RBL1P_CUPNH
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 03-AUG-2022, entry version 144.
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; Proteobacteria; 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 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 STRING; 381666.PHG427; -.
DR EnsemblBacteria; AAP86176; AAP86176; PHG427.
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 OMA; GGGTQGH; -.
DR OrthoDB; 848380at2; -.
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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 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
