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Q479W5

- RBL2_DECAR

UniProt

Q479W5 - RBL2_DECAR

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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

    BioCyciDARO159087:GI5B-3713-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:Daro_3637
    OrganismiDechloromonas aromatica (strain RCB)
    Taxonomic identifieri159087 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
    ProteomesiUP000000550: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_0000251406Add
    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

    STRINGi159087.Daro_3637.

    Structurei

    3D structure databases

    ProteinModelPortaliQ479W5.
    SMRiQ479W5. Positions 2-455.
    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.

    Q479W5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSNRYADL SLTEAELIAG GQHILCAYKM KPKAGHRYLE AAAHFAAESS    50
    TGTNVEVCTT DEFTKGVDAL VYHIDEASED MRIAYPLDLF DRNMTDGRMM 100
    MASFLTLTIG NNQGMGDIEH AKMVDFYVPR RGIELFDGPS KDISDLWRML 150
    GRPVKDGGYI AGTIIKPKLG LRPEPFARAA YEFWLGGDFI KNDEPQGNQV 200
    FAPLKKVIPL VYDSMKRAMD ETGEAKLFSM NITADDHFEM CARADFALEA 250
    FGPDADKLAF LVDGYVGGPG MITTARRQYP NQYLHYHRAG HGAVTSPSSK 300
    RGYTAYVLAK MSRLQGASGI HVGTMGYGKM EGDKDDRACA YIIERDSYTG 350
    PVYHQEWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGAYGHI 400
    DSPAAGARSL RQAYDCWKAG ADPVEWARDH YEFARAFESF PQDADQLYPG 450
    WRHKLRPAA 459
    Length:459
    Mass (Da):50,788
    Last modified:September 13, 2005 - v1
    Checksum:i813D3C3753EE1C0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ48366.1.
    RefSeqiYP_286836.1. NC_007298.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ48366; AAZ48366; Daro_3637.
    GeneIDi3568282.
    KEGGidar:Daro_3637.
    PATRICi21605954. VBIDecAro89105_3619.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000089 Genomic DNA. Translation: AAZ48366.1 .
    RefSeqi YP_286836.1. NC_007298.1.

    3D structure databases

    ProteinModelPortali Q479W5.
    SMRi Q479W5. Positions 2-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 159087.Daro_3637.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ48366 ; AAZ48366 ; Daro_3637 .
    GeneIDi 3568282.
    KEGGi dar:Daro_3637.
    PATRICi 21605954. VBIDecAro89105_3619.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DARO159087:GI5B-3713-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
      Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
      BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RCB.

    Entry informationi

    Entry nameiRBL2_DECAR
    AccessioniPrimary (citable) accession number: Q479W5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 58 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