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Q13QV1

- RBL_BURXL

UniProt

Q13QV1 - RBL_BURXL

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (22 Aug 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.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 sitei139 – 1391Substrate; in homodimeric partnerUniRule annotation
    Binding sitei189 – 1891SubstrateUniRule annotation
    Active sitei191 – 1911Proton acceptorUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Metal bindingi217 – 2171Magnesium; via carbamate groupUniRule annotation
    Metal bindingi219 – 2191MagnesiumUniRule annotation
    Metal bindingi220 – 2201MagnesiumUniRule annotation
    Active sitei309 – 3091Proton acceptorUniRule annotation
    Binding sitei310 – 3101SubstrateUniRule annotation
    Binding sitei342 – 3421SubstrateUniRule annotation
    Sitei349 – 3491Transition state stabilizerUniRule annotation
    Binding sitei394 – 3941SubstrateUniRule 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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBXEN266265:GJII-5191-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:Bxeno_B0570
    ORF Names:Bxe_B2453
    OrganismiBurkholderia xenovorans (strain LB400)
    Taxonomic identifieri266265 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
    ProteomesiUP000001817: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Ribulose bisphosphate carboxylase large chainPRO_0000251445Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei217 – 2171N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiQ13QV1.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi266265.Bxe_B2453.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13QV1.
    SMRiQ13QV1. Positions 34-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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.

    Q13QV1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDFSQPVID SIHKPRDAAN PRERYAAGVM KYREMGYWQP DYAPKDTDVI    50
    ALFRITPQPG VDPEEAAAAV AGESSTATWT VVWTDRLTAC DIYRAKAYRV 100
    DPVPASNAAE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR 150
    LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN 200
    YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFAMEA VNRAQAETGE 250
    VKGHYLNVTA GTMEDMYERA EFAKELGSCI VMIDLVIGWT AIQSMARWAR 300
    RNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL 350
    EGDPLSVQGY YNVCRESHNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG 400
    QMHQLLDLFG DDAILQFGGG TIGHPAGIQA GAVANRVALE AMVKARNEGR 450
    DIVHEGPDIL EAAARWCTPL KQALDTWRDV TFNYASTDTP DFAATPTAA 499
    Length:499
    Mass (Da):55,239
    Last modified:August 22, 2006 - v1
    Checksum:i5F82AF41666CDB74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000271 Genomic DNA. Translation: ABE33538.1.
    RefSeqiWP_011490903.1. NC_007952.1.
    YP_552888.1. NC_007952.1.

    Genome annotation databases

    EnsemblBacteriaiABE33538; ABE33538; Bxe_B2453.
    GeneIDi4007051.
    KEGGibxe:Bxe_B2453.
    PATRICi19335974. VBIBurXen52548_5256.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000271 Genomic DNA. Translation: ABE33538.1 .
    RefSeqi WP_011490903.1. NC_007952.1.
    YP_552888.1. NC_007952.1.

    3D structure databases

    ProteinModelPortali Q13QV1.
    SMRi Q13QV1. Positions 34-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266265.Bxe_B2453.

    Proteomic databases

    PRIDEi Q13QV1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE33538 ; ABE33538 ; Bxe_B2453 .
    GeneIDi 4007051.
    KEGGi bxe:Bxe_B2453.
    PATRICi 19335974. VBIBurXen52548_5256.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BXEN266265:GJII-5191-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LB400.

    Entry informationi

    Entry nameiRBL_BURXL
    AccessioniPrimary (citable) accession number: Q13QV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 55 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3