ID RBL_ALVHS Reviewed; 471 AA. AC P24672; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 02-SEP-2026, entry version 102. 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}; GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338}; GN Synonyms=rbcL {ECO:0000255|HAMAP-Rule:MF_01338}; OS Alvinoconcha hessleri symbiotic bacterium. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=2326; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2247456; DOI=10.1073/pnas.87.22.8850; RA Stein J.L., Haygood M., Felbeck H.; RT "Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate RT carboxylase gene cloned from a chemoautotrophic bacterial endosymbiont."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8850-8854(1990). 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5- CC bisphosphate + CO2 + 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 = 2-phosphoglycolate + (2R)- CC 3-phosphoglycerate + 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 {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; M34536; AAA27387.1; -; Genomic_DNA. DR PIR; A38262; A38262. DR AlphaFoldDB; P24672; -. DR SMR; P24672; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. 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 NCBIfam; NF003252; PRK04208.1; 1. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF17; 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; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; KW Monooxygenase; Oxidoreductase. FT CHAIN 1..471 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_0000062618" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT ACT_SITE 286 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 115 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 169 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 193 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 195 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 371 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT SITE 326 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 193 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" SQ SEQUENCE 471 AA; 52770 MW; 990F5E9B5E55C504 CRC64; MAKKYDAGVK DYRETYWMPD YTPKETDLLA CFKIIPQPGV PREEARAAVA AESSTGTWTT VWTDLLTDLD HYKGRAYAIE DVPGDEEAFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK AIRALRLEDV RFPIAYVMTC NGPPHGIQVE RDIMNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS QPFMRWRHGF DFVMEAIEKA ERETGERKGH YLNVTAPTPD EMFKRAEYAK EIGAPIIMHD YITGGFTANT GLAQWCRDNG VLLHIHRAMH AVLDRNPHHG IHFRVLTKIL RLSGGDHLHT GTVVGKLEGD REATLGWIDL LRESYIKEDR SRGIFFDQDW GSMPGVFAAC SGGIHVWHMP ALVTIFGEHA VLQFGGGTLG HPWGNAGAAA NRVALEACVE ARNEGHELEK EGKDILIQAA KHSPELKTAM ETWKEIKFEF DTVDKLDVAH K //