ID A0A9Y1I2I9_9RHOD Unreviewed; 488 AA. AC A0A9Y1I2I9; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 24-JAN-2024, entry version 2. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; GN Name=rbcL {ECO:0000313|EMBL:WDA99091.1}; GN Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338}; GN ORFNames=GRSY_086 {ECO:0000313|EMBL:WDA99091.1}; OS Gronococcus sybilensis. OG Plastid {ECO:0000313|EMBL:WDA99091.1}. OC Eukaryota; Rhodophyta; Bangiophyceae; Cavernulicolales; Cavernulicolaceae; OC Gronococcus. OX NCBI_TaxID=3028029 {ECO:0000313|EMBL:WDA99091.1}; RN [1] {ECO:0000313|EMBL:WDA99091.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=36792488; RA Park S.I., Cho C.H., Ciniglia C., Huang T.Y., Liu S.L., Bustamante D.E., RA Calderon M.S., Mansilla A., McDermott T., Andersen R.A., Yoon H.S.; RT "Revised classification of the Cyanidiophyceae based on plastid genome data RT with descriptions of the Cavernulicolales ord. nov. and Galdieriales ord. RT nov. (Rhodophyta)."; RL J. Phycol. 0:0-0(2023). 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 {ECO:0000256|ARBA:ARBA00011371, ECO:0000256|HAMAP-Rule:MF_01338, CC ECO:0000256|RuleBase:RU000302}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000256|RuleBase:RU000302}. 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|HAMAP-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; OP616812; WDA99091.1; -; Genomic_DNA. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. 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}; Chloroplast {ECO:0000256|RuleBase:RU000302}; 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}; Photorespiration {ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:WDA99091.1}. FT DOMAIN 28..148 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 158..465 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 179 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 297 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 127 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 205 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 207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 208 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 330 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 382 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 337 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 205 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" SQ SEQUENCE 488 AA; 53966 MW; BDE193935CDE8931 CRC64; MSQSVEERTR MKSDRYESGV IPYAKMGYWD GDYAVKETDV LALFRITPQP GVDPVEAAAA VAGESSTATW TVVWTDLLTA CEVYRAKAYR VDPVPSSNDQ YFAYIAYDMD LFEEGSIANL TASIIGNVFG FKALKALRLE DMRIPVAYLK TFQGPPTGVV VERERLNCFG RPLLGATVKP KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWRE RYLNVMEGVT RASASTGEVK GSYLNVTAAT MEDMYERAAY AKEVGSVIIM IDLVVGYTAI QSMAVWARKN DMILHLHRAG NSTYARQKNH GMNFRVICKW MRMSGVDHIH AGTVVGKLEG EPLMIKGFYN TLLLPYLEVD LPQGLFFEMD WASLRKTMPV ASGGIHAGQM HLLLDYLGED VILQFGGGTI GHPDGIQAGA TANRVALEAM VLARNEGRDY VDEGPQILRE AAKTCGPLKT ALDLWKDISF NYTSTDTADF VETPTANV //