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F8GL95

- F8GL95_NITSI

UniProt

F8GL95 - F8GL95_NITSI

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nitrosomonas sp. (strain Is79A3)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 20 (01 Oct 2014)
      Sequence version 1 (21 Sep 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 sitei130 – 1301Substrate; in homodimeric partnerUniRule annotation
    Binding sitei180 – 1801SubstrateUniRule annotation
    Active sitei182 – 1821Proton acceptorUniRule annotation
    Binding sitei184 – 1841SubstrateUniRule annotation
    Metal bindingi208 – 2081Magnesium; via carbamate groupUniRule annotation
    Metal bindingi210 – 2101MagnesiumUniRule annotation
    Metal bindingi211 – 2111MagnesiumUniRule annotation
    Active sitei300 – 3001Proton acceptorUniRule annotation
    Binding sitei301 – 3011SubstrateUniRule annotation
    Binding sitei333 – 3331SubstrateUniRule annotation
    Sitei340 – 3401Transition state stabilizerUniRule annotation
    Binding sitei385 – 3851SubstrateUniRule 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

    Enzyme and pathway databases

    BioCyciNSP261292:GH7H-3270-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
    Ordered Locus Names:Nit79A3_3235Imported
    OrganismiNitrosomonas sp. (strain Is79A3)Imported
    Taxonomic identifieri261292 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000000501: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei208 – 2081N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    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.

    F8GL95-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASETMKEGK ERYKSGVIPY KKMGYWEPSY VPKDTDVIAL FRITPQPGVD    50
    HEEAAAAVAG ESSTATWTVV WTDRLTACEL YRAKAYKSEL VPNTGPGTKN 100
    EAQYFAYIAY DIDLFEEGSI ANLTASIIGN VFGFKAVKAL RLEDMRIPVA 150
    YLKTFQGPAT GIVVERERLD KFGRPLLGAT TKPKLGLSGR NYGRVVYEGL 200
    KGGLDFMKDD ENINSQPFMH WRDRFLYCME AVNKASAATG EVKGHYLNVT 250
    AGTMEDMYER AEFAKSLGSV IVMIDLVIGY TAIQSMAKWA RRNDMILHLH 300
    RAGNSTYSRQ KNHGMNFRVI CKWMRMAGVD HIHAGTVVGK LEGDPLMIKG 350
    FYDTLRDTHT EKNLEHGLFF DQDWASLNKV MPVASGGIHA GQMHQLLDYL 400
    GEDVILQFGG GTIGHPQGIQ AGATANRVAL EAMVLARNEG RDYVKEGPQI 450
    LADAAKWCTP LKQALDTWKD ITFNYDSTDT ADFVPSATAN V 491
    Length:491
    Mass (Da):54,472
    Last modified:September 21, 2011 - v1
    Checksum:iE1561A3351780AF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002876 Genomic DNA. Translation: AEJ02969.1.
    RefSeqiWP_013967179.1. NC_015731.1.
    YP_004696368.1. NC_015731.1.

    Genome annotation databases

    EnsemblBacteriaiAEJ02969; AEJ02969; Nit79A3_3235.
    GeneIDi10935341.
    KEGGinii:Nit79A3_3235.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002876 Genomic DNA. Translation: AEJ02969.1 .
    RefSeqi WP_013967179.1. NC_015731.1.
    YP_004696368.1. NC_015731.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEJ02969 ; AEJ02969 ; Nit79A3_3235 .
    GeneIDi 10935341.
    KEGGi nii:Nit79A3_3235.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci NSP261292:GH7H-3270-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 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Is79A3Imported.

    Entry informationi

    Entry nameiF8GL95_NITSI
    AccessioniPrimary (citable) accession number: F8GL95
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 20 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