ID RBL_PEA Reviewed; 475 AA. AC P04717; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 3. DT 24-JAN-2024, entry version 131. 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 Pisum sativum (Garden pea) (Lathyrus oleraceus). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3714502; DOI=10.1093/nar/14.9.3975; RA Zurawski G., Whitfeld P.R., Bottomley W.; RT "Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate RT carboxylase from pea chloroplasts."; RL Nucleic Acids Res. 14:3975-3976(1986). RN [2] RP PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, AND ACETYLATION AT PRO-3. RX PubMed=16668742; DOI=10.1104/pp.98.3.1170; RA Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.; RT "Posttranslational modifications in the amino-terminal region of the large RT subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several RT plant species."; RL Plant Physiol. 98:1170-1174(1992). RN [3] {ECO:0007744|PDB:4HHH} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF INACTIVE HOLOENZYME IN COMPLEX RP WITH RIBULOSE 1,5-BISPHOSPHATE, AND SUBUNIT. RX PubMed=23295478; DOI=10.1107/s1744309112047549; RA Loewen P.C., Didychuk A.L., Switala J., Perez-Luque R., Fita I., RA Loewen M.C.; RT "Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate."; RL Acta Crystallogr. F 69:10-14(2013). RN [4] {ECO:0007744|PDB:4MKV} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 12-469 OF INACTIVE HOLOENZYME IN RP COMPLEX WITH RIBULOSE 1,5-BISPHOSPHATE AND ABSCISIC ACID, SUBUNIT, AND RP DISULFIDE BOND. RX PubMed=26197050; DOI=10.1371/journal.pone.0133033; RA Galka M.M., Rajagopalan N., Buhrow L.M., Nelson K.M., Switala J., RA Cutler A.J., Palmer D.R., Loewen P.C., Abrams S.R., Loewen M.C.; RT "Identification of Interactions between Abscisic Acid and Ribulose-1,5- RT Bisphosphate Carboxylase/Oxygenase."; RL PLoS ONE 10:e0133033-e0133033(2015). 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 (Probable). CC Binds to abscisic acid (ABA); only half of the possible binding sites CC are occupied in the crystal and there are indications this is a low CC affinity site (PubMed:26197050). {ECO:0000269|PubMed:26197050, CC ECO:0000305|PubMed:23295478, ECO:0000305|PubMed:26197050}. 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, ECO:0000305|PubMed:23295478, CC ECO:0000305|PubMed:26197050}; 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 ECO:0000305|PubMed:23295478, ECO:0000305|PubMed:26197050}; 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 (PubMed:23295478). Heterohexadecamer; disulfide-linked. The disulfide CC link is formed within the large subunit homodimers (PubMed:26197050). CC {ECO:0000269|PubMed:23295478, ECO:0000269|PubMed:26197050}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_01338}. 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:0000250|UniProtKB:P11383}. 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, ECO:0000269|PubMed:23295478, CC ECO:0000269|PubMed:26197050}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA27483.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; X03853; CAA27483.1; ALT_INIT; Genomic_DNA. DR PIR; A24471; RKPMLC. DR RefSeq; YP_003587524.1; NC_014057.1. DR PDB; 4HHH; X-ray; 2.20 A; A/B/C/D=1-475. DR PDB; 4MKV; X-ray; 2.15 A; A/B/C/D=12-469. DR PDBsum; 4HHH; -. DR PDBsum; 4MKV; -. DR AlphaFoldDB; P04717; -. DR SMR; P04717; -. DR iPTMnet; P04717; -. DR GeneID; 9073048; -. DR BRENDA; 4.1.1.39; 4872. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation; KW Chloroplast; Direct protein sequencing; Disulfide bond; Lyase; Magnesium; KW Metal-binding; Methylation; Monooxygenase; Oxidoreductase; KW Photorespiration; Photosynthesis; Plastid. FT PROPEP 1..2 FT /evidence="ECO:0000269|PubMed:16668742" FT /id="PRO_0000031333" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000031334" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 294 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 177 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000250" FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 327 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 334 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 379 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 381 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 403 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT BINDING 404 FT /ligand="D-ribulose 1,5-bisphosphate" FT /ligand_id="ChEBI:CHEBI:57870" FT /evidence="ECO:0000269|PubMed:26197050, FT ECO:0007744|PDB:4MKV" FT SITE 334 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 3 FT /note="N-acetylproline" FT /evidence="ECO:0000269|PubMed:16668742" FT MOD_RES 14 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:16668742" FT MOD_RES 201 FT /note="N6-carboxylysine" FT /evidence="ECO:0000250" FT DISULFID 247 FT /note="Interchain; in linked form" FT /evidence="ECO:0000250, ECO:0007744|PDB:4MKV" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 50..60 FT /evidence="ECO:0007829|PDB:4MKV" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:4HHH" FT HELIX 70..74 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 113..121 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 130..139 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:4HHH" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 182..194 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 214..232 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 247..260 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 274..287 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 311..321 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 331..335 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 387..394 FT /evidence="ECO:0007829|PDB:4MKV" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 404..407 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 413..432 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 437..448 FT /evidence="ECO:0007829|PDB:4MKV" FT TURN 449..451 FT /evidence="ECO:0007829|PDB:4MKV" FT HELIX 453..462 FT /evidence="ECO:0007829|PDB:4MKV" SQ SEQUENCE 475 AA; 52763 MW; 1F673855DD921DF9 CRC64; MSPQTETKAK VGFKAGVKDY KLTYYTPDYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYEIEPV PGEDNQFIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PYAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM LKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDYIKKDRSR GIYFTQDWVS LPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNAIIREACK WSPELAAACE VWKEIKFEFP AMDTL //