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E0U7P5

- E0U7P5_CYAP2

UniProt

E0U7P5 - E0U7P5_CYAP2

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain PCC 7822)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (02 Nov 2010)
      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 sitei120 – 1201Substrate; in homodimeric partnerUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Active sitei172 – 1721Proton acceptorUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Metal bindingi198 – 1981Magnesium; via carbamate groupUniRule annotation
    Metal bindingi200 – 2001MagnesiumUniRule annotation
    Metal bindingi201 – 2011MagnesiumUniRule annotation
    Active sitei291 – 2911Proton acceptorUniRule annotation
    Binding sitei292 – 2921SubstrateUniRule annotation
    Binding sitei324 – 3241SubstrateUniRule annotation
    Sitei331 – 3311Transition state stabilizerUniRule annotation
    Binding sitei376 – 3761SubstrateUniRule 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 annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciCSP497965:GJAC-2935-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:Cyan7822_2899Imported
    OrganismiCyanothece sp. (strain PCC 7822)Imported
    Taxonomic identifieri497965 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
    ProteomesiUP000008206: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliE0U7P5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.

    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.

    E0U7P5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQSKAKGGF QAGVKDYRLT YYTPDYTPKD TDLLACFRVT PQPGVPPEEA    50
    GAAVAAESST GTWTTVWTDG LTDLDRYKGR CYDIEPVPNE DNQYFCFVAY 100
    PLDLFEEGSV TNILTSIVGN VFGFKALRAL RLEDIRFPVA LLKTFQGPPH 150
    GITVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 200
    ENINSQPFMR WRDRFLFVQE AIEKAQAETN EIKGHYLNVT AGTLEEMMKR 250
    AEFAKEIKTP IIMHDYLTGG FTANTTLAKF CRDNGLLLHI HRAMHAVIDR 300
    QKNHGIHFRV LAKCLRMSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY 350
    VEEDRARGIF FTQDWASMPG VMPVASGGIH VWHMPALVEI FGDDSCLQFG 400
    GGTLGHPWGN APGATANRVA LEACIQARNE GRSLAREGNE VIREAARWSP 450
    ELAAACELWK EIKFEFEAMD TL 472
    Length:472
    Mass (Da):52,657
    Last modified:November 2, 2010 - v1
    Checksum:iCE42E983A700A93A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002198 Genomic DNA. Translation: ADN14857.1.
    RefSeqiWP_013322960.1. NC_014501.1.
    YP_003888132.1. NC_014501.1.

    Genome annotation databases

    EnsemblBacteriaiADN14857; ADN14857; Cyan7822_2899.
    GeneIDi9739388.
    KEGGicyj:Cyan7822_2899.
    PATRICi42286569. VBICyaSp18455_3032.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002198 Genomic DNA. Translation: ADN14857.1 .
    RefSeqi WP_013322960.1. NC_014501.1.
    YP_003888132.1. NC_014501.1.

    3D structure databases

    ProteinModelPortali E0U7P5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADN14857 ; ADN14857 ; Cyan7822_2899 .
    GeneIDi 9739388.
    KEGGi cyj:Cyan7822_2899.
    PATRICi 42286569. VBICyaSp18455_3032.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci CSP497965:GJAC-2935-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. "Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
      Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
      MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 7822Imported.

    Entry informationi

    Entry nameiE0U7P5_CYAP2
    AccessioniPrimary (citable) accession number: E0U7P5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 2, 2010
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 27 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