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H0Q551

- H0Q551_9RHOO

UniProt

H0Q551 - H0Q551_9RHOO

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Azoarcus sp. KH32C
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 (22 Feb 2012)
      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 sitei128 – 1281Substrate; in homodimeric partnerUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Active sitei180 – 1801Proton acceptorUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Metal bindingi206 – 2061Magnesium; via carbamate groupUniRule annotation
    Metal bindingi208 – 2081MagnesiumUniRule annotation
    Metal bindingi209 – 2091MagnesiumUniRule annotation
    Active sitei298 – 2981Proton acceptorUniRule annotation
    Binding sitei299 – 2991SubstrateUniRule annotation
    Binding sitei331 – 3311SubstrateUniRule annotation
    Sitei338 – 3381Transition state stabilizerUniRule annotation
    Binding sitei383 – 3831SubstrateUniRule 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 annotationImported
    Synonyms:rbcLImported
    ORF Names:AZKH_p0231Imported
    Encoded oniPlasmid pAZKHImported
    OrganismiAzoarcus sp. KH32CImported
    Taxonomic identifieri748247 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus
    ProteomesiUP000007106: Plasmid pAZKH

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliH0Q551.
    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.

    H0Q551-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGALETAEAI IDPKQRYRAG VLKYAQMGYW DGDYEPKETD VLALFRITPQ    50
    EGVDPIEAAA AVAGESSTAT WTVVWTDRLT ACDRYRAKAY RVDPVPGQPG 100
    QYFCYVAYEL DLFEEGSIAN LTASIIGNVF SFKPIKAARL EDMRLPVAYV 150
    KTFRGPPTGI VVERERLNCF GRPLLGATTK PKLGLSGKNY GRVVYEALLG 200
    GLDFTKDDEN INSQPFMHWR DRFLYVMEGV NRASAATGEV KGHYLNVTAG 250
    TMEEMYARAE FAKSLGSTIV MVDLIIGWTA IQSMSNWCRA NDMILHMHRA 300
    GHGTYTRQKN HGISFRVIAK WLRLAGVDHL HAGTAVGKLE GDPMTVQGYY 350
    NVCREMKNAV DLPRGIFFEQ DWASLRRVMP VASGGIHAGQ MHQLLDLFGD 400
    DVVLQFGGGT IGHPMGIQAG ATANRVALEA MVLARNEGRD IASEGSDILK 450
    AAARDCAPLR AALDTWGEVS FNYTSTDTSD FVPTASVA 488
    Length:488
    Mass (Da):53,586
    Last modified:February 22, 2012 - v1
    Checksum:iA955779E87AD0C45
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012305 Genomic DNA. Translation: BAL27114.1.
    RefSeqiWP_015451888.1. NC_020548.1.
    YP_007598171.1. NC_020548.1.

    Genome annotation databases

    EnsemblBacteriaiBAL27114; BAL27114; AZKH_p0231.
    GeneIDi14823035.
    KEGGiaza:AZKH_p0231.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012305 Genomic DNA. Translation: BAL27114.1 .
    RefSeqi WP_015451888.1. NC_020548.1.
    YP_007598171.1. NC_020548.1.

    3D structure databases

    ProteinModelPortali H0Q551.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAL27114 ; BAL27114 ; AZKH_p0231 .
    GeneIDi 14823035.
    KEGGi aza:AZKH_p0231.

    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 genome sequence of Azoarcus sp. KH32C."
      Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., Senoo K.
      Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: KH32CImported.
      Plasmid: pAZKH

    Entry informationi

    Entry nameiH0Q551_9RHOO
    AccessioniPrimary (citable) accession number: H0Q551
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 22, 2012
    Last sequence update: February 22, 2012
    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, PlasmidImported, Reference proteomeImported

    External Data

    Dasty 3