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 02-SEP-2026, entry version 167. 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:2928307, CC PubMed:3681999). 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(+) = D-ribulose 1,5- CC bisphosphate + CO2 + 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 = 2-phosphoglycolate + (2R)- CC 3-phosphoglycerate + 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}. 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; 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 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; HADPDEM; -. DR OrthoDB; 1578724at2759; -. DR BRENDA; 4.1.1.39; 3645. DR SABIO-RK; P00876; -. DR EvolutionaryTrace; P00876; -. DR Proteomes; UP000790787; Unplaced. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; EXP:UniProtKB. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. DR CDD; cd08212; RuBisCO_large_I; 1. DR FunFam; 3.20.20.110:FF:000001; Ribulose bisphosphate carboxylase large chain; 1. DR FunFam; 3.30.70.150:FF:000001; Ribulose bisphosphate carboxylase large chain; 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 NCBIfam; NF003252; PRK04208.1; 1. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF16; 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. DR PDBsum; 1EJ7; -. DR PDBsum; 1RLC; -. DR PDBsum; 1RLD; -. DR PDBsum; 3RUB; -. DR PDBsum; 4RUB; -. 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; Reference proteome. 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 HELIX 29..32 FT /evidence="ECO:0007829|PDB:1RLD" 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 HELIX 371..373 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 //