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Q21YM9

- RBL2_ALBFT

UniProt

Q21YM9 - RBL2_ALBFT

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (18 Apr 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. 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

    BioCyciAFER338969:GHU9-1397-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:Rfer_1391
    OrganismiAlbidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens)
    Taxonomic identifieri338969 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax
    ProteomesiUP000008332: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_0000251408Add
    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

    STRINGi338969.Rfer_1391.

    Structurei

    3D structure databases

    ProteinModelPortaliQ21YM9.
    SMRiQ21YM9. Positions 2-457.
    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.

    Q21YM9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSKRYADL SLQEAALIAG GQHILCAYKM APKDGLNYLE AAAHFAAESS    50
    TGTNVEVCTT DDFTRDVDAL VYYVNEATED MRIAYPLALF DRNITDGRFM 100
    LVSFLTLAVG NNQGMGDIKH AKMIDFYVPE RVIQMFDGPA KDISDLWRIL 150
    GRPVKDGGFI VGTIIKPKLG LRPEPFAQAA YQFWLGGDFI KNDEPQGNQV 200
    FSPIKKTLPL VYDALKRAQD ETGQAKLFSM NITADDHFEM CARADFALET 250
    FGADADKLAF LVDGFVGGPG MVTTARRQYP NQYLHYHRGG HGMVTSPSSK 300
    RGYTALVLAK MSRLQGASGI HVGTMGHGKM EGAGDDRVMA YMIERDECQG 350
    PVYFQKWYGI KPTTPIVSGG MNALRLPGFF DNLGHGNIIN TAGGGSYGHL 400
    DSPAAGAVSL RQAYECWKAG ADPIEWAKEH REFARAFESF PQDADRLFAG 450
    WRDKLGVGA 459
    Length:459
    Mass (Da):50,391
    Last modified:April 18, 2006 - v1
    Checksum:i089F31E7B2FF938D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000267 Genomic DNA. Translation: ABD69124.1.
    RefSeqiYP_522655.1. NC_007908.1.

    Genome annotation databases

    EnsemblBacteriaiABD69124; ABD69124; Rfer_1391.
    GeneIDi3960215.
    KEGGirfr:Rfer_1391.
    PATRICi23235349. VBIRhoFer131161_1696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000267 Genomic DNA. Translation: ABD69124.1 .
    RefSeqi YP_522655.1. NC_007908.1.

    3D structure databases

    ProteinModelPortali Q21YM9.
    SMRi Q21YM9. Positions 2-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338969.Rfer_1391.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD69124 ; ABD69124 ; Rfer_1391 .
    GeneIDi 3960215.
    KEGGi rfr:Rfer_1391.
    PATRICi 23235349. VBIRhoFer131161_1696.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci AFER338969:GHU9-1397-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. "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.
      , Kyrpides N., Ivanova N., Richardson P.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-621 / DSM 15236 / T118.

    Entry informationi

    Entry nameiRBL2_ALBFT
    AccessioniPrimary (citable) accession number: Q21YM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 57 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