ID A0A510B505_9POAL Unreviewed; 477 AA. AC A0A510B505; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 02-JUN-2021, entry version 6. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|HAMAP-Rule:MF_01338}; DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|HAMAP-Rule:MF_01338}; GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338, GN ECO:0000313|EMBL:AXF82424.1}; GN ORFNames=AMA_cp048 {ECO:0000313|EMBL:AXF82424.1}; OS Avena maroccana. OG Plastid; Chloroplast {ECO:0000313|EMBL:AXF82424.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Poodae; Poeae; Aveninae; Avena. OX NCBI_TaxID=84388 {ECO:0000313|EMBL:AXF82424.1}; RN [1] {ECO:0000313|EMBL:AXF82424.1} RP NUCLEOTIDE SEQUENCE. RA Li P., Biligetu B., Fu Y.-B.; RT "Chloroplast Genome de novo Assembly of 25 Diverse Oat Accessions."; RL Submitted (DEC-2017) 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001067, ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; 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:0000256|ARBA:ARBA00000537, CC ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338, CC ECO:0000256|RuleBase:RU000302}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338, CC ECO:0000256|RuleBase:RU000302}; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. CC {ECO:0000256|RuleBase:RU000302}. 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:0000256|HAMAP-Rule:MF_01338}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. 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:0000256|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:0000256|HAMAP-Rule:MF_01338}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC {ECO:0000256|RuleBase:RU000302}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000256|ARBA:ARBA00006204, ECO:0000256|HAMAP- CC Rule:MF_01338}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; MG687298; AXF82424.1; -; Genomic_DNA. DR SMR; A0A510B505; -. 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-KW. DR CDD; cd08212; RuBisCO_large_I; 1. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SUPFAM; SSF51649; SSF51649; 1. DR SUPFAM; SSF54966; SSF54966; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AXF82424.1}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AXF82424.1}. FT DOMAIN 24..144 FT /note="RuBisCO_large_N" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 154..462 FT /note="RuBisCO_large" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 175 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 294 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 201 FT /note="Magnesium; via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 203 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 204 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 123 FT /note="Substrate; in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 173 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 177 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 295 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 327 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 379 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 334 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 201 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT DISULFID 247 FT /note="Interchain; in linked form" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 477 AA; 52935 MW; F1D58ED95AED05DD CRC64; MSPQTETKAS VGFQAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEDNQWICY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM IKRAVFAREL GVPIVMHDYI TGGFTANTSL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE MTLGFVDLLR DDFIEKDRAR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN RVALEACVQA RNEGRDLARE GNEIIREACK WSPELAAACE VWKAIKFEFE PVDTIDE //