os06g0229800.
DR KEGG; osa:4340567; -.
DR eggNOG; ENOG502QT35; Eukaryota.
DR HOGENOM; CLU_009583_31_0_1; -.
DR InParanoid; Q0DDE3; -.
DR OMA; FVIPDAT; -.
DR OrthoDB; 732319at2759; -.
DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q0DDE3; baseline and differential.
DR Genevisible; Q0DDE3; OS.
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; Reference proteome; Starch biosynthesis; Transferase;
KW 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_0000011141"
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 VARIANT 737
FT /note="M -> V (in strain: cv. Kinmaze)"
FT /evidence="ECO:0000269|PubMed:16027975"
FT VARIANT 781
FT /note="L -> F (in strain: cv. Kinmaze)"
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 88
FT /note="D->E: Increased activity; when associated with V-
FT 737."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 604
FT /note="S->G: Increased activity; when associated with V-
FT 737. Slightly increased activity; when associated with V-
FT 737 and F-781."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 737
FT /note="M->V: Increased activity. Increased activity; when
FT associated with E-88 and/or G-604. Slightly increased
FT activity; when associated with G-604 and F-781."
FT /evidence="ECO:0000269|PubMed:16027975"
FT MUTAGEN 781
FT /note="L->F: Slightly increased activity; when associated
FT with G-604 and V-737."
FT /evidence="ECO:0000269|PubMed:16027975"
SQ SEQUENCE 810 AA; 88375 MW; 9676434321EAFE72 CRC64;
MSSAVVASST TFLVALASSA SRGGPRRGRV VGVAAPPALL YDGRAGRLAL RAPPPPRPRP
RRRDAGVVRR ADDGENEAAV ERAGEDDDEE 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
LDSSKPRCKA ALQRELGLEV RDDVPLIGFI GRLDGQKGVD IIGDAMPWIA GQDVQLVLLG
SGRRDLEVML QRFEAQHNSK VRGWVGFSVK MAHRITAGAD VLVMPSRFEP CGLNQLYAMA
YGTVPVVHAV GGLRDTMSAF DPFEDTGLGW TFDRAEPHKL IEALGHCLET YRKYKESWRG
LQVRGMSQDL SWDHAAELYE EVLVKAKYQW
