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O28635

- RBL_ARCFU

UniProt

O28635 - RBL_ARCFU

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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.1 PublicationUniRule annotation
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.1 PublicationUniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Enzyme regulationi

    Reversibly inhibited by O2.1 Publication

    Temperature dependencei

    Active over a broad temperature range.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei160 – 1601Proton acceptorUniRule annotation
    Binding sitei162 – 1621SubstrateUniRule annotation
    Metal bindingi186 – 1861Magnesium; via carbamate groupUniRule annotation
    Metal bindingi188 – 1881MagnesiumUniRule annotation
    Metal bindingi189 – 1891MagnesiumUniRule annotation
    Active sitei278 – 2781Proton acceptorUniRule annotation
    Binding sitei279 – 2791SubstrateUniRule annotation
    Binding sitei311 – 3111SubstrateUniRule annotation
    Sitei319 – 3191Transition 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

    BioCyciAFUL224325:GJBC-1672-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:AF_1638
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Ribulose bisphosphate carboxylasePRO_0000062671Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei186 – 1861N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.1 Publication

    Protein-protein interaction databases

    STRINGi224325.AF1638.

    Structurei

    3D structure databases

    ProteinModelPortaliO28635.
    SMRiO28635. Positions 10-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni364 – 3663Substrate bindingUniRule annotation
    Regioni386 – 3894Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    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.

    O28635-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG    50
    TWTSLHPWYD EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG 100
    LLASIAGNVF GMKRVKGLRL EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA 150
    DRPIVGTVPK PKVGYSAEEV EKLAYELLSG GMDYIKDDEN LTSPAYCRFE 200
    ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL VAELGNPHVM 250
    VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK 300
    LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS 350
    QNFHHIKPAM PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA 400
    GAKAVRQALD AIISAIPLEE HAKQHPELQA ALEKWGRVTP I 441
    Length:441
    Mass (Da):48,557
    Last modified:January 1, 1998 - v1
    Checksum:iF191B4A83F36F3FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89603.1.
    PIRiE69454.
    RefSeqiNP_070466.1. NC_000917.1.
    WP_010879134.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB89603; AAB89603; AF_1638.
    GeneIDi1484861.
    KEGGiafu:AF1638.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89603.1 .
    PIRi E69454.
    RefSeqi NP_070466.1. NC_000917.1.
    WP_010879134.1. NC_000917.1.

    3D structure databases

    ProteinModelPortali O28635.
    SMRi O28635. Positions 10-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224325.AF1638.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB89603 ; AAB89603 ; AF_1638 .
    GeneIDi 1484861.
    KEGGi afu:AF1638.

    Phylogenomic databases

    eggNOGi COG1850.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci AFUL224325:GJBC-1672-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 the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    2. "Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea."
      Finn M.W., Tabita F.R.
      J. Bacteriol. 185:3049-3059(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

    Entry informationi

    Entry nameiRBL_ARCFU
    AccessioniPrimary (citable) accession number: O28635
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 100 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