ID Q3JE88_NITOC Unreviewed; 145 AA. AC Q3JE88; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 91. 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=Noc_0332 {ECO:0000313|EMBL:ABA56858.1}; OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB OS 11848 / C-107). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Nitrosococcus. OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA56858.1, ECO:0000313|Proteomes:UP000006838}; RN [1] {ECO:0000313|Proteomes:UP000006838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107 RC {ECO:0000313|Proteomes:UP000006838}; RX PubMed=16957257; DOI=10.1128/AEM.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., RA Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia- RT oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). 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; CP000127; ABA56858.1; -; Genomic_DNA. DR RefSeq; WP_011330305.1; NC_007484.1. DR AlphaFoldDB; Q3JE88; -. DR STRING; 323261.Noc_0332; -. DR KEGG; noc:Noc_0332; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_6; -. DR InParanoid; Q3JE88; -. DR Proteomes; UP000006838; 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:ABA56858.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006838}. FT DOMAIN 10..109 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 145 AA; 16935 MW; 66886402EAD96369 CRC64; MMTNHGNRIT QGQFSFLPDL TDEQILAQIK YALKNDWAVN VEYTDDPHPR NTYWEMFGIP MFDLKDPAGI MMEINDCRKT YPNHYVRVTA FNSHRGVESP CMSFIVNRPK NEPGFGLVRQ EVDGRHINYT VRSYAADRPE GERYQ //