ID RBL_CHLRE Reviewed; 475 AA. AC P00877; B7U1I9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 163. 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; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBOXYLATION AT LYS-201. RX PubMed=6302265; DOI=10.1016/0022-2836(82)90547-2; RA Dron M., Rahire M., Rochaix J.-D.; RT "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii RT containing the gene of the large subunit of ribulose bisphosphate RT carboxylase and parts of its flanking genes."; RL J. Mol. Biol. 162:775-793(1982). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503; RX PubMed=19473533; DOI=10.1186/1471-2148-9-120; RA Smith D.R., Lee R.W.; RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: RT addressing the mutational-hazard hypothesis."; RL BMC Evol. Biol. 9:120-120(2009). RN [3] RP PROTEIN SEQUENCE OF 3-14, 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 [4] RP IDENTIFICATION, AND COMPLETE PLASTID GENOME. RX PubMed=12417694; DOI=10.1105/tpc.006155; RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., RA Stern D.B.; RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a RT sea of repeats."; RL Plant Cell 14:2659-2679(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH RP TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT, HYDROXYLATION AT RP PRO-104 AND PRO-151, CARBOXYLATION AT LYS-201, AND METHYLATION AT CYS-256 RP AND CYS-369. RC STRAIN=2137; RX PubMed=11641402; DOI=10.1074/jbc.m107765200; RA Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.; RT "First crystal structure of Rubisco from a green alga, Chlamydomonas RT reinhardtii."; RL J. Biol. Chem. 276:48159-48164(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF RP ACTIVATED HOLOENZYME IN COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND RP MAGNESIUM, FUNCTION, SUBUNIT, DISULFIDE BONDS, CARBOXYLATION AT LYS-201, RP HYDROXYLATION AT PRO-104 AND PRO-151, AND METHYLATION AT CYS-256 AND RP CYS-369. RC STRAIN=137c / CC-125; RX PubMed=11866526; DOI=10.1006/jmbi.2001.5381; RA Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J., RA Kato K., Shibata N., Inoue T., Yokota A., Kai Y.; RT "Crystal structure of activated ribulose-1,5-bisphosphate RT carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed RT with 2-carboxyarabinitol-1,5-bisphosphate."; RL J. Mol. Biol. 316:679-691(2002). 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:0000269|PubMed:11866526}. 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11641402, CC ECO:0000269|PubMed:11866526}; 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:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- PTM: The disulfide bond which can form between Cys-247 in the large CC chain dimeric partners within the hexadecamer appears to be associated CC with oxidative stress and protein turnover (By similarity). The CC disulfide bond reported in 1IR2 may be the result of oxidation during CC crystallization. {ECO:0000250|UniProtKB:P11383, ECO:0000305}. CC -!- PTM: The electron density found in the position of Thr-471 suggests it CC is either O-methylthreonine, or Ile, which may be produced by RNA CC editing (PubMed:11866526). {ECO:0000305|PubMed:11866526}. 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:0000269|PubMed:11641402}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {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; J01399; AAA84449.1; -; Genomic_DNA. DR EMBL; FJ423446; ACJ50136.1; -; Genomic_DNA. DR EMBL; BK000554; DAA00950.1; -; Genomic_DNA. DR PIR; A01097; RKKML. DR RefSeq; NP_958405.1; NC_005353.1. DR PDB; 1GK8; X-ray; 1.40 A; A/C/E/G=1-475. DR PDB; 1IR2; X-ray; 1.84 A; A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z=1-475. DR PDB; 1UW9; X-ray; 2.05 A; A/B/E/H/K/O/R/V=1-475. DR PDB; 1UWA; X-ray; 2.30 A; A/B/E/H/K/O/R/V=1-475. DR PDB; 1UZD; X-ray; 2.40 A; A/B/E/H/K/O/R/V=1-475. DR PDB; 1UZH; X-ray; 2.20 A; A/B/E/H/K/O/R/V=1-475. DR PDB; 2V63; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2V67; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2V68; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2V69; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2V6A; X-ray; 1.50 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2VDH; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 2VDI; X-ray; 2.65 A; A/B/C/D/E/F/G/H=1-475. DR PDB; 