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F9ZF99

- F9ZF99_9PROT

UniProt

F9ZF99 - F9ZF99_9PROT

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nitrosomonas sp. AL212
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (19 Oct 2011)
      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 sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Metal bindingi197 – 1971MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei327 – 3271Transition state stabilizerUniRule annotation
    Binding sitei372 – 3721SubstrateUniRule 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

    BioCyciNSP153948:GHZ8-718-MONOMER.

    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:NAL212_0872Imported
    OrganismiNitrosomonas sp. AL212Imported
    Taxonomic identifieri153948 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000001629: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliF9ZF99.
    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.
    InterProiIPR020888. 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.

    Sequencei

    Sequence statusi: Complete.

    F9ZF99-1 [UniParc]FASTAAdd to Basket

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    MAVKIYNAGV KEYRQTYWTP DYTPLDTDIL ACFKITPQPG VPREEVAAAV    50
    AAESSTGTWT TVWTDLLTDL DYYKGRAYKI EDVPGDDTCF YAFVAYPIDL 100
    FEEGSVVNVL TSLVGNVFGF KALRALRLED VRFPIAYVKT CGGPPAGIQV 150
    ERDRFNKYGR ALLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENIN 200
    SQPFMRWRDR FQFVVEACQK AERETGERKG HYLNVTAPTP EEMYKRAEFA 250
    KELGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 300
    GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DRAATLGWID TMRDKFIKED 350
    RSRGLFFDQD WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL 400
    GHPWGNAAGA AANRVALEAC VEARNQGVEI EKEGKAILTK AAKSSPELKI 450
    AMETWKEIKF EFDTVDKLDI AHK 473
    Length:473
    Mass (Da):52,537
    Last modified:October 19, 2011 - v1
    Checksum:iB60FE80DB1D12792
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002552 Genomic DNA. Translation: ADZ25799.1.
    RefSeqiWP_013646860.1. NC_015222.1.
    YP_004293961.1. NC_015222.1.

    Genome annotation databases

    EnsemblBacteriaiADZ25799; ADZ25799; NAL212_0872.
    GeneIDi10297382.
    KEGGinit:NAL212_0872.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002552 Genomic DNA. Translation: ADZ25799.1 .
    RefSeqi WP_013646860.1. NC_015222.1.
    YP_004293961.1. NC_015222.1.

    3D structure databases

    ProteinModelPortali F9ZF99.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADZ25799 ; ADZ25799 ; NAL212_0872 .
    GeneIDi 10297382.
    KEGGi nit:NAL212_0872.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci NSP153948:GHZ8-718-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi 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.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of chromosome of Nitrosomonas sp. AL212."
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y.
      , Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.
      Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: AL212Imported.

    Entry informationi

    Entry nameiF9ZF99_9PROT
    AccessioniPrimary (citable) accession number: F9ZF99
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 19 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 proteomeImported

    External Data

    Dasty 3