GenomeNet

Database: UniProt/SWISS-PROT
Entry: RBL1C_CUPNH
LinkDB: RBL1C_CUPNH
Original site: 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   05-DEC-2018, entry version 77.
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 / H16 / DSM 428 / Stanier 337)
OS   (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
RP   GROWTH 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
RT   carboxylase 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 / H16 / DSM 428 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
RA   Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
RA   Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
RA   Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium
RT   Ralstonia 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
RT   in 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
CC       at the same active site (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 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 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, 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
CC       subunit homodimers (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: Total RuBisCO activity (both chromosome and plasmid-
CC       derived enzyme) is high under lithoautotrophic growth conditions,
CC       intermediate when grown on fructose and poor when grown on
CC       pyruvate.
CC   -!- PTM: The disulfide bond which can form between Cys-278 in the
CC       large chain dimeric partners within the hexadecamer appears to be
CC       associated with oxidative stress and protein turnover.
CC       {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
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel" (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
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; NC_008314.1.
DR   ProteinModelPortal; Q0K1E0; -.
DR   SMR; Q0K1E0; -.
DR   STRING; 381666.H16_B1395; -.
DR   EnsemblBacteria; CAJ96184; CAJ96184; H16_B1395.
DR   KEGG; reh:H16_B1395; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; FTQDWAS; -.
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-KW.
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; Complete proteome;
KW   Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    486       Ribulose bisphosphate carboxylase large
FT                                chain, chromosomal.
FT                                /FTId=PRO_0000273254.
FT   ACT_SITE    178    178       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    296    296       Proton acceptor. {ECO:0000250}.
FT   METAL       204    204       Magnesium; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       206    206       Magnesium. {ECO:0000250}.
FT   METAL       207    207       Magnesium. {ECO:0000250}.
FT   BINDING     126    126       Substrate; in homodimeric partner.
FT                                {ECO:0000250}.
FT   BINDING     176    176       Substrate. {ECO:0000250}.
FT   BINDING     180    180       Substrate. {ECO:0000250}.
FT   BINDING     297    297       Substrate. {ECO:0000250}.
FT   BINDING     329    329       Substrate. {ECO:0000250}.
FT   BINDING     381    381       Substrate. {ECO:0000250}.
FT   SITE        336    336       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   MOD_RES     204    204       N6-carboxylysine. {ECO:0000250}.
FT   CONFLICT     83     88       YRAKAY -> SVQGL (in Ref. 1; AAA83745).
FT                                {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
//
DBGET integrated database retrieval system