ID RBL_ADICA Reviewed; 475 AA. AC P36476; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 118. 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 Adiantum capillus-veneris (Maidenhair fern). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae; OC Vittarioideae; Adiantum. OX NCBI_TaxID=13818; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Leaf; RX PubMed=8283479; DOI=10.1007/bf00160428; RA Hasebe M., Ito M., Kofuji R., Ueda K., Iwatsuki K.; RT "Phylogenetic relationships of ferns deduced from rbcL gene sequence."; RL J. Mol. Evol. 37:476-482(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. H3; RX PubMed=12755170; DOI=10.1093/dnares/10.2.59; RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.; RT "Complete nucleotide sequence of the chloroplast genome from a RT leptosporangiate fern, Adiantum capillus-veneris L."; RL DNA Res. 10:59-65(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ABSENCE OF RNA EDITING. RC STRAIN=cv. H3; TISSUE=Frond; RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018; RA Wolf P.G., Rowe C.A., Hasebe M.; RT "High levels of RNA editing in a vascular plant chloroplast genome: RT analysis of transcripts from the fern Adiantum capillus-veneris."; RL Gene 339:89-97(2004). 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(+) = D-ribulose 1,5- CC bisphosphate + CO2 + 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 = 2-phosphoglycolate + (2R)- CC 3-phosphoglycerate + 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; D14880; BAA03599.1; -; Genomic_DNA. DR EMBL; AY178864; AAP29399.1; -; Genomic_DNA. DR RefSeq; NP_848068.1; NC_004766.1. DR AlphaFoldDB; P36476; -. DR SMR; P36476; -. DR GeneID; 807346; -. DR Proteomes; UP000886520; Chloroplast. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. DR CDD; cd08212; RuBisCO_large_I; 1. DR FunFam; 3.20.20.110:FF:000001; Ribulose bisphosphate carboxylase large chain; 1. DR FunFam; 3.30.70.150:FF:000001; Ribulose bisphosphate carboxylase large chain; 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 NCBIfam; NF003252; PRK04208.1; 1. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF17; 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 2: Evidence at transcript level; KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; KW Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation; KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid; KW Reference proteome. FT PROPEP 1..2 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT /id="PRO_0000031101" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000031102" 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; 52634 MW; DF0BFC53861EA998 CRC64; MSPQTETKAG VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE GSVTNMLTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFLG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEALFKSQA ETGEIKGHYL NATAGTCEEM MKRAVFAREL GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQKNHGIH FRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS MPGVFPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE IWKAIKFEFE TIDTL //