ID RBL_PHYPA Reviewed; 475 AA. AC P34915; Q95FY7; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2003, sequence version 2. DT 24-JAN-2024, entry version 128. 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 Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium. OX NCBI_TaxID=3218; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kruse S., Martin W., Wehe M., Reski R.; RT "An open reading frame (ycf11) is evolutionary conserved from Cyanobacteria RT to the plastid DNAs of Archegoniates and Gymnosperms is modified in the RT plastid DNAs of Dicots and is not plastome encoded in Monocots."; RL J. Plant Physiol. 146:258-262(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Protonema; RA Sugita M., Sugiura C.; RT "Physcomitrella patens chloroplast genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004; RX PubMed=12954768; DOI=10.1093/nar/gkg726; RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.; RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens: RT evidence for the loss and relocation of rpoA from the chloroplast to the RT nucleus."; RL Nucleic Acids Res. 31:5324-5331(2003). RN [4] RP PROTEIN SEQUENCE OF 184-195. RC TISSUE=Protonema; RX PubMed=9129336; DOI=10.1007/s004250050065; RA Kasten B., Buck F., Nuske J., Reski R.; RT "Cytokinin affects nuclear- and plastome-encoded energy-converting plastid RT enzymes."; RL Planta 201:261-272(1997). 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: 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01338}; 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; Evidence={ECO:0000255|HAMAP-Rule:MF_01338}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01338}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-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 subunit CC 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 oxidative CC stress and protein turnover. {ECO:0000255|HAMAP-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 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: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; X74156; CAA52269.1; -; Genomic_DNA. DR EMBL; AB066207; BAB62086.1; -; Genomic_DNA. DR EMBL; AP005672; BAC85044.1; -; Genomic_DNA. DR PIR; S34663; S34663. DR RefSeq; NP_904194.1; NC_005087.1. DR AlphaFoldDB; P34915; -. DR SMR; P34915; -. DR STRING; 3218.P34915; -. DR GeneID; 2546763; -. DR KEGG; ppp:2546763; -. DR InParanoid; P34915; -. DR OrthoDB; 1275719at2759; -. DR Proteomes; UP000006727; 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:0000255|HAMAP-Rule:MF_01338" FT /id="PRO_0000031347" FT CHAIN 3..475 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000031348" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT ACT_SITE 294 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 123 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 201 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 295 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 379 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT SITE 334 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 3 FT /note="N-acetylproline" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 14 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 201 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT DISULFID 247 FT /note="Interchain; in linked form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT CONFLICT 9 FT /note="A -> T (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="Q -> H (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 50 FT /note="A -> L (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="Y -> N (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 251 FT /note="I -> L (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 255..256 FT /note="QF -> PC (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="L -> V (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="R -> L (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 372..374 FT /note="PGV -> QVF (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="W -> G (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="A -> T (in Ref. 1; CAA52269)" FT /evidence="ECO:0000305" SQ SEQUENCE 475 AA; 52705 MW; 30A91B8A714507AF CRC64; MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EECGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY VAYPLDLFEE GSVTNLFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQG ETGEIKGHYL NATAGTCEEM IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFD TVDTL //