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A1VNQ9

- RBL2_POLNA

UniProt

A1VNQ9 - RBL2_POLNA

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Polaromonas naphthalenivorans (strain CJ2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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 sitei111 – 1111Substrate; in homodimeric partnerUniRule annotation
    Active sitei166 – 1661Proton acceptorUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
    Metal bindingi193 – 1931MagnesiumUniRule annotation
    Metal bindingi194 – 1941MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei321 – 3211SubstrateUniRule annotation
    Sitei329 – 3291Transition state stabilizerUniRule annotation
    Binding sitei368 – 3681SubstrateUniRule 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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciPNAP365044:GJ8X-2009-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:Pnap_1978
    OrganismiPolaromonas naphthalenivorans (strain CJ2)
    Taxonomic identifieri365044 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
    ProteomesiUP000000644: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_1000067649Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi365044.Pnap_1978.

    Structurei

    3D structure databases

    ProteinModelPortaliA1VNQ9.
    SMRiA1VNQ9. 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.

    A1VNQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSNRYADL SLKEEDLIAG GRHILVAYKM KPKAGHGYLE AAAHFAAESS    50
    TGTNVEVSTT DEFTKGVDAL VYLIDEATEE MRIAFPMDLF DRNILDGRMM 100
    IVSFLTLVIG NNQGMGDIQH AKIYDFFMPP RAIQLFDGPS KDISDMWRIL 150
    GRPVKDGGYI AGTIIKPKLG LRPEPFAQAA YQFWLGGDFI KNDEPQGNQT 200
    FAPMNKVMPL VHDAMKRAMD ETGEAKLFSA NITADDHYEM LARGDYILRT 250
    FGPDADKVAF LVDGYVGGPG MITTARRAFP NQYLHYHRAG HGAVTSPSAK 300
    RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGTHDDRAIA YIIERDSYTG 350
    PAYHQEWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGAYGHI 400
    DSPAAGATSL RQAYECWKAK ADPIEWAKEH PEFARAFASF PGDADMLFPG 450
    WRDKLASHR 459
    Length:459
    Mass (Da):50,571
    Last modified:February 6, 2007 - v1
    Checksum:i6FEEDE1CB0783D9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000529 Genomic DNA. Translation: ABM37287.1.
    RefSeqiYP_982208.1. NC_008781.1.

    Genome annotation databases

    EnsemblBacteriaiABM37287; ABM37287; Pnap_1978.
    GeneIDi4688038.
    KEGGipna:Pnap_1978.
    PATRICi22948612. VBIPolNap76733_2845.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000529 Genomic DNA. Translation: ABM37287.1 .
    RefSeqi YP_982208.1. NC_008781.1.

    3D structure databases

    ProteinModelPortali A1VNQ9.
    SMRi A1VNQ9. Positions 2-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 365044.Pnap_1978.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM37287 ; ABM37287 ; Pnap_1978 .
    GeneIDi 4688038.
    KEGGi pna:Pnap_1978.
    PATRICi 22948612. VBIPolNap76733_2845.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PNAP365044:GJ8X-2009-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: CJ2.

    Entry informationi

    Entry nameiRBL2_POLNA
    AccessioniPrimary (citable) accession number: A1VNQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 50 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3