ID RBL_PTEVI Reviewed; 440 AA. AC Q33015; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 22-FEB-2023, entry version 96. 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: Fragment; GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338}; OS Pteris vittata (Chinese ladder brake). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae; OC Pteridoideae; Pteris; Pteris subgen. Pteris; Pteris sect. Pteris. OX NCBI_TaxID=13821; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Leaf; RX PubMed=7697195; DOI=10.1006/mpev.1994.1044; RA Wolf P.G., Soltis P.S., Soltis D.E.; RT "Phylogenetic relationships of dennstaedtioid ferns: evidence from rbcL RT sequences."; RL Mol. Phylogenet. Evol. 3:383-392(1994). 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; U05941; AAC48966.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. 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 Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond; Lyase; KW Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase; KW Photorespiration; Photosynthesis; Plastid. FT CHAIN <1..>440 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000062577" FT ACT_SITE 165 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT ACT_SITE 284 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 113 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 191 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 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 285 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT SITE 324 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 4 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 191 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT DISULFID 237 FT /note="Interchain; in linked form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT NON_TER 1 FT NON_TER 440 SQ SEQUENCE 440 AA; 48575 MW; 904A064E8BB40578 CRC64; VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE GSVTNMLTSI VGNVFGXKAX RALRLEDLRI LPAYSKTFIG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL CAKNYGRAVY ECLRGGLDFT KDDENVNSQP SMRWRDRFLF VAEALFKAQA ETGEVKGHYL NATAGTCEEM IKRATFAREL GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQRNHGMH LRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK //