ID   SSY22_ORYSJ             Reviewed;         694 AA.
AC   Q6Z2T8; Q949A6; Q94ET4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Soluble starch synthase 2-2, chloroplastic/amyloplastic;
DE            EC=2.4.1.21;
DE   AltName: Full=Soluble starch synthase II-2;
DE   Flags: Precursor;
GN   Name=SSII-2; Synonyms=SS2;
GN   OrderedLocusNames=Os02g0744700, LOC_Os02g51070;
GN   ORFNames=OJ1118_G04.8, OJ1734_E02.35;
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].
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 [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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-694.
RA   Frohberg C.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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: May contribute to the deposition of transient starch in
CC       chloroplasts of leaves.
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
CC       {ECO:0000269|PubMed:15232694}. Plastid, chloroplast
CC       {ECO:0000269|PubMed:15232694}. Note=Amyloplast or chloroplast, granule-
CC       bound and soluble.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and weakly in endosperm and
CC       roots. {ECO:0000269|PubMed:15232694}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing caryopsis at 1 to 5 days
CC       after flowering. Expressed exclusively in the pericarp at 5 days after
CC       flowering.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD15539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD16123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF395537; AAK81729.1; -; mRNA.
DR   EMBL; AP004114; BAD15539.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP005297; BAD16123.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJ308110; CAC59826.1; -; mRNA.
DR   RefSeq; XP_015627452.1; XM_015771966.1.
DR   AlphaFoldDB; Q6Z2T8; -.
DR   SMR; Q6Z2T8; -.
DR   STRING; 39947.Q6Z2T8; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PaxDb; 39947-Q6Z2T8; -.
DR   EnsemblPlants; Os02t0744700-03; Os02t0744700-03; Os02g0744700.
DR   GeneID; 4330709; -.
DR   Gramene; Os02t0744700-03; Os02t0744700-03; Os02g0744700.
DR   KEGG; osa:4330709; -.
DR   eggNOG; ENOG502QT35; Eukaryota.
DR   InParanoid; Q6Z2T8; -.
DR   OrthoDB; 141134at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
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   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:SF13; SOLUBLE STARCH SYNTHASE 2-2, 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; Q6Z2T8; OS.
PE   2: Evidence at transcript level;
KW   Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Reference proteome;
KW   Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..15
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..694
FT                   /note="Soluble starch synthase 2-2,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011140"
FT   REGION          93..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         217
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        76
FT                   /note="T -> A (in Ref. 4; CAC59826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="V -> M (in Ref. 4; CAC59826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="Y -> S (in Ref. 4; CAC59826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="S -> P (in Ref. 4; CAC59826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="Y -> C (in Ref. 1; AAK81729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="G -> S (in Ref. 1; AAK81729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   694 AA;  75623 MW;  721D438F0C9092FC CRC64;
     MSGAIASSPA ATLFLAGSSS SSPRRRRSRV SGVWWHLYGG TGLRLHWERR GLVRDGAVVC
     SASAAGGEDG VAKAKTKSAG SSKAVAVQGS TAKADHVEDS VSSPKYVKPA VAKQNGEVVS
     RATKSDAPVS KPKVDPSVPA SKAEADGNAQ AVESKAALDK KEDVGVAEPL EAKADAGGDA
     GAVSSADDSE NKESGPLAGP NVMNVIVVAS ECSPFCKTGG LGDVVGALPK ALARRGHRVM
     VVIPRYGEYA EAKDLGVRKR YRVAGQDSEV SYFHAFIDGV DFVFLEAPPF RHRHNDIYGG
     ERFDVLKRMI LFCKAAVEVP WFAPCGGSIY GDGNLVFIAN DWHTALLPVY LKAYYRDNGL
     MQYTRSVLVI HNIAHQGRGP VDDFATMDLP EHYIDHFRLY DPVGGEHSNV FAAGLKMADR
     AVTVSHGYLW EIKTMDGGWG LHEIINHNDW KLQGIVNGID MAEWNPEVDE HLQSDGYANY
     TFETLDTGKK QCKEALQRQL GLQVRDDVPL IGFIGRLDHQ KGVDIIGDAM PWIAGQDVQV
     VMLGTGRPDL EEMLRRFESE HNDKVRGWVG FSVQLAHRIT AGADVLLMPS RFEPCGLNQL
     YAMAYGTVPV VHAVGGLRDT VAPFDPFADT GLGWTFDRAE ANRMIDALGH CLNTYRNYKE
     SWRGLQARGM AQDLSWDHAA ELYEDVLVKA KYQW
//