AC MF_01338; DC Protein; auto TR HAMAP; MF_01338; -; 1; level=0 XX Names: RuBisCO_L_type1 XX ID RBL case and DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; DE Flags: Precursor; GN Name=rbcL; else case and not DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; GN Name=rbcL; else case DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; GN Name=cbbL; Synonyms=rbcL; else case not and not DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; GN Name=cbbL; end case XX case or 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. else case not and not 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. end case 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; 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; case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; end case case 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. else CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. end case case CC -!- SUBCELLULAR LOCATION: Carboxysome. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case case 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. end case 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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. XX DR PROSITE; PS00157; RUBISCO_LARGE; 1; trigger=no DR Pfam; PF00016; RuBisCO_large; 1; trigger=no DR Pfam; PF02788; RuBisCO_large_N; 1; trigger=no XX case KW Acetylation end case case KW Carboxysome end case KW Calvin cycle KW Carbon dioxide fixation case KW Disulfide bond end case KW Lyase case KW Magnesium KW Metal-binding end case case KW Methylation end case KW Monooxygenase KW Oxidoreductase case or KW Photorespiration end case case or KW Photosynthesis end case XX case GO GO:0000287; F:magnesium ion binding end case GO GO:0015977; P:carbon fixation GO GO:0016984; F:ribulose-bisphosphate carboxylase activity GO GO:0019253; P:reductive pentose-phosphate cycle case GO GO:0031470; C:carboxysome end case case GO GO:0009507; C:chloroplast end case XX FT From: RBL_TOBAC (P00876) case FT PROPEP 1..2 FT CHAIN 3..Cter FT /note="Ribulose bisphosphate carboxylase large chain" end case FT SITE 334 FT /note="Transition state stabilizer" FT Condition: K FT ACT_SITE 175 FT /note="Proton acceptor" FT Condition: K FT ACT_SITE 294 FT /note="Proton acceptor" FT Condition: H FT BINDING 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT Group: 1; Condition: K FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: E FT BINDING 123 FT /ligand="substrate" FT /note="in homodimeric partner" FT Condition: N FT BINDING 173 FT /ligand="substrate" FT Condition: T FT BINDING 177 FT /ligand="substrate" FT Condition: K FT BINDING 295 FT /ligand="substrate" FT Condition: R FT BINDING 327 FT /ligand="substrate" FT Condition: H FT BINDING 379 FT /ligand="substrate" FT Condition: S case FT MOD_RES 3 FT /note="N-acetylproline" FT Condition: P FT MOD_RES 14 FT /note="N6,N6,N6-trimethyllysine" FT Condition: K end case FT MOD_RES 201 FT /note="N6-carboxylysine" FT Condition: K FT DISULFID 247 FT /note="Interchain; in linked form" FT Optional; Condition: C XX Size: 463-501; Related: MF_01133; MF_01339; Template: P00876; P0C2C2; P00880; P00877; P0C512; P00875; F4CQ77; Q31NB3; Scope: Bacteria; Cyanobacteriota Bacteria; Pseudomonadota Bacteria; Actinomycetota Bacteria; Verrucomicrobiota Plastid Fusion: Nter: None Cter: None Duplicate: in BRASB, BRASO, CHRVI, HYDMR, METPP, NITSX, RALEU, CERS5, ACIFR Plasmid: in PARP8, OLICA, RALEU, RHIME, CERS5 Comments: None XX # Revision 1.50 2023/02/17 //