RBL1C_CUPNH
ID RBL1C_CUPNH Reviewed; 486 AA.
AC Q0K1E0; P09657; P77811;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; OrderedLocusNames=H16_B1395;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
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=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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 (By similarity). {ECO:0000250}.
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 disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers (By similarity). {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 -!- PTM: The disulfide bond which can form between Cys-278 in the large
CC chain dimeric partners within the hexadecamer appears to be associated
CC with oxidative stress and protein turnover. {ECO:0000250}.
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; U20584; AAA83745.1; -; Genomic_DNA.
DR EMBL; AM260480; CAJ96184.1; -; Genomic_DNA.
DR EMBL; M65065; AAA21981.1; -; Genomic_DNA.
DR PIR; I39557; I39557.
DR RefSeq; WP_010809289.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0K1E0; -.
DR SMR; Q0K1E0; -.
DR STRING; 381666.H16_B1395; -.
DR EnsemblBacteria; CAJ96184; CAJ96184; H16_B1395.
DR GeneID; 57647293; -.
DR KEGG; reh:H16_B1395; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_4; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000008210; Chromosome 2.
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; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..486
FT /note="Ribulose bisphosphate carboxylase large chain,
FT chromosomal"
FT /id="PRO_0000273254"
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 83..88
FT /note="YRAKAY -> SVQGL (in Ref. 1; AAA83745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53729 MW; 47C20867581EDDB4 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 KSLGSVIIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTHADL
SRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLISLFGDDV VLQFGGGTIG HPQGIQAGAT
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCGPLRAA LDTWGDISFN YTPTDTSDFA
PTASVA
