ID RBL_SOYBN Reviewed; 475 AA. AC P27066; Q2PMV1; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 3. DT 24-JAN-2024, entry version 126. 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 Glycine max (Soybean) (Glycine hispida). 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; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Leaf; RX PubMed=9242596; DOI=10.1006/mpev.1997.0410; RA Kaess E., Wink M.; RT "Phylogenetic relationships in the Papilionoideae (family Leguminosae) RT based on nucleotide sequences of cpDNA (rbcL) and ncDNA (ITS 1 and 2)."; RL Mol. Phylogenet. Evol. 8:65-88(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. PI 437654; RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0; RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G., RA Jansen R.K.; RT "Complete chloroplast genome sequence of Glycine max and comparative RT analyses with other legume genomes."; RL Plant Mol. Biol. 59:309-322(2005). RN [3] 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). 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 -!- 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; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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}. 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' (By CC similarity). {ECO:0000250}. 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; Z95552; CAB08877.1; -; Genomic_DNA. DR EMBL; DQ317523; ABC25107.1; -; Genomic_DNA. DR RefSeq; YP_538747.1; NC_007942.1. DR AlphaFoldDB; P27066; -. DR SMR; P27066; -. DR STRING; 3847.P27066; -. DR iPTMnet; P27066; -. DR GeneID; 3989271; -. DR KEGG; gmx:3989271; -. DR InParanoid; P27066; -. DR OrthoDB; 1275719at2759; -. DR Proteomes; UP000008827; 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 Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; KW Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding; KW Methylation; Monooxygenase; Oxidoreductase; Photorespiration; KW Photosynthesis; Plastid; Reference proteome. FT PROPEP 1..2 FT /evidence="ECO:0000269|PubMed:16668742" FT /id="PRO_0000031411" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000031412" 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 123 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000250" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000250" 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="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="substrate" FT /evidence="ECO:0000250" 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" FT CONFLICT 143 FT /note="A -> S (in Ref. 1; CAB08877)" FT /evidence="ECO:0000305" FT CONFLICT 470 FT /note="E -> P (in Ref. 1; CAB08877)" FT /evidence="ECO:0000305" FT CONFLICT 474..475 FT /note="Missing (in Ref. 1; CAB08877)" FT /evidence="ECO:0000305" SQ SEQUENCE 475 AA; 52610 MW; 481460745D587783 CRC64; MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGLEPV AGEENQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYIKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRL SGGDHVHAGT VVGKLEGERE ITLGFVDLLR DDFVEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE VWKEIKFEFE AMDTL //