ID A0A6B9TN46_9ROSI Unreviewed; 484 AA. AC A0A6B9TN46; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 22-FEB-2023, entry version 10. 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:QHN51054.1}; OS Hibiscus taiwanensis. OG Plastid; Chloroplast {ECO:0000313|EMBL:QHN51054.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus. OX NCBI_TaxID=1898877 {ECO:0000313|EMBL:QHN51054.1}; RN [1] {ECO:0000313|EMBL:QHN51054.1} RP NUCLEOTIDE SEQUENCE. RA Xu X.-R., Zhou S.-D., Shi X.-Q.; RT "The complete chloroplast genome of Hibiscus Taiwanensis (Malvaceae)."; RL Mitochondrial DNA Part B Resour 4:2533-2534(2019). RN [2] {ECO:0000313|EMBL:QHN51054.1} RP NUCLEOTIDE SEQUENCE. RA Xu X.; RL Submitted (MAY-2019) 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|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|ARBA:ARBA00004229, ECO:0000256|HAMAP-Rule:MF_01338, 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 -!- 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; MK937807; QHN51054.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6B9TN46; -. 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 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:QHN51054.1}; 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}; 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:QHN51054.1}. FT DOMAIN 31..151 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 161..469 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 301 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 130 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 184 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 208 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 211 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 302 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 334 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 386 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 341 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 208 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT DISULFID 254 FT /note="Interchain; in linked form" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 484 AA; 53592 MW; 2AD214755E0F4F62 CRC64; MSCREGLMSP QTETKTGVGF QAGVKEYKLT YYTPQYEVKD TDILAAFRVT PQPGVPPEEA GAAVAAESST GTWTTVWTDG LTSLDRYKGR CYHIDPVPGE DDQYICYVAY PLDLFEEGSV TNMFTSIVGN VFGFKALRAL RLEDLRIPTA YIKTFQGPPH GIQVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD ENVNSQPFMR WRDRFLFCAE AIYKAQAETG EIKGHYLNAT AGTCEEMMKR AACARELGVP IVMHDYLTGG FTANTTLAHY CRDNGLLLHI HRAMHAVIDR QKNHGMHFRV LAKALRMSGG DHIHAGTVVG KLEGEREITL GFVDLLRDDF IEKDSSRGIY FTQDWVSLPG VLPVASGGIH VWHMPALTEI FGDDSVLQFG GGTLGHPWGN APGAVANRVA LEACVKARNE GRDLAAQGNE IIREASKWSP ELAAACEVWK EIKFEFKPVD TLDK //