ID RBL_SOLBU Reviewed; 477 AA. AC Q2MIH9; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 11-NOV-2015, entry version 48. 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 Solanum bulbocastanum (Wild potato). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=147425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. PT29; RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., RA Guda C., Tomkins J., Jansen R.K.; RT "Complete chloroplast genome sequences of Solanum tuberosum, Solanum RT lycopersicum and comparative analyses with other Solanaceae genomes."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose CC 1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP- CC Rule:MF_01338}. CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = CC D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP- CC Rule:MF_01338}. 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- CC Rule:MF_01338}; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; CC disulfide-linked. The disulfide link is formed within the large CC subunit homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}. 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 CC oxidative stress and protein turnover. {ECO:0000255|HAMAP- CC Rule:MF_01338}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a "head-to-tail" conformation. In form I CC RuBisCO this homodimer is arranged in a barrel-like tetramer with CC the small subunits forming a tetrameric "cap" on each end of the CC "barrel". {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}. 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; DQ347958; ABC56221.1; -; Genomic_DNA. DR RefSeq; YP_538856.1; NC_007943.1. DR ProteinModelPortal; Q2MIH9; -. DR SMR; Q2MIH9; 9-472. DR PRIDE; Q2MIH9; -. DR GeneID; 3989432; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 1. DR HAMAP; MF_01338; RuBisCO_L_type1; 1. DR InterPro; IPR020878; RuBisCo_large_chain_AS. DR InterPro; IPR020888; RuBisCO_lsu. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SUPFAM; SSF51649; SSF51649; 1. DR SUPFAM; SSF54966; SSF54966; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; KW Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation; KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; KW Plastid. FT PROPEP 1 2 {ECO:0000255|HAMAP-Rule:MF_01338}. FT /FTId=PRO_0000251438. FT CHAIN 3 477 Ribulose bisphosphate carboxylase large FT chain. FT /FTId=PRO_0000251439. FT ACT_SITE 175 175 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT ACT_SITE 294 294 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT METAL 201 201 Magnesium; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_01338}. FT METAL 203 203 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT METAL 204 204 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT BINDING 123 123 Substrate; in homodimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01338}. FT BINDING 173 173 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT BINDING 177 177 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT BINDING 295 295 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT BINDING 327 327 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT BINDING 379 379 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT SITE 334 334 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01338}. FT MOD_RES 3 3 N-acetylproline. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT MOD_RES 14 14 N6,N6,N6-trimethyllysine. FT {ECO:0000255|HAMAP-Rule:MF_01338}. FT MOD_RES 201 201 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_01338}. FT DISULFID 247 247 Interchain; in linked form. FT {ECO:0000255|HAMAP-Rule:MF_01338}. SQ SEQUENCE 477 AA; 52974 MW; 296FEE923BAA6DF6 CRC64; MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQT ETGEIKGHYL NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEQDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVKA RNEGRDLARE GNEIIREASK WSPELAAACE VWKEIVFNFA AVDVLDK //