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C7QSC5

- C7QSC5_CYAP0

UniProt

C7QSC5 - C7QSC5_CYAP0

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain PCC 8802) (Synechococcus sp. (strain RF-2))
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (13 Oct 2009)
      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

    BioCyciCSP395962:GJC3-1637-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:Cyan8802_1628Imported
    OrganismiCyanothece sp. (strain PCC 8802) (Synechococcus sp. (strain RF-2))Imported
    Taxonomic identifieri395962 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
    ProteomesiUP000000415: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-carboxylysineUniRule annotation
    Disulfide bondi244 – 244Interchain; 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 bondUniRule annotation

    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

    STRINGi395962.Cyan8802_1628.

    Structurei

    3D structure databases

    ProteinModelPortaliC7QSC5.
    SMRiC7QSC5. Positions 9-466.
    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.

    C7QSC5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQAKSKSGF EAGVKDYRLT YYTPDYTPKD TDLLACFRMT PQPGVPPEEA    50
    GAAVAAESST GTWTTVWTDN LTDLDRYKGR CYDIEKVENE DNQYFCFIAY 100
    PLDLFEEGSV TNVLTSLVGN VFGFKALRAL RLEDIRFPVA LIKTFQGPPH 150
    GITVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 200
    ENINSQPFMR WRDRFLFVQD AIEKAQAETN EVKGHYLNVT AGTCEEMLKR 250
    AEFAKEIKTP IIMHDFLTGG FTANTTLAKF CRDNGLLLHI HRAMHAVIDR 300
    QKNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY 350
    VEEDRSRGIF FTQDYASMPG TMPVASGGIH VWHMPALVEI FGDDSCLQFG 400
    GGTLGHPWGN APGATANRVA LEACIQARNE GRSLAREGND VIREACKWSP 450
    ELAAACELWK EIKFEFEAMD TL 472
    Length:472
    Mass (Da):52,735
    Last modified:October 13, 2009 - v1
    Checksum:i9E7709AB3A482831
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001701 Genomic DNA. Translation: ACV00534.1.
    RefSeqiYP_003137369.1. NC_013161.1.

    Genome annotation databases

    EnsemblBacteriaiACV00534; ACV00534; Cyan8802_1628.
    GeneIDi8390940.
    KEGGicyh:Cyan8802_1628.
    PATRICi21584769. VBICyaSp112625_1713.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001701 Genomic DNA. Translation: ACV00534.1 .
    RefSeqi YP_003137369.1. NC_013161.1.

    3D structure databases

    ProteinModelPortali C7QSC5.
    SMRi C7QSC5. Positions 9-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 395962.Cyan8802_1628.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACV00534 ; ACV00534 ; Cyan8802_1628 .
    GeneIDi 8390940.
    KEGGi cyh:Cyan8802_1628.
    PATRICi 21584769. VBICyaSp112625_1713.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CSP395962:GJC3-1637-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 8802Imported.

    Entry informationi

    Entry nameiC7QSC5_CYAP0
    AccessioniPrimary (citable) accession number: C7QSC5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 13, 2009
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 38 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