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Q8U1P9

- RBL_PYRFU

UniProt

Q8U1P9 - RBL_PYRFU

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.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
    Active sitei155 – 1551Proton acceptorUniRule annotation
    Binding sitei157 – 1571SubstrateUniRule annotation
    Metal bindingi181 – 1811Magnesium; via carbamate groupUniRule annotation
    Metal bindingi183 – 1831MagnesiumUniRule annotation
    Metal bindingi184 – 1841MagnesiumUniRule annotation
    Active sitei273 – 2731Proton acceptorUniRule annotation
    Binding sitei274 – 2741SubstrateUniRule annotation
    Binding sitei306 – 3061SubstrateUniRule annotation
    Sitei313 – 3131Transition state stabilizerUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. AMP catabolic process Source: UniProtKB-HAMAP
    2. carbon fixation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Oxidoreductase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:rbcLUniRule annotation
    Ordered Locus Names:PF1156
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Ribulose bisphosphate carboxylasePRO_0000062676Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiQ8U1P9.

    Interactioni

    Subunit structurei

    Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.UniRule annotation

    Protein-protein interaction databases

    STRINGi186497.PF1156.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8U1P9.
    SMRiQ8U1P9. Positions 1-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3453Substrate bindingUniRule annotation
    Regioni365 – 3684Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiVIVTFRV.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01133. RuBisCO_L_type3.
    InterProiIPR017712. RuBisCO_III.
    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.
    TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8U1P9-1 [UniParc]FASTAAdd to Basket

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    MKVEWYLDFV DLDYTPGRDE LIVEYYFEPN GVSPEEAAGR IASESSIGTW    50
    TTLWKMPEMA KRSMAKVFYL EKSGEGYIAK IAYPLTLFEE GSIVQLLSAI 100
    AGNIFGMKAL KNLRLLDFHP PYEYLRHFKG PQYGVKGIRE FMGVKERPLT 150
    ATVPKPKMGW SVDEYAEIAY ELWSGGIDLL KDDENFTSFP FNRFEERVKK 200
    LYRIRDIVEA ETEERKEYLI NITGSVDVME KRAELVANEG GQYVMIDIIV 250
    TGWSALQYMR EVTEDLGLAI HAHRAMHAAF TRNPKHGITM YAIAKLARMI 300
    GVDQIHTGTA VGKMAGDYEE VKRINDFLLS KWEHIREVFP VASGGLHPGL 350
    MPELIRLFGK DLVIQAGGGV MGHPDGPRAG AKALRDAIDA ALEGVDLEEK 400
    AKSSPELKKA LDKWGYLKPK 420
    Length:420
    Mass (Da):47,348
    Last modified:June 1, 2002 - v1
    Checksum:i0271D055DCFF3DC4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81280.1.
    RefSeqiNP_578885.1. NC_003413.1.
    WP_011012296.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL81280; AAL81280; PF1156.
    GeneIDi1469025.
    KEGGipfu:PF1156.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81280.1 .
    RefSeqi NP_578885.1. NC_003413.1.
    WP_011012296.1. NC_003413.1.

    3D structure databases

    ProteinModelPortali Q8U1P9.
    SMRi Q8U1P9. Positions 1-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF1156.

    Proteomic databases

    PRIDEi Q8U1P9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL81280 ; AAL81280 ; PF1156 .
    GeneIDi 1469025.
    KEGGi pfu:PF1156.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi VIVTFRV.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01133. RuBisCO_L_type3.
    InterProi IPR017712. RuBisCO_III.
    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.
    TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

    Entry informationi

    Entry nameiRBL_PYRFU
    AccessioniPrimary (citable) accession number: Q8U1P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3