ID RBSP_CUPNH Reviewed; 139 AA. AC Q59102; Q59103; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 134. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, plasmid {ECO:0000303|PubMed:7543477}; DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00859}; GN Name=cbbS {ECO:0000255|HAMAP-Rule:MF_00859}; GN Synonyms=cbbSP, cbxSP, cfxSP, rbcS; OrderedLocusNames=PHG426; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OG Plasmid megaplasmid pHG1. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7543477; DOI=10.1128/jb.177.15.4442-4450.1995; RA Kusian B., Bednarski R., Husemann M., Bowien B.; RT "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase RT genes and cbb promoters of Alcaligenes eutrophus."; RL J. Bacteriol. 177:4442-4450(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337; RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5; RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.; RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."; RL J. Mol. Biol. 332:369-383(2003). 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_00859}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00859}. 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; U20584; AAA83746.1; -; Genomic_DNA. DR EMBL; U20585; AAA83748.1; -; Genomic_DNA. DR EMBL; AY305378; AAP86175.1; -; Genomic_DNA. DR PIR; I39558; I39558. DR PIR; I39560; I39560. DR RefSeq; WP_011154338.1; NZ_CP039289.1. DR AlphaFoldDB; Q59102; -. DR SMR; Q59102; -. DR STRING; 381666.H16_B1394; -. DR GeneID; 39976389; -. DR KEGG; reh:PHG426; -. DR PATRIC; fig|381666.6.peg.354; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_4; -. DR OrthoDB; 9788955at2; -. DR Proteomes; UP000008210; Plasmid megaplasmid pHG1. 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; Plasmid; Reference proteome. FT CHAIN 1..139 FT /note="Ribulose bisphosphate carboxylase small subunit, FT plasmid" FT /id="PRO_0000198608" FT CONFLICT 105 FT /note="D -> E (in Ref. 1; AAA83746)" FT /evidence="ECO:0000305" FT CONFLICT 121 FT /note="I -> M (in Ref. 1; AAA83746)" FT /evidence="ECO:0000305" SQ SEQUENCE 139 AA; 15985 MW; 96B373592929C454 CRC64; MRITQGTFSF LPDLTDAQIT SQLEYCLNQG WAVGIEYTDD PHPRNTYWEM FGLPMFDLRD AAGILLEINN ARSTFPNHYI RVTAFDSTHT VESVVMSFIV NRPADEPGFR LVRQEEPGRT IRYSIESYAV QARPEGSRY //