RBL_TOBAC
ID RBL_TOBAC Reviewed; 477 AA.
AC P00876; Q32716;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39 {ECO:0000269|PubMed:3681999};
DE Flags: Precursor;
GN Name=rbcL; Synonyms=rbcA;
OS Nicotiana tabacum (Common tobacco).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7160620; DOI=10.1016/0378-1119(82)90090-7;
RA Shinozaki K., Sugiura M.;
RT "The nucleotide sequence of the tobacco chloroplast gene for the large
RT subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL Gene 20:91-102(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA Tohdoh N., Shimada H., Sugiura M.;
RT "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT gene organization and expression.";
RL EMBO J. 5:2043-2049(1986).
RN [3]
RP PROTEIN SEQUENCE OF 5-477, AND VARIANTS VAL-394 AND MET-405.
RA Amiri I., Salnikow J., Vater J.;
RT "Amino-acid sequence of the large subunit of D-ribulose bisphosphate
RT carboxylase/oxygenase from Nicotiana tabacum.";
RL Biochim. Biophys. Acta 784:116-123(1984).
RN [4]
RP PROTEIN SEQUENCE OF 3-18, FUNCTION, ACETYLATION AT PRO-3, AND METHYLATION
RP AT LYS-14.
RX PubMed=2928307; DOI=10.1073/pnas.86.6.1855;
RA Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.;
RT "Post-translational modifications in the large subunit of ribulose
RT bisphosphate carboxylase/oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF ACTIVATED HOLOENZYME, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=3681999; DOI=10.1016/0022-2836(87)90129-x;
RA Suh S.W., Cascio D., Chapman M.S., Eisenberg D.;
RT "A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from
RT Nicotiana tabacum in the activated state.";
RL J. Mol. Biol. 197:363-365(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF UNACTIVATED HOLOENZYME, SUBUNIT,
RP AND DISULFIDE BOND.
RC STRAIN=cv. Turkish samsun;
RX PubMed=1512238; DOI=10.1016/s0021-9258(18)41881-9;
RA Curmi P.M.G., Cascio D., Sweet R.M., Eisenberg D., Schreuder H.;
RT "Crystal structure of the unactivated form of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase from tobacco refined at 2.0-A resolution.";
RL J. Biol. Chem. 267:16980-16989(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-477 OF UNACTIVATED HOLOENZYME,
RP SUBUNIT, DISULFIDE BOND, AND CARBOXYLATION AT LYS-201.
RC STRAIN=cv. Wisconsin-38;
RX PubMed=10801357; DOI=10.1006/jmbi.2000.3724;
RA Duff A.P., Andrews T.J., Curmi P.M.G.;
RT "The transition between the open and closed states of rubisco is triggered
RT by the inter-phosphate distance of the bound bisphosphate.";
RL J. Mol. Biol. 298:903-916(2000).
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 (PubMed:3681999,
CC PubMed:2928307). Both reactions occur simultaneously and in competition
CC at the same active site. {ECO:0000269|PubMed:2928307,
CC ECO:0000269|PubMed:3681999, ECO:0000305}.
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 Evidence={ECO:0000269|PubMed:3681999};
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 Note=Binds 1 Mg(2+) ion per subunit.;
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:1512238, ECO:0000269|PubMed:3681999}.
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 bonds reported in 3RUB and 4RUB may be the result of
CC oxidation during crystallization (PubMed:1512238).
CC {ECO:0000250|UniProtKB:P11383, ECO:0000269|PubMed:1512238}.
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:1512238}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000305}.
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DR EMBL; J01450; AAD15025.1; -; Genomic_DNA.
DR EMBL; Z00044; CAA77361.1; -; Genomic_DNA.
DR PIR; A01095; RKNTL.
DR RefSeq; NP_054507.1; NC_001879.2.
DR PDB; 1EJ7; X-ray; 2.45 A; L=3-477.
DR PDB; 1RLC; X-ray; 2.70 A; L=1-477.
DR PDB; 1RLD; X-ray; 2.50 A; A/B=22-467.
DR PDB; 3RUB; X-ray; 2.00 A; L=1-477.
DR PDB; 4RUB; X-ray; 2.70 A; A/B/C/D=1-477.
DR PDBsum; 1EJ7; -.
DR PDBsum; 1RLC; -.
DR PDBsum; 1RLD; -.
DR PDBsum; 3RUB; -.
DR PDBsum; 4RUB; -.
DR AlphaFoldDB; P00876; -.
DR SMR; P00876; -.
DR DIP; DIP-42221N; -.
DR IntAct; P00876; 2.
DR MINT; P00876; -.
DR iPTMnet; P00876; -.
DR GeneID; 800513; -.
DR KEGG; nta:800513; -.
DR OMA; EYRETYW; -.
DR OrthoDB; 474428at2759; -.
DR SABIO-RK; P00876; -.
DR EvolutionaryTrace; P00876; -.
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:2928307"
FT /id="PRO_0000031427"
FT CHAIN 3..477
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031428"
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 BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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:2928307"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:2928307"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:10801357"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000269|PubMed:10801357,
FT ECO:0000269|PubMed:1512238, ECO:0000269|PubMed:3681999"
FT VARIANT 394
FT /note="F -> V"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 405
FT /note="G -> M"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 284
FT /note="C -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="V -> E (in Ref. 1; AAD15025)"
FT /evidence="ECO:0000305"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1EJ7"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:3RUB"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1EJ7"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1EJ7"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1RLD"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1RLD"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:3RUB"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:3RUB"
FT TURN 404..408
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 437..451
FT /evidence="ECO:0007829|PDB:3RUB"
FT HELIX 453..466
FT /evidence="ECO:0007829|PDB:3RUB"
SQ SEQUENCE 477 AA; 52898 MW; 232D54E42263198F CRC64;
MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVKA RNEGRDLAQE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK