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F0IX26

- F0IX26_ACIMA

UniProt

F0IX26 - F0IX26_ACIMA

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (03 May 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 sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Active sitei184 – 1841Proton acceptorUniRule annotation
    Binding sitei186 – 1861SubstrateUniRule annotation
    Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
    Metal bindingi212 – 2121MagnesiumUniRule annotation
    Metal bindingi213 – 2131MagnesiumUniRule annotation
    Active sitei302 – 3021Proton acceptorUniRule annotation
    Binding sitei303 – 3031SubstrateUniRule annotation
    Binding sitei335 – 3351SubstrateUniRule annotation
    Sitei342 – 3421Transition state stabilizerUniRule annotation
    Binding sitei387 – 3871SubstrateUniRule 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

    BioCyciAMUL926570:GI8V-1104-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 annotationImported
    Ordered Locus Names:ACMV_10890Imported
    OrganismiAcidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301)Imported
    Taxonomic identifieri926570 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
    ProteomesiUP000007100: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliF0IX26.
    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.

    F0IX26-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR    50
    ITPQDGVDPV EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP 100
    NAPGQYFAYI AYDLALFEPG SIANLTASII GNVFGFKPLK ALRLEDMRLP 150
    VAYVKTFDGP ATGIVVERER LDKFGRPLLG ATVKPKLGLS GRNYGRVVYE 200
    ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA TGEVKGTYLN 250
    VTAGTMEDMY ERASFAHELG STIIMIDLVI GYTAIQSMSK WARKHDMILH 300
    LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT 350
    RGFYDILRED YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH 400
    HLGEDVVLQF GGGTIGHPQG IAAGAMANRV ALEAMILARN EGRDYLAEGP 450
    QILNDAARHC LPLRQALDTW GEVTFNYAST DTPDFAPTAM PAY 493
    Length:493
    Mass (Da):54,783
    Last modified:May 3, 2011 - v1
    Checksum:iF3AEA66096D65998
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012035 Genomic DNA. Translation: BAJ80436.1.
    RefSeqiWP_013639783.1. NC_015186.1.
    YP_004283318.1. NC_015186.1.

    Genome annotation databases

    EnsemblBacteriaiBAJ80436; BAJ80436; ACMV_10890.
    GeneIDi10320528.
    KEGGiamv:ACMV_10890.
    PATRICi46810953. VBIAciMul178205_1458.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012035 Genomic DNA. Translation: BAJ80436.1 .
    RefSeqi WP_013639783.1. NC_015186.1.
    YP_004283318.1. NC_015186.1.

    3D structure databases

    ProteinModelPortali F0IX26.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAJ80436 ; BAJ80436 ; ACMV_10890 .
    GeneIDi 10320528.
    KEGGi amv:ACMV_10890.
    PATRICi 46810953. VBIAciMul178205_1458.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci AMUL926570:GI8V-1104-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. "Whole genome sequence of Acidiphilium multivorum AIU301."
      Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H., Hosoyama A., Yamada R., Fujita N.
      Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 11245 / JCM 8867 / AIU301Imported.

    Entry informationi

    Entry nameiF0IX26_ACIMA
    AccessioniPrimary (citable) accession number: F0IX26
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 22 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