ID A1B2Q3_PARDP Unreviewed; 129 AA. AC A1B2Q3; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 87. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859}; DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859}; GN Name=cbbS {ECO:0000256|HAMAP-Rule:MF_00859}; GN OrderedLocusNames=Pden_1700 {ECO:0000313|EMBL:ABL69797.1}; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69797.1, ECO:0000313|Proteomes:UP000000361}; RN [1] {ECO:0000313|Proteomes:UP000000361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., RA Richardson P.; RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."; RL Submitted (DEC-2006) 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. 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:0000256|HAMAP-Rule:MF_00859}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000256|ARBA:ARBA00038826, ECO:0000256|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:0000256|HAMAP-Rule:MF_00859}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000256|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; CP000489; ABL69797.1; -; Genomic_DNA. DR RefSeq; WP_011747995.1; NC_008686.1. DR AlphaFoldDB; A1B2Q3; -. DR STRING; 318586.Pden_1700; -. DR EnsemblBacteria; ABL69797; ABL69797; Pden_1700. DR GeneID; 75501183; -. DR KEGG; pde:Pden_1700; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_5; -. DR OrthoDB; 9788955at2; -. DR Proteomes; UP000000361; Chromosome 1. 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 {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_00859}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00859}; Lyase {ECO:0000313|EMBL:ABL69797.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000361}. FT DOMAIN 4..103 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 129 AA; 15312 MW; BCC5D6059B360BD4 CRC64; MRITQGCFSF LPDLTDEQIR DQVEYILSRD WAVGIEFTDE PHPRNTYWEM WGNPMFDLKD AKGVMMELDE CRKAHGDSYI RINAFDSTRG WETVMMSFIV NRPKSEPGFR TWRMEADGRH IRYTHELVG //