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}.
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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
//
