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Database: UniProt/SWISS-PROT
Entry: RBL_TOBAC
LinkDB: RBL_TOBAC
Original site: 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   24-JAN-2024, entry version 159.
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; 1275719at2759; -.
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; 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: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
//
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