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Q10WH6

- RBL_TRIEI

UniProt

Q10WH6 - RBL_TRIEI

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Trichodesmium erythraeum (strain IMS101)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      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

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciTERY203124:GJDR-4456-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:Tery_4410
    OrganismiTrichodesmium erythraeum (strain IMS101)
    Taxonomic identifieri203124 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium
    ProteomesiUP000008878: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Ribulose bisphosphate carboxylase large chainPRO_0000299976Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-carboxylysineUniRule annotation
    Disulfide bondi248 – 248Interchain; 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

    PRIDEiQ10WH6.

    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

    STRINGi203124.Tery_4410.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10WH6.
    SMRiQ10WH6. Positions 13-470.
    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.

    Q10WH6-1 [UniParc]FASTAAdd to Basket

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    MSYAKTQTQS KSGYQAGVKD YKLTYYTPDY IPKDTDLLAA FRMSPQPGVP    50
    PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIES VPGEDNQYIC 100
    YVAYPLDLFE EGSVTNMLTS IVGNVFGFKA LRSLRLEDLR IPVAYLKTFQ 150
    GPPHGITVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
    TKDDENINSQ PFMRWRDRFL FAQEAIEKAQ AETGEIKGHY LNVTAPTCEE 250
    MLERADFAKE IGTPIIMHDY LTGGFTANTT LAKWCRRNGV LLHIHRAMHA 300
    VIDRQKAHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM 350
    REDHVEQDRE RGIYFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC 400
    LQFGGGTLGH PWGNAPGATA NRVALEACIQ ARNEGRNLFR EGGDVIREAA 450
    KWSPDLAVAC ELWKEIKFEF EAMDTL 476
    Length:476
    Mass (Da):53,078
    Last modified:August 22, 2006 - v1
    Checksum:i99344CF2E8D99C19
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000393 Genomic DNA. Translation: ABG53398.1.
    RefSeqiYP_723871.1. NC_008312.1.

    Genome annotation databases

    EnsemblBacteriaiABG53398; ABG53398; Tery_4410.
    GeneIDi4246063.
    KEGGiter:Tery_4410.
    PATRICi23994367. VBITriEry99848_5586.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000393 Genomic DNA. Translation: ABG53398.1 .
    RefSeqi YP_723871.1. NC_008312.1.

    3D structure databases

    ProteinModelPortali Q10WH6.
    SMRi Q10WH6. Positions 13-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203124.Tery_4410.

    Proteomic databases

    PRIDEi Q10WH6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG53398 ; ABG53398 ; Tery_4410 .
    GeneIDi 4246063.
    KEGGi ter:Tery_4410.
    PATRICi 23994367. VBITriEry99848_5586.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TERY203124:GJDR-4456-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: IMS101.

    Entry informationi

    Entry nameiRBL_TRIEI
    AccessioniPrimary (citable) accession number: Q10WH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 62 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