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Q0K1E0

- RBL1C_CUPNH

UniProt

Q0K1E0 - RBL1C_CUPNH

Protein

Ribulose bisphosphate carboxylase large chain, chromosomal

Gene

cbbL1

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.By similarity

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261Substrate; in homodimeric partnerBy similarity
    Binding sitei176 – 1761SubstrateBy similarity
    Active sitei178 – 1781Proton acceptorBy similarity
    Binding sitei180 – 1801SubstrateBy similarity
    Metal bindingi204 – 2041Magnesium; via carbamate groupBy similarity
    Metal bindingi206 – 2061MagnesiumBy similarity
    Metal bindingi207 – 2071MagnesiumBy similarity
    Active sitei296 – 2961Proton acceptorBy similarity
    Binding sitei297 – 2971SubstrateBy similarity
    Binding sitei329 – 3291SubstrateBy similarity
    Sitei336 – 3361Transition state stabilizerBy similarity
    Binding sitei381 – 3811SubstrateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. monooxygenase activity Source: UniProtKB-KW
    3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciCNEC381666:GJUJ-5100-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain, chromosomal (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:cbbL1
    Synonyms:cbbL, cbxLC, cfxLC
    Ordered Locus Names:H16_B1395
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, chromosomalPRO_0000273254Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041N6-carboxylysineBy similarity

    Post-translational modificationi

    The disulfide bond which can form between Cys-278 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Total RuBisCO activity (both chromosome and plasmid-derived enzyme) is high under lithoautotrophic growth conditions, intermediate when grown on fructose and poor when grown on pyruvate.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.By similarity

    Protein-protein interaction databases

    STRINGi381666.H16_B1395.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0K1E0.
    SMRiQ0K1E0. Positions 24-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiCTPLKQA.
    OrthoDBiEOG6ZKXMS.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view]
    PfamiPF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q0K1E0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL ALFRITPQDG    50
    VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF 100
    FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT 150
    FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL 200
    DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM 250
    EEMYRRAEFA KSLGSVIIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 300
    GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV 350
    CRDAYTHADL SRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLISLFGDDV 400
    VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA 450
    ARWCGPLRAA LDTWGDISFN YTPTDTSDFA PTASVA 486
    Length:486
    Mass (Da):53,729
    Last modified:October 3, 2006 - v1
    Checksum:i47C20867581EDDB4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 886YRAKAY → SVQGL in AAA83745. (PubMed:7543477)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20584 Genomic DNA. Translation: AAA83745.1.
    AM260480 Genomic DNA. Translation: CAJ96184.1.
    M65065 Genomic DNA. Translation: AAA21981.1.
    PIRiI39557.
    RefSeqiYP_840914.1. NC_008314.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ96184; CAJ96184; H16_B1395.
    GeneIDi4456354.
    KEGGireh:H16_B1395.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20584 Genomic DNA. Translation: AAA83745.1 .
    AM260480 Genomic DNA. Translation: CAJ96184.1 .
    M65065 Genomic DNA. Translation: AAA21981.1 .
    PIRi I39557.
    RefSeqi YP_840914.1. NC_008314.1.

    3D structure databases

    ProteinModelPortali Q0K1E0.
    SMRi Q0K1E0. Positions 24-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.H16_B1395.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ96184 ; CAJ96184 ; H16_B1395 .
    GeneIDi 4456354.
    KEGGi reh:H16_B1395.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi CTPLKQA.
    OrthoDBi EOG6ZKXMS.

    Enzyme and pathway databases

    BioCyci CNEC381666:GJUJ-5100-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi IPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view ]
    Pfami PF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus."
      Kusian B., Bednarski R., Husemann M., Bowien B.
      J. Bacteriol. 177:4442-4450(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION UNDER DIFFERENT GROWTH CONDITIONS.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
    3. "Identification of cfxR, an activator gene of autotrophic CO2 fixation in Alcaligenes eutrophus."
      Windhoevel U., Bowien B.
      Mol. Microbiol. 5:2695-2705(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

    Entry informationi

    Entry nameiRBL1C_CUPNH
    AccessioniPrimary (citable) accession number: Q0K1E0
    Secondary accession number(s): P09657, P77811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3