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B3QB68

- RBL2_RHOPT

UniProt

B3QB68 - RBL2_RHOPT

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodopseudomonas palustris (strain TIE-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (02 Sep 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. 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 sitei112 – 1121Substrate; in homodimeric partnerUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi192 – 1921Magnesium; via carbamate groupUniRule annotation
    Metal bindingi194 – 1941MagnesiumUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Active sitei288 – 2881Proton acceptorUniRule annotation
    Binding sitei289 – 2891SubstrateUniRule annotation
    Binding sitei322 – 3221SubstrateUniRule annotation
    Sitei330 – 3301Transition state stabilizerUniRule annotation
    Binding sitei369 – 3691SubstrateUniRule 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. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciRPAL395960:GHPC-5175-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:cbbMUniRule annotation
    Ordered Locus Names:Rpal_5122
    OrganismiRhodopseudomonas palustris (strain TIE-1)
    Taxonomic identifieri395960 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    ProteomesiUP000001725: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Ribulose bisphosphate carboxylasePRO_1000142754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei192 – 1921N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi395960.Rpal_5122.

    Structurei

    3D structure databases

    ProteinModelPortaliB3QB68.
    SMRiB3QB68. Positions 2-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiAKEHREF.
    OrthoDBiEOG66QKT8.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01339. RuBisCO_L_type2.
    InterProiIPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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.

    B3QB68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSNRYANL NLKESELIAG GRHVLCAYIM KPKAGFGNFI QTAAHFAAES    50
    STGTNVEVST TDDFTRGVDA LVYEVDEANS LMKIAYPIEL FDRNVIDGRA 100
    MIASFLTLTI GNNQGMGDVE YAKMYDFYVP PAYLKLFDGP STTIKDLWRV 150
    LGRPVINGGF IVGTIIKPKL GLRPQPFANA CYDFWLGGDF IKNDEPQGNQ 200
    VFAPFKDTVR AVADAMRRAQ DKTGEAKLFS FNITADDHYE MLARGEFILE 250
    TFADNADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 300
    KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAI AYMITEDAAD 350
    GPYFHQEWLG MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH 400
    VDGGAAGAKS LRQAEQCWKQ GADPVEFAKD HREFARAFES FPQDADKLYP 450
    NWRAKLKPQA A 461
    Length:461
    Mass (Da):50,485
    Last modified:September 2, 2008 - v1
    Checksum:i907EFB041943AABC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001096 Genomic DNA. Translation: ACF03611.1.
    RefSeqiYP_001994086.1. NC_011004.1.

    Genome annotation databases

    EnsemblBacteriaiACF03611; ACF03611; Rpal_5122.
    GeneIDi6412816.
    KEGGirpt:Rpal_5122.
    PATRICi23314835. VBIRhoPal88240_5197.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001096 Genomic DNA. Translation: ACF03611.1 .
    RefSeqi YP_001994086.1. NC_011004.1.

    3D structure databases

    ProteinModelPortali B3QB68.
    SMRi B3QB68. Positions 2-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 395960.Rpal_5122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACF03611 ; ACF03611 ; Rpal_5122 .
    GeneIDi 6412816.
    KEGGi rpt:Rpal_5122.
    PATRICi 23314835. VBIRhoPal88240_5197.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi AKEHREF.
    OrthoDBi EOG66QKT8.

    Enzyme and pathway databases

    BioCyci RPAL395960:GHPC-5175-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01339. RuBisCO_L_type2.
    InterProi IPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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: TIE-1.

    Entry informationi

    Entry nameiRBL2_RHOPT
    AccessioniPrimary (citable) accession number: B3QB68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 38 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3