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L0GWD2

- L0GWD2_9GAMM

UniProt

L0GWD2 - L0GWD2_9GAMM

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thioflavicoccus mobilis 8321
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 11 (01 Oct 2014)
      Sequence version 1 (06 Mar 2013)
      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 sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei286 – 2861Proton acceptorUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei326 – 3261Transition state stabilizerUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule 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 annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunitUniRule annotation
    Gene namesi
    Name:cbbLUniRule annotation
    ORF Names:Thimo_0765Imported
    OrganismiThioflavicoccus mobilis 8321Imported
    Taxonomic identifieri765912 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThioflavicoccus
    ProteomesiUP000010816: Chromosome

    PTM / Processingi

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliL0GWD2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    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.

    L0GWD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKTYNAGVK DYRETYWMPD YTPKDTDILA CFKITPQPGV PREEAAAAVA    50
    AESSTGTWTT VWTDLLTDLD YYKGRAYAIE DVPGDDERFY AFIAYPIDLF 100
    EEGSVVNVFT SLVGNVFGFK AVRTLRLEDV RFPIAYVMTC NGPPHGIQVE 150
    RDIMNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS 200
    QPFMRWRQRF DFVMEAIDKA ESETGERKGH YLNVTAPTPD EMFKRAEHAK 250
    ELGAPIIMHD YITGGWCANT GLAQWCRDNG VLLHIHRAMH AVIDRHPHHG 300
    IHFRVLAKLL RLSGGDHLHT GTVVGKLEGD RAATLGWIDL LRESYVEEDR 350
    SRGIFFDQDW GSMPGVFAVA SGGIHVWHMP ALVTIFGDDA VLQFGGGTLG 400
    HPWGNAAGAA ANRVALEACV EARNRGVAIE KEGKEVLTAA ANNSPELKAA 450
    METWKEIKFE FDTVDKLDVA HK 472
    Length:472
    Mass (Da):52,514
    Last modified:March 6, 2013 - v1
    Checksum:i265A348FD4ADD3DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003051 Genomic DNA. Translation: AGA89604.1.
    RefSeqiWP_015279751.1. NC_019940.1.
    YP_007243234.1. NC_019940.1.

    Genome annotation databases

    EnsemblBacteriaiAGA89604; AGA89604; Thimo_0765.
    GeneIDi14303029.
    KEGGitmb:Thimo_0765.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003051 Genomic DNA. Translation: AGA89604.1 .
    RefSeqi WP_015279751.1. NC_019940.1.
    YP_007243234.1. NC_019940.1.

    3D structure databases

    ProteinModelPortali L0GWD2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AGA89604 ; AGA89604 ; Thimo_0765 .
    GeneIDi 14303029.
    KEGGi tmb:Thimo_0765.

    Phylogenomic databases

    KOi K01601.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi IPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    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. "Complete sequence of chromosome of Thioflavicoccus mobilis 8321."
      US DOE Joint Genome Institute
      Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K.
      , Liu Z., Imhoff J., Thiel V., Frigaard N.-U., Bryant D., Woyke T.
      Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: 8321Imported.

    Entry informationi

    Entry nameiL0GWD2_9GAMM
    AccessioniPrimary (citable) accession number: L0GWD2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 6, 2013
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 11 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 form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel".UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3