ID RBS_THANO Reviewed; 139 AA. AC O98948; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 22-FEB-2023, entry version 82. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000255|HAMAP-Rule:MF_00859}; DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859}; GN Name=rbcS {ECO:0000255|HAMAP-Rule:MF_00859}; OS Thalassiosira nordenskioeldii (Marine diatom). OG Plastid; Chloroplast. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales; OC Thalassiosiraceae; Thalassiosira. OX NCBI_TaxID=83372; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tomizawa K.; RT "Structure and function study of ribulose-1,5-bisphosphate RT carboxylase/oxygenase of the marine diatom, Thalassiosira RT nordenskioeldii."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. 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 in the photorespiration process. Both reactions occur CC simultaneously and in competition at the same active site. Although the CC small subunit is not catalytic it is essential for maximal activity. CC {ECO:0000255|HAMAP-Rule:MF_00859}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00859}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_00859}. CC -!- MISCELLANEOUS: In this alga, in contrast to plants, the small subunit CC is encoded in the chloroplast. 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_00859}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000255|HAMAP-Rule:MF_00859}. 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; AB018007; BAA75795.1; -; Genomic_DNA. DR AlphaFoldDB; O98948; -. DR SMR; O98948; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. 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; IPR036385; RuBisCO_ssu_sf. DR PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31262:SF23; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT; 1. DR Pfam; PF00101; RuBisCO_small; 1. DR SMART; SM00961; RuBisCO_small; 1. DR SUPFAM; SSF55239; RuBisCO, small subunit; 1. PE 3: Inferred from homology; KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration; KW Photosynthesis; Plastid. FT CHAIN 1..139 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /id="PRO_0000198606" SQ SEQUENCE 139 AA; 15897 MW; 7112892F351D10A7 CRC64; MRLTQGCFSF LPDLTDTQIE KQVAYAMNKG WAMNVEWTDD PHPRNNYWEL WGLPLFDIKD PATVMFELNE ARKSCASGYI RINAFDASYG VESCVMSFIT NRPATEPGFY LDRTEGPGRQ VIYSIKSYSV QANPEGSRY //