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G2TF86

- G2TF86_RHORU

UniProt

G2TF86 - G2TF86_RHORU

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodospirillum rubrum F11
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 20 (01 Oct 2014)
      Sequence version 1 (16 Nov 2011)
      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

    LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciRRUB1036743:GLJ7-2504-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
    ORF Names:F11_12335Imported
    OrganismiRhodospirillum rubrum F11Imported
    Taxonomic identifieri1036743 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
    ProteomesiUP000001277: Chromosome

    PTM / Processingi

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliG2TF86.
    SMRiG2TF86. Positions 2-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    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.

    G2TF86-1 [UniParc]FASTAAdd to Basket

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    MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS    50
    TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF DRNITDGKAM 100
    IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL 150
    GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP 200
    FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET 250
    FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 300
    RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG 350
    PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI 400
    DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG 450
    WRKALGVEDT RSALPA 466
    Length:466
    Mass (Da):50,482
    Last modified:November 16, 2011 - v1
    Checksum:i4D9F800450AB0155
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003046 Genomic DNA. Translation: AEO48931.1.
    RefSeqiWP_011390153.1. NC_017584.1.
    YP_006048728.1. NC_017584.1.

    Genome annotation databases

    EnsemblBacteriaiAEO48931; AEO48931; F11_12335.
    GeneIDi12643578.
    KEGGirrf:F11_12335.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003046 Genomic DNA. Translation: AEO48931.1 .
    RefSeqi WP_011390153.1. NC_017584.1.
    YP_006048728.1. NC_017584.1.

    3D structure databases

    ProteinModelPortali G2TF86.
    SMRi G2TF86. Positions 2-460.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEO48931 ; AEO48931 ; F11_12335 .
    GeneIDi 12643578.
    KEGGi rrf:F11_12335.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci RRUB1036743:GLJ7-2504-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. "Identification of a New Gene Required for the Biosynthesis of Rhodoquinone in Rhodospirillum rubrum."
      Lonjers Z.T., Dickson E.L., Chu T.P., Kreutz J.E., Neacsu F.A., Anders K.R., Shepherd J.N.
      J. Bacteriol. 194:965-971(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: F11Imported.

    Entry informationi

    Entry nameiG2TF86_RHORU
    AccessioniPrimary (citable) accession number: G2TF86
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 16, 2011
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 20 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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 proteomeImported

    External Data

    Dasty 3