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B0JVL8

- RBL_MICAN

UniProt

B0JVL8 - RBL_MICAN

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Microcystis aeruginosa (strain NIES-843)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      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 sitei119 – 1191Substrate; in homodimeric partnerUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Active sitei171 – 1711Proton acceptorUniRule annotation
    Binding sitei173 – 1731SubstrateUniRule annotation
    Metal bindingi197 – 1971Magnesium; via carbamate groupUniRule annotation
    Metal bindingi199 – 1991MagnesiumUniRule annotation
    Metal bindingi200 – 2001MagnesiumUniRule annotation
    Active sitei290 – 2901Proton acceptorUniRule annotation
    Binding sitei291 – 2911SubstrateUniRule annotation
    Binding sitei323 – 3231SubstrateUniRule annotation
    Sitei330 – 3301Transition state stabilizerUniRule annotation
    Binding sitei375 – 3751SubstrateUniRule 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

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMAER449447:GHO8-4825-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
    Synonyms:rbcLUniRule annotation
    Ordered Locus Names:MAE_47890
    OrganismiMicrocystis aeruginosa (strain NIES-843)
    Taxonomic identifieri449447 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis
    ProteomesiUP000001510: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Ribulose bisphosphate carboxylase large chainPRO_0000355751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei197 – 1971N6-carboxylysineUniRule annotation
    Disulfide bondi243 – 243Interchain; in linked formUniRule annotation

    Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiB0JVL8.
    PRIDEiB0JVL8.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

    Protein-protein interaction databases

    STRINGi449447.MAE_47890.

    Structurei

    3D structure databases

    ProteinModelPortaliB0JVL8.
    SMRiB0JVL8. Positions 8-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    OrthoDBiEOG6ZKXMS.

    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.

    B0JVL8-1 [UniParc]FASTAAdd to Basket

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    MVQAKSKGFQ AGVKDYRLTY YTPDYTPKDT DLLACFRVTP QPGVPPEEAG    50
    AAVAAESSTG TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQFFCFVAYP 100
    LDLFEEGSVT NILTSIVGNV FGFKALRGLR LEDIRFPVAL IKTFQGPPHG 150
    ITVERDKLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE 200
    NINSQPFMRW RDRFLFVQEA IVKSQAETNE VKGHYLNVTA PTCEQMMQRA 250
    EFAAEIKTPI IMHDYLTGGF TANTTLAKFC RDKGLLLHIH RAMHAVIDRQ 300
    KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV 350
    EEDRARGIFF TQDYASLPGV MPVASGGIHV WHMPALVEIF GDDSCLQFGG 400
    GTLGHPWGNA PGATANRVAL EACIQARNEG RSLAREGNDV IREACRWSPE 450
    LAAACELWKE IKFEFEAMDT L 471
    Length:471
    Mass (Da):52,544
    Last modified:March 18, 2008 - v1
    Checksum:i0758222DD0F46B6C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009552 Genomic DNA. Translation: BAG04611.1.
    RefSeqiYP_001659803.1. NC_010296.1.

    Genome annotation databases

    EnsemblBacteriaiBAG04611; BAG04611; MAE_47890.
    GeneIDi5865621.
    KEGGimar:MAE_47890.
    PATRICi22634095. VBIMicAer59304_4356.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009552 Genomic DNA. Translation: BAG04611.1 .
    RefSeqi YP_001659803.1. NC_010296.1.

    3D structure databases

    ProteinModelPortali B0JVL8.
    SMRi B0JVL8. Positions 8-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 449447.MAE_47890.

    Proteomic databases

    PaxDbi B0JVL8.
    PRIDEi B0JVL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAG04611 ; BAG04611 ; MAE_47890 .
    GeneIDi 5865621.
    KEGGi mar:MAE_47890.
    PATRICi 22634095. VBIMicAer59304_4356.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.
    OrthoDBi EOG6ZKXMS.

    Enzyme and pathway databases

    BioCyci MAER449447:GHO8-4825-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: NIES-843.

    Entry informationi

    Entry nameiRBL_MICAN
    AccessioniPrimary (citable) accession number: B0JVL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 43 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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 proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3