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B6YXA9

- RBL_THEON

UniProt

B6YXA9 - RBL_THEON

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermococcus onnurineus (strain NA1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (20 Jan 2009)
      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 sitei163 – 1631Proton acceptorUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Metal bindingi189 – 1891Magnesium; via carbamate groupUniRule annotation
    Metal bindingi191 – 1911MagnesiumUniRule annotation
    Metal bindingi192 – 1921MagnesiumUniRule annotation
    Active sitei281 – 2811Proton acceptorUniRule annotation
    Binding sitei282 – 2821SubstrateUniRule annotation
    Binding sitei314 – 3141SubstrateUniRule annotation
    Sitei322 – 3221Transition 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

    Enzyme and pathway databases

    BioCyciTONN523850:GC7X-1267-MONOMER.

    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:TON_1234
    OrganismiThermococcus onnurineus (strain NA1)
    Taxonomic identifieri523850 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000002727: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Ribulose bisphosphate carboxylasePRO_1000137340Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei189 – 1891N6-carboxylysineUniRule annotation

    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

    STRINGi523850.TON_1234.

    Structurei

    3D structure databases

    ProteinModelPortaliB6YXA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni367 – 3693Substrate bindingUniRule annotation
    Regioni389 – 3924Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.

    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.

    B6YXA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEKFDKIYD YYVDKSYEPN KKRDIIAVFR ITPAEGYTIE QVAGGVAAES    50
    STGTWTTLYN WYEEERWADL SAKAYDFIDM GDGSWIVKIA YPFHAFEEAN 100
    LPGLLASIAG NVFGMRRAKG LRLEDMYFPE KLIREFSGPA FGIEGVRKML 150
    EIKDRPIYGV VPKPKVGYSP EEFEKLSYEL LLNGADYMKD DENLTSPWYN 200
    RFEERAETIA KIIEKVESET GEKKTWFANI TADVREMERR LEILADLGLK 250
    HAMVDVVITG WGALEYIRDL AADYGLAIHG HRAMHATFTR NPYHGISMFV 300
    LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARILREE HYKPDENDVF 350
    HLEQKFYSIK PAFPTSSGGL HPGNLPIVID ALGTDIVLQL GGGTLGHPDG 400
    PAAGARAVRQ AIDALVQGIP LDEYAKTHKE LARALEKWGH VTPI 444
    Length:444
    Mass (Da):49,875
    Last modified:January 20, 2009 - v1
    Checksum:i69F7078ECAF9346D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000855 Genomic DNA. Translation: ACJ16722.1.
    RefSeqiYP_002307619.1. NC_011529.1.

    Genome annotation databases

    EnsemblBacteriaiACJ16722; ACJ16722; TON_1234.
    GeneIDi7018257.
    KEGGiton:TON_1234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000855 Genomic DNA. Translation: ACJ16722.1 .
    RefSeqi YP_002307619.1. NC_011529.1.

    3D structure databases

    ProteinModelPortali B6YXA9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 523850.TON_1234.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACJ16722 ; ACJ16722 ; TON_1234 .
    GeneIDi 7018257.
    KEGGi ton:TON_1234.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TONN523850:GC7X-1267-MONOMER.

    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. "The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
      Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
      J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NA1.

    Entry informationi

    Entry nameiRBL_THEON
    AccessioniPrimary (citable) accession number: B6YXA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: January 20, 2009
    Last modified: October 1, 2014
    This is version 41 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