ID F7YAX9_MESOW Unreviewed; 129 AA. AC F7YAX9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 24-JAN-2024, entry version 44. 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=Mesop_5542 {ECO:0000313|EMBL:AEH89955.1}; OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH89955.1, ECO:0000313|Proteomes:UP000001623}; RN [1] {ECO:0000313|EMBL:AEH89955.1, ECO:0000313|Proteomes:UP000001623} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075 RC {ECO:0000313|Proteomes:UP000001623}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P., RA Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.; RT "Complete sequence of Mesorhizobium opportunistum WSM2075."; RL Submitted (OCT-2010) 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; CP002279; AEH89955.1; -; Genomic_DNA. DR RefSeq; WP_013896592.1; NC_015675.1. DR AlphaFoldDB; F7YAX9; -. DR STRING; 536019.Mesop_5542; -. DR KEGG; mop:Mesop_5542; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_5; -. DR Proteomes; UP000001623; Chromosome. 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:AEH89955.1}. FT DOMAIN 4..103 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 129 AA; 15010 MW; 16C2264CE994B5B7 CRC64; MRITQGTFSF LPDLSDEQIS AQVEYCLRKE WSIGVEYTDD PHPRNIFWEM WGNPMFDLKD AAGVMMEVRA CRVAQPDSYI RLNAFDSSRG FETVMLSFIV NRPKVEPKFV LTRTETDSRV QRYSMKAAL //