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K9SU87

- K9SU87_9SYNE

UniProt

K9SU87 - K9SU87_9SYNE

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. PCC 7502
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 12 (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 in the photorespiration process. 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 sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Active sitei176 – 1761Proton acceptorUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule 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. photorespiration Source: UniProtKB-KW
    2. 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, PhotorespirationUniRule 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
    Synonyms:rbcLUniRule annotation
    ORF Names:Syn7502_01669Imported
    OrganismiSynechococcus sp. PCC 7502Imported
    Taxonomic identifieri1173263 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000010385: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-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.

    K9SU87-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYSQTKTQA KAGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP    50
    FEEAAAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
    YIAYPLDLFE EGSVTNLLTS LVGNVFGFKA LKALRLEDLR IPVAYLKTFQ 150
    GPPHGIQVER DKINKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
    TKDDENINSQ PFQRWRDRFL FVADAIHKAQ AETGEIKGHY LNVTAGTVEE 250
    MLKRAEFAKE LNMPIIMHDF LTAGFTANTT LAHWCRDNGV LLHIHRAMHA 300
    VIDRQKNHGI HFRVLAKCLR MSGGDHIHTG TVVGKLEGDK AITLGFVDLL 350
    RENYVEQDKT RGIYFTQDWA SMPGVMAVAS GGIHIWHMPA LVEIFGDDSV 400
    LQFGGGTLGH PWGNAPGATA NRVALEACVE ARNEGRDLYR EGGDIIREAA 450
    KWSPELAVAC ELWKEIKFEF EAVDTV 476
    Length:476
    Mass (Da):52,993
    Last modified:March 6, 2013 - v1
    Checksum:i40A02D193CE6230C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003594 Genomic DNA. Translation: AFY73725.1.
    RefSeqiWP_015168382.1. NC_019702.1.
    YP_007105860.1. NC_019702.1.

    Genome annotation databases

    EnsemblBacteriaiAFY73725; AFY73725; Syn7502_01669.
    GeneIDi14132214.
    KEGGisynp:Syn7502_01669.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003594 Genomic DNA. Translation: AFY73725.1 .
    RefSeqi WP_015168382.1. NC_019702.1.
    YP_007105860.1. NC_019702.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFY73725 ; AFY73725 ; Syn7502_01669 .
    GeneIDi 14132214.
    KEGGi synp:Syn7502_01669.

    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. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: PCC 7502Imported.

    Entry informationi

    Entry nameiK9SU87_9SYNE
    AccessioniPrimary (citable) accession number: K9SU87
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 6, 2013
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 12 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