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B9KQ06

- RBL_RHOSK

UniProt

B9KQ06 - RBL_RHOSK

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei125 – 1251Substrate; in homodimeric partnerUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Active sitei177 – 1771Proton acceptorUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule annotation
    Metal bindingi203 – 2031Magnesium; via carbamate groupUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Metal bindingi206 – 2061MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule annotation

    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, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciRSPH557760:GH1P-2714-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunitUniRule annotation
    Gene namesi
    Name:cbbLUniRule annotation
    Ordered Locus Names:RSKD131_2681
    OrganismiRhodobacter sphaeroides (strain KD131 / KCTC 12085)
    Taxonomic identifieri557760 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    ProteomesiUP000001597: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_1000166262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Protein-protein interaction databases

    STRINGi557760.RSKD131_2681.

    Structurei

    3D structure databases

    ProteinModelPortaliB9KQ06.
    SMRiB9KQ06. Positions 6-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    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.

    B9KQ06-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV    50
    DPVEAAAAVA GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF 100
    CYVAYDLILF EEGSIANLTA SIIGNVFSFK PLKAARLEDM RFPVAYVKTY 150
    KGPPTGIVGE RERLDKFGKP LLGATTKPKL GLSGKNYGRV VYEGLKGGLD 200
    FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH YLNITAGTME 250
    EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG 300
    TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC 350
    REPFNTVDLP RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV 400
    LQFGGGTIGH PMGIQAGATA NRVALEAMVL ARNEGRNIDV EGPEILRAAA 450
    KWCKPLEAAL DTWGNITFNY TSTDTSDFVP TASVAM 486
    Length:486
    Mass (Da):53,686
    Last modified:March 24, 2009 - v1
    Checksum:i82B91D700303C3C0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001150 Genomic DNA. Translation: ACM02541.1.
    RefSeqiYP_002527042.1. NC_011963.1.

    Genome annotation databases

    EnsemblBacteriaiACM02541; ACM02541; RSKD131_2681.
    GeneIDi7358468.
    KEGGirsk:RSKD131_2681.
    PATRICi23184494. VBIRhoSph125910_4087.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001150 Genomic DNA. Translation: ACM02541.1 .
    RefSeqi YP_002527042.1. NC_011963.1.

    3D structure databases

    ProteinModelPortali B9KQ06.
    SMRi B9KQ06. Positions 6-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 557760.RSKD131_2681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM02541 ; ACM02541 ; RSKD131_2681 .
    GeneIDi 7358468.
    KEGGi rsk:RSKD131_2681.
    PATRICi 23184494. VBIRhoSph125910_4087.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci RSPH557760:GH1P-2714-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. "Complete genome sequence of Rhodobacter sphaeroides KD131."
      Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
      J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KD131 / KCTC 12085.

    Entry informationi

    Entry nameiRBL_RHOSK
    AccessioniPrimary (citable) accession number: B9KQ06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 33 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".UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3