ID RBL1C_CUPNE Reviewed; 486 AA. AC P0C2C2; P09657; P77811; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 03-MAY-2023, entry version 73. DE RecName: Full=Ribulose bisphosphate carboxylase large chain, chromosomal; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; GN Name=cbbL1; Synonyms=cbbL, cbxLC, cfxLC; OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=106590; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBOXYLATION AT LYS-204. RC STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R; RX PubMed=2820933; DOI=10.1128/jb.169.10.4547-4558.1987; RA Andersen K., Caton J.; RT "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded RT ribulose bisphosphate carboxylase large and small subunit genes and their RT gene products."; RL J. Bacteriol. 169:4547-4558(1987). RN [2] RP SEQUENCE REVISION. RA Andersen K.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-467 OF UNACTIVATED HOLOENYZYME, RP AND SUBUNIT. RC STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R; RX PubMed=10329167; DOI=10.1006/jmbi.1999.2701; RA Hansen S., Vollan V.B., Hough E., Andersen K.; RT "The crystal structure of rubisco from Alcaligenes eutrophus reveals a RT novel central eight-stranded beta-barrel formed by beta-strands from four RT subunits."; RL J. Mol. Biol. 288:609-621(1999). 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(+) = 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. A CC disulfide link might be formed within the large subunit homodimers. CC {ECO:0000269|PubMed:10329167}. CC -!- PTM: A disulfide bond might be able to form between Cys-278 in the CC large chain dimeric partners within the hexadecamer. CC {ECO:0000305|PubMed:10329167}. 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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000305}. 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; M17744; AAC28129.1; -; Genomic_DNA. DR PIR; A26954; RKALLE. DR PDB; 1BXN; X-ray; 2.70 A; A/C/E/G=1-486. DR PDBsum; 1BXN; -. DR AlphaFoldDB; P0C2C2; -. DR SMR; P0C2C2; -. DR EvolutionaryTrace; P0C2C2; -. 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: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 1: Evidence at protein level; KW 3D-structure; Calvin cycle; Carbon dioxide fixation; Disulfide bond; Lyase; KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase. FT CHAIN 1..486 FT /note="Ribulose bisphosphate carboxylase large chain, FT chromosomal" FT /id="PRO_0000062641" FT ACT_SITE 178 FT /note="Proton acceptor" FT ACT_SITE 296 FT /note="Proton acceptor" FT BINDING 126 FT /ligand="substrate" FT /note="in homodimeric partner" FT BINDING 176 FT /ligand="substrate" FT BINDING 180 FT /ligand="substrate" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT BINDING 206 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 297 FT /ligand="substrate" FT BINDING 329 FT /ligand="substrate" FT BINDING 381 FT /ligand="substrate" FT SITE 336 FT /note="Transition state stabilizer" FT MOD_RES 204 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:2820933" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 38..47 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:1BXN" FT TURN 63..66 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 100..107 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 116..124 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 158..165 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 185..197 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 217..235 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 250..262 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 266..271 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 276..287 FT /evidence="ECO:0007829|PDB:1BXN" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1BXN" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 335..338 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 341..352 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 377..383 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 386..388 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 389..396 FT /evidence="ECO:0007829|PDB:1BXN" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 406..409 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 414..435 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 439..453 FT /evidence="ECO:0007829|PDB:1BXN" FT HELIX 455..463 FT /evidence="ECO:0007829|PDB:1BXN" SQ SEQUENCE 486 AA; 53840 MW; 66EAB4A11982FAB5 CRC64; MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTQTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCAPLRAA LDTWGDITFN YTPTDTSDFV PTASVA //