ID RBS3_FRIAG Reviewed; 179 AA. AC O22573; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 {ECO:0000255|HAMAP-Rule:MF_00860}; DE Short=RuBisCO small subunit 3 {ECO:0000255|HAMAP-Rule:MF_00860}; DE Flags: Precursor; GN Name=RBCS3 {ECO:0000255|HAMAP-Rule:MF_00860}; OS Fritillaria agrestis (Stinkbells). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Fritillaria. OX NCBI_TaxID=64177; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Panico E., Baysdorfer C.; RL Submitted (SEP-1997) 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:0000255|HAMAP-Rule:MF_00860}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00860}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_00860}. 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_00860}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000255|HAMAP-Rule:MF_00860}. 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; AF024574; AAB84181.1; -; mRNA. DR AlphaFoldDB; O22573; -. DR SMR; O22573; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW. 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; IPR024680; RuBisCO_ssu_N. DR InterPro; IPR036385; RuBisCO_ssu_sf. DR PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31262:SF10; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 2; 1. DR Pfam; PF12338; RbcS; 1. DR Pfam; PF00101; RuBisCO_small; 1. DR PRINTS; PR00152; RUBISCOSMALL. DR SMART; SM00961; RuBisCO_small; 1. DR SUPFAM; SSF55239; RuBisCO, small subunit; 1. PE 2: Evidence at transcript level; KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Photorespiration; KW Photosynthesis; Plastid; Transit peptide. FT TRANSIT 1..58 FT /note="Chloroplast" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860" FT CHAIN 59..179 FT /note="Ribulose bisphosphate carboxylase small subunit, FT chloroplastic 3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860" FT /id="PRO_0000031502" SQ SEQUENCE 179 AA; 19615 MW; D2C68A6CC0E0BF66 CRC64; MASSATMLSS VATAARAAPA QASMVAPFVG LKSASAFPVT QKPATGLSTL PSNGGRVQCM KVWPIVGLKK FETLSYLPTL SVESLLKQIE YLIRNGWVPC LEFSLEGFVS RDNNKSPGYY DGRYWTMWKL PMFGCTDAAQ VVKEAAECKK EYPAAFIRVI GFDNVRQVQC VSFIVEKPE //