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 27-MAR-2024, entry version 114. 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; GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39947.Q0INY7; -. DR PaxDb; 39947-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; IRNNWIP; -. DR OrthoDB; 5482775at2759; -. 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 GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. DR CDD; cd03527; RuBisCO_small; 1. DR Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31262:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 2; 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; RuBisCO, small subunit; 1. DR Genevisible; Q0INY7; OS. 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 //