RBL_PEA
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 03-AUG-2022, entry version 128.
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).
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;
CC Evidence={ECO:0000255|HAMAP-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};
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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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 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
