ID A0A4D6PZY6_9ERIC Unreviewed; 475 AA. AC A0A4D6PZY6; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 29-SEP-2021, entry version 9. 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:0000313|EMBL:QCF39502.1}; GN Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338}; OS Vaccinium oldhamii. OG Plastid {ECO:0000313|EMBL:QCF39502.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Ericaceae; Vaccinioideae; Vaccinieae; Vaccinium. OX NCBI_TaxID=190543 {ECO:0000313|EMBL:QCF39502.1}; RN [1] {ECO:0000313|EMBL:QCF39502.1} RP NUCLEOTIDE SEQUENCE. RA Kim S.-C., Baek S.-H., Lee J.-W., Hyun H.J.; RT "Complete chloroplast genome of Vaccinium oldhamii and phylogenetic RT analysis."; RL Mitochondrial DNA Part B Resour 4:902-903(2019). 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. Both reactions occur simultaneously and in competition at CC the same active site. {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|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 disulfide-linked. The disulfide link is formed within the large subunit CC homodimers. {ECO:0000256|HAMAP-Rule:MF_01338}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {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. Type I CC subfamily. {ECO:0000256|ARBA:ARBA00006204, ECO:0000256|HAMAP- CC 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; MK049537; QCF39502.1; -; Genomic_DNA. 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; -; 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}; Chloroplast {ECO:0000256|RuleBase:RU000302}; KW Disulfide bond {ECO:0000256|HAMAP-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}; Methylation {ECO:0000256|HAMAP-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, KW ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QCF39502.1}. 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 14 FT /note="N6,N6,N6-trimethyllysine" 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 475 AA; 52529 MW; 5E9FC9010639239C CRC64; MSPQTETKAS VGFKAGVKDY KLTYYTPNYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDENQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIFKAQA ETGEIKGHYL NATAGTCEEM NKRAAFAREL GVPIVMHDYL TGGFTANTSL AEYCRDNGLL LHIHRAMHAV IDRQKNHGIH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDYIEKDRAR GIYFSQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGGVAN RVALEACVQA RNEGRDLARE GNEIIREAAQ WSNELSAACA VWKEIKFEFP AMDTL //