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B1WXH3

- RBL_CYAA5

UniProt

B1WXH3 - RBL_CYAA5

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain ATCC 51142)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (20 May 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

    BioCyciCSP43989:GKC8-3206-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:cce_3166
    OrganismiCyanothece sp. (strain ATCC 51142)
    Taxonomic identifieri43989 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
    ProteomesiUP000001203: Chromosome circular

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Ribulose bisphosphate carboxylase large chainPRO_0000355749Add
    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

    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

    STRINGi43989.cce_3166.

    Structurei

    3D structure databases

    ProteinModelPortaliB1WXH3.
    SMRiB1WXH3. 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.

    B1WXH3-1 [UniParc]FASTAAdd to Basket

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    MAQATKSGFN AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QPGVPPEEAG    50
    AAVAAESSTG TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQYFCFIAYP 100
    LDLFEEGSVT NVLTSLVGNV FGFKALRALR LEDIRFPVAL IKTFQGPPHG 150
    ITVERDKLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE 200
    NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA GTCEEMMKRA 250
    EFAKEIGTPI VMHDFLTGGF TANTTLAKFC RDNGILLHIH RAMHAVIDRQ 300
    KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV 350
    EEDRSRGIFF TQDYASMPGT MPVASGGIHV WHMPALVEIF GDDSCLQFGG 400
    GTLGHPWGNA PGATANRVAL EACIQARNEG RNLAREGNDV IREACKWSPE 450
    LAAACELWKE ITFEFEAMDT L 471
    Length:471
    Mass (Da):52,462
    Last modified:May 20, 2008 - v1
    Checksum:i549FB4FF3AFDE916
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000806 Genomic DNA. Translation: ACB52514.1.
    RefSeqiYP_001804580.1. NC_010546.1.

    Genome annotation databases

    EnsemblBacteriaiACB52514; ACB52514; cce_3166.
    GeneIDi6170227.
    KEGGicyt:cce_3166.
    PATRICi21544734. VBICyaSp130209_3185.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000806 Genomic DNA. Translation: ACB52514.1 .
    RefSeqi YP_001804580.1. NC_010546.1.

    3D structure databases

    ProteinModelPortali B1WXH3.
    SMRi B1WXH3. Positions 8-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 43989.cce_3166.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB52514 ; ACB52514 ; cce_3166 .
    GeneIDi 6170227.
    KEGGi cyt:cce_3166.
    PATRICi 21544734. VBICyaSp130209_3185.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CSP43989:GKC8-3206-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: ATCC 51142.

    Entry informationi

    Entry nameiRBL_CYAA5
    AccessioniPrimary (citable) accession number: B1WXH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 40 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