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F0LLL8

- F0LLL8_THEBM

UniProt

F0LLL8 - F0LLL8_THEBM

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermococcus barophilus (strain DSM 11836 / MP)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      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

    LyaseUniRule annotation, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciTBAR391623:GH3I-839-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:TERMP_00818Imported
    OrganismiThermococcus barophilus (strain DSM 11836 / MP)Imported
    Taxonomic identifieri391623 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000007478: Chromosome

    PTM / Processingi

    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

    Structurei

    3D structure databases

    ProteinModelPortaliF0LLL8.
    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

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiIFRESHY.

    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.

    F0LLL8-1 [UniParc]FASTAAdd to Basket

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    MSEKFDKIYD YYVDKSYEPN KKRDIIAVFR ITPAEGYSIE AVAGGVAAES    50
    STGTWTTLYN WYEEERWADL SAKAYDFHDM GDGSWIVKIA YPFHAFEEAN 100
    LPGLLASIAG NIFGMRRAKA LRLEDIYFPE KLIREFDGPA FGMEGVRKML 150
    EIKDRPIYGV VPKPKVGYSP EEFEKLATEL LMNGADYMKD DENLTSPWYN 200
    RFEERAEIIA RIIEKVENET GEKKTWFANI TANVPEMEER LEILADLGLK 250
    HAMVDVVITG WGALQYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV 300
    LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARIFRES HYKPDENDVF 350
    HLEQKFYHIK AGFPTSSGGL HPGNLPIVFD ALGTDIVIQV GGGTLGHPDG 400
    PAAGARAVRQ AIDAYMQGIP LDEYAKTHEE LARALEKWGH VTPV 444
    Length:444
    Mass (Da):49,883
    Last modified:May 3, 2011 - v1
    Checksum:i8912158B172E6588
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002372 Genomic DNA. Translation: ADT83795.1.
    RefSeqiWP_013467093.1. NC_014804.1.
    YP_004071018.1. NC_014804.1.

    Genome annotation databases

    EnsemblBacteriaiADT83795; ADT83795; TERMP_00818.
    GeneIDi10041136.
    KEGGitba:TERMP_00818.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002372 Genomic DNA. Translation: ADT83795.1 .
    RefSeqi WP_013467093.1. NC_014804.1.
    YP_004071018.1. NC_014804.1.

    3D structure databases

    ProteinModelPortali F0LLL8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADT83795 ; ADT83795 ; TERMP_00818 .
    GeneIDi 10041136.
    KEGGi tba:TERMP_00818.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi IFRESHY.

    Enzyme and pathway databases

    BioCyci TBAR391623:GH3I-839-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. "Complete genome sequence of the hyperthermophilic, piezophilic, heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP."
      Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.
      J. Bacteriol. 193:1481-1482(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 11836 / MPImported.

    Entry informationi

    Entry nameiF0LLL8_THEBM
    AccessioniPrimary (citable) accession number: F0LLL8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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 proteomeImported

    External Data

    Dasty 3