ID F8GEW4_NITSI Unreviewed; 118 AA. AC F8GEW4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 45. 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=Nit79A3_1254 {ECO:0000313|EMBL:AEJ01096.1}; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01096.1}; RN [1] {ECO:0000313|EMBL:AEJ01096.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01096.1}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J., RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.; RT "Complete sequence of Nitrosomonas sp. Is79A3."; RL Submitted (JUN-2011) 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|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; CP002876; AEJ01096.1; -; Genomic_DNA. DR AlphaFoldDB; F8GEW4; -. DR STRING; 261292.Nit79A3_1254; -. DR KEGG; nii:Nit79A3_1254; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_4; -. DR OrthoDB; 9788955at2; -. 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 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}. FT DOMAIN 18..115 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 118 AA; 13662 MW; E4697D6D0D6A41FA CRC64; MSEVIDYKSR VSDPASRKFE TFSYLPAMSD KDIKKQVQYL ISKGWNPAIE HTEPEYVMDS YWYMWKLPMF GETDVDRVLA EAAACHKANP NNHVRLIGYN NFNQSQGTAM VIYRGKTV //