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D6CTT0

- D6CTT0_THIA3

UniProt

D6CTT0 - D6CTT0_THIA3

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.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
    Binding sitei113 – 1131Substrate; in homodimeric partnerUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei289 – 2891Proton acceptorUniRule annotation
    Binding sitei290 – 2901SubstrateUniRule annotation
    Binding sitei323 – 3231SubstrateUniRule annotation
    Sitei331 – 3311Transition state stabilizerUniRule annotation
    Binding sitei370 – 3701SubstrateUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciTARS426114-WGS:GSYJ-1952-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:cbbMUniRule annotationImported
    Ordered Locus Names:THI_2041Imported
    OrganismiThiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)Imported
    Taxonomic identifieri426114 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas
    ProteomesiUP000002372: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliD6CTT0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01339. RuBisCO_L_type2.
    InterProiIPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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.
    PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    D6CTT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE    50
    SSTGTNVEVS TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR 100
    FMIVSFLTLV IGNNQGMGDV EYGKMIDFYV PERAIQMFDG PATDISNLWR 150
    ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ AAYQFWLGGD FIKNDEPQGN 200
    QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH EMCARADFAL 250
    EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS 300
    SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC 350
    QGPVYYQKWY GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG 400
    HIDSPAAGAK SLRQAYECWK AGADPIEYAK EHIEFARAFE SFPGDADKLF 450
    PGWRDKLGVH K 461
    Length:461
    Mass (Da):50,819
    Last modified:July 13, 2010 - v1
    Checksum:i15B9E0F51FEAA8D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP475956 Genomic DNA. Translation: CAZ88699.1.
    RefSeqiWP_013106007.1. NC_014145.1.
    YP_003624515.1. NC_014145.1.

    Genome annotation databases

    EnsemblBacteriaiCAZ88699; CAZ88699; THI_2041.
    GeneIDi13879779.
    KEGGithi:THI_2041.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP475956 Genomic DNA. Translation: CAZ88699.1 .
    RefSeqi WP_013106007.1. NC_014145.1.
    YP_003624515.1. NC_014145.1.

    3D structure databases

    ProteinModelPortali D6CTT0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAZ88699 ; CAZ88699 ; THI_2041 .
    GeneIDi 13879779.
    KEGGi thi:THI_2041.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci TARS426114-WGS:GSYJ-1952-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01339. RuBisCO_L_type2.
    InterProi IPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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.
    PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Genoscope - CEA
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: 3As.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 22701 / CIP 110005 / 3AsImported.

    Entry informationi

    Entry nameiD6CTT0_THIA3
    AccessioniPrimary (citable) accession number: D6CTT0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 28 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3