ID RBL_CHAVU Reviewed; 475 AA. AC Q1ACK0; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 22-FEB-2023, entry version 69. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338}; DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338}; DE Flags: Precursor; GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338}; OS Chara vulgaris (Common stonewort). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae; OC Chara. OX NCBI_TaxID=55564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16611644; DOI=10.1093/molbev/msk018; RA Turmel M., Otis C., Lemieux C.; RT "The chloroplast genome sequence of Chara vulgaris sheds new light into the RT closest green algal relatives of land plants."; RL Mol. Biol. Evol. 23:1324-1338(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 in the photorespiration process. Both reactions occur CC simultaneously and in competition at the same active site. CC {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5- CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, CC ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01338}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, CC ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01338}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338}; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; CC disulfide-linked. The disulfide link is formed within the large subunit CC homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- PTM: The disulfide bond which can form in the large chain dimeric CC partners within the hexadecamer appears to be associated with oxidative CC stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}. 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_01338}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}. 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; DQ229107; ABA61952.1; -; Genomic_DNA. DR RefSeq; YP_635747.1; NC_008097.1. DR AlphaFoldDB; Q1ACK0; -. DR SMR; Q1ACK0; -. DR GeneID; 4100318; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. 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; cd08212; RuBisCO_large_I; 1. DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1. DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1. DR HAMAP; MF_01338; RuBisCO_L_type1; 1. DR InterPro; IPR033966; RuBisCO. DR InterPro; IPR020878; RuBisCo_large_chain_AS. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR036376; RuBisCO_lsu_C_sf. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR InterPro; IPR036422; RuBisCO_lsu_N_sf. DR InterPro; IPR020888; RuBisCO_lsuI. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDG01052; RuBisCO; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1. DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; KW Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation; KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid. FT PROPEP 1..2 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT /id="PRO_0000251418" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000251419" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT ACT_SITE 294 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 123 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 295 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 379 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT SITE 334 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 3 FT /note="N-acetylproline" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 14 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 201 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT DISULFID 247 FT /note="Interchain; in linked form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" SQ SEQUENCE 475 AA; 52700 MW; AD02CA001E110B06 CRC64; MSPQTETKTS AGFKAGVKDY RLTYYTPEYK TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQFIAY VAYPLDLFEE GSVTNLFTSI VGNVFGFKAL RALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKSQA ETGEIKGHYL NATAGTCEEM LKRAQCAREL GMPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV LDRQKNHGMH FRVLAKALRL SGGDHVHSGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR GVYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFE TIDTL //