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RBS1_ORYSJ
ID   RBS1_ORYSJ              Reviewed;         175 AA.
AC   Q0INY7; B7E6P1; O65105; P05347; P18567; Q2QU37;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   AltName: Full=Ribulose bisphosphate carboxylase small chain C;
DE            Short=RuBisCO small subunit C;
DE   Flags: Precursor;
GN   Name=RBCS; Synonyms=RBCS-C; OrderedLocusNames=Os12g0274700, LOC_Os12g17600;
GN   ORFNames=OsJ_016909, OsJ_17688 {ECO:0000312|EMBL:EEE62884.1};
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 [GENOMIC DNA].
RX   PubMed=3412915; DOI=10.1093/nar/16.15.7749;
RA   Xie Y., Wu R.;
RT   "Nucleotide sequence of a ribulose-1,5-bisphosphate carboxylase/oxygenase
RT   small subunit gene (rbcS) in rice.";
RL   Nucleic Acids Res. 16:7749-7749(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RA   Matsuoka M., Kano-Murakami Y., Tanaka Y., Ozeki Y., Yamamoto N.;
RT   "Classification and nucleotide sequence of cDNA encoding the small subunit
RT   of ribulose-1,5-bisphosphate carboxylase from rice.";
RL   Plant Cell Physiol. 29:1015-1022(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ilpoombyeo;
RA   Yoon U.H., Hahn J.H., Yun C.-H., Eun M.Y.;
RT   "Molecular cloning and characterization of cDNA encoding the small subunit
RT   of ribulose 1,5-bisphosphate carboxylase in rice.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [9]
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   [10]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-54, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16758443; DOI=10.1002/pmic.200600043;
RA   Nozu Y., Tsugita A., Kamijo K.;
RT   "Proteomic analysis of rice leaf, stem and root tissues during growth
RT   course.";
RL   Proteomics 6:3665-3670(2006).
RN   [11] {ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK, ECO:0007744|PDB:3AXM}
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 48-175 OF ACTIVATED HOLOENZYME IN
RP   COMPLEX WITH MAGNESIUM AND NADP; 6-PHOSPHOGLUCONATE OR TRANSITION-STATE
RP   ANALOG 2-CABP, FUNCTION, AND SUBUNIT.
RC   STRAIN=cv. Notohikari; TISSUE=Leaf;
RX   PubMed=22609438; DOI=10.1016/j.jmb.2012.05.014;
RA   Matsumura H., Mizohata E., Ishida H., Kogami A., Ueno T., Makino A.,
RA   Inoue T., Yokota A., Mae T., Kai Y.;
RT   "Crystal structure of rice Rubisco and implications for activation induced
RT   by positive effectors NADPH and 6-phosphogluconate.";
RL   J. Mol. Biol. 422:75-86(2012).
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. Although the small subunit is not catalytic it is
CC       essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00860,
CC       ECO:0000305|PubMed:22609438}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:22609438}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00860}.
CC   -!- MISCELLANEOUS: NADPH and 6-phosphogluconate function as positive
CC       effectors to promote enzyme activation. {ECO:0000305|PubMed:22609438}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_00860, ECO:0000269|PubMed:22609438}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00860}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA30393.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA30393.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; X07515; CAA30393.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; D00643; BAA00538.1; -; mRNA.
DR   EMBL; AF052305; AAC14064.1; -; mRNA.
DR   EMBL; DP000011; ABA97056.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29578.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT16666.1; -; Genomic_DNA.
DR   EMBL; CM000142; EAZ33426.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE62884.1; -; Genomic_DNA.
DR   EMBL; AK061611; BAG88038.1; -; mRNA.
DR   EMBL; AK119219; BAG99587.1; -; mRNA.
DR   EMBL; AK121444; BAH00491.1; -; mRNA.
DR   PIR; JA0070; RKRZS9.
DR   PIR; S01235; RKRZS.
DR   RefSeq; XP_015619872.1; XM_015764386.1.
DR   PDB; 1WDD; X-ray; 1.35 A; S/W=48-175.
DR   PDB; 3AXK; X-ray; 1.90 A; S/T=48-175.
DR   PDB; 3AXM; X-ray; 1.65 A; S/T/U/V/W/X/Y/Z=48-175.
DR   PDB; 6KYI; X-ray; 1.75 A; S/T=1-175.
DR   PDBsum; 1WDD; -.
DR   PDBsum; 3AXK; -.
DR   PDBsum; 3AXM; -.
DR   PDBsum; 6KYI; -.
DR   AlphaFoldDB; Q0INY7; -.
DR   SMR; Q0INY7; -.
DR   STRING; 4530.OS12T0274700-01; -.
DR   PaxDb; Q0INY7; -.
DR   PRIDE; Q0INY7; -.
DR   EnsemblPlants; Os12t0274700-01; Os12t0274700-01; Os12g0274700.
DR   EnsemblPlants; Os12t0274700-02; Os12t0274700-02; Os12g0274700.
DR   GeneID; 4351966; -.
DR   Gramene; Os12t0274700-01; Os12t0274700-01; Os12g0274700.
DR   Gramene; Os12t0274700-02; Os12t0274700-02; Os12g0274700.
DR   KEGG; osa:4351966; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   HOGENOM; CLU_098114_1_0_1; -.
DR   InParanoid; Q0INY7; -.
DR   OMA; PQQNYSW; -.
DR   OrthoDB; 1258997at2759; -.
DR   BRENDA; 4.1.1.39; 4460.
DR   PlantReactome; R-OSA-1119312; Photorespiration.
DR   PlantReactome; R-OSA-1119519; Calvin cycle.
DR   EvolutionaryTrace; Q0INY7; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 12.
DR   ExpressionAtlas; Q0INY7; baseline and differential.
DR   Genevisible; Q0INY7; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; -; 1.
DR   HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; PTHR31262; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; SSF55239; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Direct protein sequencing; Photorespiration; Photosynthesis; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:16758443"
FT   TRANSIT         1..46
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT   CHAIN           47..175
FT                   /note="Ribulose bisphosphate carboxylase small subunit,
FT                   chloroplastic 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031537"
FT   REGION          60..64
FT                   /note="Interaction with large subunit"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   TURN            61..64
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           70..82
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:3AXM"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           126..139
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          143..151
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          156..164
FT                   /evidence="ECO:0007829|PDB:1WDD"
SQ   SEQUENCE   175 AA;  19647 MW;  E95B68AC3178A7D7 CRC64;
     MAPSVMASSA TTVAPFQGLK STAGMPVARR SGNSSFGNVS NGGRIRCMQV WPIEGIKKFE
     TLSYLPPLTV EDLLKQIEYL LRSKWVPCLE FSKVGFVYRE NHRSPGYYDG RYWTMWKLPM
     FGCTDATQVL KELEEAKKAY PDAFVRIIGF DNVRQVQLIS FIAYKPPGCE ESGGN
 
 
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