ID   RBL1P_CUPNH             Reviewed;         486 AA.
AC   P42721; Q7WWS4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 3.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain, plasmid;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
GN   Name=cbbL2; Synonyms=cbbL, cbxLP, cfxLP; OrderedLocusNames=PHG427;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION UNDER DIFFERENT GROWTH
RP   CONDITIONS.
RX   PubMed=7543477; DOI=10.1128/jb.177.15.4442-4450.1995;
RA   Kusian B., Bednarski R., Husemann M., Bowien B.;
RT   "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase
RT   genes and cbb promoters of Alcaligenes eutrophus.";
RL   J. Bacteriol. 177:4442-4450(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX   PubMed=1779759; DOI=10.1111/j.1365-2958.1991.tb01978.x;
RA   Windhoevel U., Bowien B.;
RT   "Identification of cfxR, an activator gene of autotrophic CO2 fixation in
RT   Alcaligenes eutrophus.";
RL   Mol. Microbiol. 5:2695-2705(1991).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Total RuBisCO activity (both chromosome and plasmid-derived
CC       enzyme) is high under lithoautotrophic growth conditions, intermediate
CC       when grown on fructose and poor when grown on pyruvate.
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' (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U20585; AAA83747.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP86176.1; -; Genomic_DNA.
DR   EMBL; M65064; AAA21980.1; -; Genomic_DNA.
DR   PIR; I39559; I39559.
DR   RefSeq; WP_011154339.1; NZ_CP039289.1.
DR   AlphaFoldDB; P42721; -.
DR   SMR; P42721; -.
DR   GeneID; 39976596; -.
DR   KEGG; reh:PHG427; -.
DR   PATRIC; fig|381666.6.peg.355; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_2_0_4; -.
DR   OrthoDB; 9770811at2; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..486
FT                   /note="Ribulose bisphosphate carboxylase large chain,
FT                   plasmid"
FT                   /id="PRO_0000062642"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            336
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         204
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        198
FT                   /note="G -> R (in Ref. 1; AAA83747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  53809 MW;  38443E663E0EEE13 CRC64;
     MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL ALFRITPQDG VDPVEAAAAV
     AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT
     ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK
     LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG
     SYLNVTAGTM EEMYRRAEFA KSLGSVVIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
     GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTHTDL
     TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT
     ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCGPLRAA LDTWGDISFN YTPTDTSDFA
     PTASVA
//