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D5U228

- D5U228_THEAM

UniProt

D5U228 - D5U228_THEAM

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermosphaera aggregans (strain DSM 11486 / M11TL)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (13 Jul 2010)
      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 sitei164 – 1641Proton acceptorUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Metal bindingi190 – 1901Magnesium; via carbamate groupUniRule annotation
    Metal bindingi192 – 1921MagnesiumUniRule annotation
    Metal bindingi193 – 1931MagnesiumUniRule annotation
    Active sitei282 – 2821Proton acceptorUniRule annotation
    Binding sitei283 – 2831SubstrateUniRule annotation
    Binding sitei315 – 3151SubstrateUniRule annotation
    Sitei323 – 3231Transition 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 annotationImported, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciTAGG633148:GHBI-919-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:Tagg_0906Imported
    OrganismiThermosphaera aggregans (strain DSM 11486 / M11TL)Imported
    Taxonomic identifieri633148 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermosphaera
    ProteomesiUP000002376: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei190 – 1901N6-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

    ProteinModelPortaliD5U228.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 3703Substrate bindingUniRule annotation
    Regioni390 – 3934Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    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.

    D5U228-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEKFDFETY HEYIDRTFKP DPDNHVIAVF RIKPAQGFTI DDAAGGVAAE    50
    SSTGTWTTVY NWYDRERVRR LSGRAYEFLD LKDGSWIVKI AYPVELFEEG 100
    NIPGLLASIA GNVFGMRRVE GLRLEDIYLP GGFLKDFKGP SKGVEGVREI 150
    FKVKDRPIVG TVPKPKVGYS PEEVEKLATE LLMGGLDYIK DDENLTSPKY 200
    CSFEARAKAI MKVIDKVEKE TGERKAWFAN ITADVREMEK RLRLVADYGN 250
    PYVMVDVVVS GWGVLNYIRD LAEEYGLAVH AHRAMHASFT RNPYHGISMF 300
    VLAKLYRVIG VDQLHVGTAG AGKLEGGRLD VIRCAKILRE QSFTPDPEDP 350
    FHLPQDMRHI KPAMPVSSGG LHPGNLPPVI DALGPDIVLQ VGGGVVGHPD 400
    GPRAGAMAVR QALDAIVKGI PLDKYAESHR ELARALEKWG FVKPI 445
    Length:445
    Mass (Da):49,428
    Last modified:July 13, 2010 - v1
    Checksum:i358B529EF1A31E75
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001939 Genomic DNA. Translation: ADG91178.1.
    RefSeqiYP_003650130.1. NC_014160.1.

    Genome annotation databases

    EnsemblBacteriaiADG91178; ADG91178; Tagg_0906.
    GeneIDi9165923.
    KEGGitag:Tagg_0906.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001939 Genomic DNA. Translation: ADG91178.1 .
    RefSeqi YP_003650130.1. NC_014160.1.

    3D structure databases

    ProteinModelPortali D5U228.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADG91178 ; ADG91178 ; Tagg_0906 .
    GeneIDi 9165923.
    KEGGi tag:Tagg_0906.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi VIVTFRV.

    Enzyme and pathway databases

    BioCyci TAGG633148:GHBI-919-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 11486 / M11TLImported.
    2. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: DSM 11486.

    Entry informationi

    Entry nameiD5U228_THEAM
    AccessioniPrimary (citable) accession number: D5U228
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 32 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 proteome, Reference proteomeImported

    External Data

    Dasty 3