ID RBL_ACAM1 Reviewed; 476 AA. AC B0CCC1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 84. 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}; GN OrderedLocusNames=AM1_1785; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales; OC Acaryochloridaceae; Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., RA Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). 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:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01338}; 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: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 disulfide-linked. The disulfide link is formed within the large subunit CC homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}. CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338}. 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: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; CP000828; ABW26806.1; -; Genomic_DNA. DR RefSeq; WP_010467950.1; NC_009925.1. DR AlphaFoldDB; B0CCC1; -. DR SMR; B0CCC1; -. DR STRING; 329726.AM1_1785; -. DR KEGG; amr:AM1_1785; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_2_0_3; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0031470; C:carboxysome; 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 Bacterial microcompartment; Calvin cycle; Carbon dioxide fixation; KW Carboxysome; Disulfide bond; Lyase; Magnesium; Metal-binding; KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; KW Reference proteome. FT CHAIN 1..476 FT /note="Ribulose bisphosphate carboxylase large chain" FT /id="PRO_1000142747" FT ACT_SITE 176 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT ACT_SITE 295 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 124 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 202 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 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 205 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 328 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT BINDING 380 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT SITE 335 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT MOD_RES 202 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" FT DISULFID 248 FT /note="Interchain; in linked form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338" SQ SEQUENCE 476 AA; 52981 MW; 4991C37529C5BBC1 CRC64; MSYSQTRTQS KAGYDAGVKD YKLTYYTPDY TPKDTDILAA FRMTPQPGVP PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEA VANEDNQYIA YIAYPLDLFE EGSVVNLLTS LVGNVFGFKA LRALRLEDIR IPVAYMKTFQ GPPHGITVER DKINKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENINSQ PFMRWRDRFL FVAEAIHKAQ AETGEIKGHY LNVTAATCEE MLKRAEFAKE LEMPIIMHDF ITGGFTANTT LSHWCRDNGV LLHIHRAMHA VIDRQKNHGM HFRVLSKCLR MSGGDHIHTG TVVGKLEGEK GITMGFVDLL RENYVEKDLS RGIYFTQDWA SMGGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGCAPGATA NRVALEACVQ ARNEGRDMAR EGGDILREAA KWSPELAVAL EVWKEIKFEF EAMDTV //