5BS2; X-ray; 1.97 A; A/B=462-473, R=462-467. DR PDB; 7JFO; EM; 2.13 A; A/C/E/G/I/K/M/O=1-475. DR PDB; 7JN4; EM; 2.68 A; A/C/E/G/I/K/M/O=1-475. DR PDB; 7JSX; EM; 2.06 A; A/C/E/G/I/K/M/O=1-475. DR PDBsum; 1GK8; -. DR PDBsum; 1IR2; -. DR PDBsum; 1UW9; -. DR PDBsum; 1UWA; -. DR PDBsum; 1UZD; -. DR PDBsum; 1UZH; -. DR PDBsum; 2V63; -. DR PDBsum; 2V67; -. DR PDBsum; 2V68; -. DR PDBsum; 2V69; -. DR PDBsum; 2V6A; -. DR PDBsum; 2VDH; -. DR PDBsum; 2VDI; -. DR PDBsum; 5BS2; -. DR PDBsum; 7JFO; -. DR PDBsum; 7JN4; -. DR PDBsum; 7JSX; -. DR AlphaFoldDB; P00877; -. DR EMDB; EMD-22308; -. DR EMDB; EMD-22401; -. DR EMDB; EMD-22462; -. DR SMR; P00877; -. DR STRING; 3055.P00877; -. DR iPTMnet; P00877; -. DR PaxDb; 3055-DAA00950; -. DR GeneID; 2717040; -. DR KEGG; cre:ChreCp049; -. DR eggNOG; ENOG502QTI9; Eukaryota. DR HOGENOM; CLU_031450_2_0_1; -. DR InParanoid; P00877; -. DR BioCyc; CHLAMY:CHRECP049-MONOMER; -. DR EvolutionaryTrace; P00877; -. DR Proteomes; UP000006906; Chloroplast. 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; Hydroxylation; KW Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase; KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid; KW Reference proteome. FT PROPEP 1..2 FT /evidence="ECO:0000269|PubMed:16668742" FT /id="PRO_0000031175" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000031176" FT ACT_SITE 175 FT /note="Proton acceptor" FT ACT_SITE 294 FT /note="Proton acceptor" FT BINDING 123 FT /ligand="substrate" FT /note="in homodimeric partner" FT BINDING 173 FT /ligand="substrate" FT BINDING 177 FT /ligand="substrate" FT BINDING 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT BINDING 295 FT /ligand="substrate" FT BINDING 327 FT /ligand="substrate" FT BINDING 379 FT /ligand="substrate" FT SITE 334 FT /note="Transition state stabilizer" FT MOD_RES 3 FT /note="N-acetylproline" FT /evidence="ECO:0000269|PubMed:16668742" FT MOD_RES 104 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT MOD_RES 151 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT MOD_RES 201 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526, ECO:0000269|PubMed:6302265" FT MOD_RES 256 FT /note="S-methylcysteine" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT MOD_RES 369 FT /note="S-methylcysteine" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT DISULFID 247 FT /note="Interchain; in linked form" FT /evidence="ECO:0000269|PubMed:11641402, FT ECO:0000269|PubMed:11866526" FT VARIANT 46 FT /note="L -> P (in strain: 137c and CC-503)" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 50..60 FT /evidence="ECO:0007829|PDB:1GK8" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1GK8" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:7JSX" FT HELIX 70..74 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:2V6A" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 113..121 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 130..139 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 182..194 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7JN4" FT HELIX 214..232 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 247..260 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 274..287 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 311..321 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 331..335 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 387..394 FT /evidence="ECO:0007829|PDB:1GK8" FT STRAND 396..401 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 404..407 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 413..432 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 437..451 FT /evidence="ECO:0007829|PDB:1GK8" FT HELIX 453..462 FT /evidence="ECO:0007829|PDB:1GK8" SQ SEQUENCE 475 AA; 52543 MW; 5A9BFD394CF7D4D4 CRC64; MVPQTETKAG AGFKAGVKDY RLTYYTPDYV VRDTDILAAF RMTPQLGVPP EECGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEDNQYIAY VAYPIDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYVKTFVG PPHGIQVERD KLNKYGRGLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKAQA ETGEVKGHYL NATAGTCEEM MKRAVCAKEL GVPIIMHDYL TGGFTANTSL AIYCRDNGLL LHIHRAMHAV IDRQRNHGIH FRVLAKALRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR DDYVEKDRSR GIYFTQDWCS MPGVMPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP WGNAPGAAAN RVALEACTQA RNEGRDLARE GGDVIRSACK WSPELAAACE VWKEIKFEFD TIDKL //