ID E1Z3C9_CHLVA Unreviewed; 184 AA. AC E1Z3C9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 50. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860}; DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00860}; GN Name=RBCS {ECO:0000256|HAMAP-Rule:MF_00860}; GN ORFNames=CHLNCDRAFT_29368 {ECO:0000313|EMBL:EFN60145.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae; OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN60145.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN60145.1, RC ECO:0000313|Proteomes:UP000008141}; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). 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_00860, CC ECO:0000256|RuleBase:RU003627}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|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:0000256|HAMAP-Rule:MF_00860}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}. 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; GL433835; EFN60145.1; -; Genomic_DNA. DR RefSeq; XP_005852247.1; XM_005852185.1. DR AlphaFoldDB; E1Z3C9; -. DR SMR; E1Z3C9; -. DR STRING; 554065.E1Z3C9; -. DR GeneID; 17359197; -. DR KEGG; cvr:CHLNCDRAFT_29368; -. DR eggNOG; ENOG502QTPB; Eukaryota. DR InParanoid; E1Z3C9; -. DR OMA; VIHISYT; -. DR OrthoDB; 5482775at2759; -. DR Proteomes; UP000008141; Unassembled WGS sequence. 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-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:SF28; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT, CHLOROPLASTIC 1; 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 3: Inferred from homology; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00860}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_00860}; KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00860}; KW Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}. FT DOMAIN 54..170 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 184 AA; 20675 MW; 14C8D6EB216CBB93 CRC64; MASTVAAIAP VAVRPMASTP LKQAKNTFAA RTVSNGSIKK VSAMQVWTPL NNKMFETFSF LPPLTDGEIS RQVDYIVRNG WTPCLEFADA DHAYVDDTST IRLRGNAVPL YYDNRYWCMW KLPMFGCTDG QQVLREIQNC RRAFPDAYIR LVGFDSVRQV QVAGLLVNRP ASVRDYQSPS TRSV //