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G8MDQ6

- G8MDQ6_9BURK

UniProt

G8MDQ6 - G8MDQ6_9BURK

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Burkholderia sp. YI23
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (22 Feb 2012)
      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 sitei136 – 1361Substrate; in homodimeric partnerUniRule annotation
    Binding sitei186 – 1861SubstrateUniRule annotation
    Active sitei188 – 1881Proton acceptorUniRule annotation
    Binding sitei190 – 1901SubstrateUniRule annotation
    Metal bindingi214 – 2141Magnesium; via carbamate groupUniRule annotation
    Metal bindingi216 – 2161MagnesiumUniRule annotation
    Metal bindingi217 – 2171MagnesiumUniRule annotation
    Active sitei306 – 3061Proton acceptorUniRule annotation
    Binding sitei307 – 3071SubstrateUniRule annotation
    Binding sitei339 – 3391SubstrateUniRule annotation
    Sitei346 – 3461Transition state stabilizerUniRule annotation
    Binding sitei391 – 3911SubstrateUniRule 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 annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciBSP1097668:GKEO-5926-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunitUniRule annotation
    Gene namesi
    Name:cbbLUniRule annotation
    ORF Names:BYI23_B014300Imported
    OrganismiBurkholderia sp. YI23Imported
    Taxonomic identifieri1097668 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
    ProteomesiUP000006801: Chromosome 2

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei214 – 2141N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    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.

    G8MDQ6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDFSKAAVE AARNPSDPRS RYAAGVMKYR EMGYWQPDYT PKDTDVIALF    50
    RITPQAGVEP EEAAAAVAGE SSTATWTVVW TDRLTACDMY RAKAYRVDPV 100
    PNQRADEPQY FAYIAYELDL FEEGSVANLT ASIIGNVFGF KPLKALRLED 150
    MRIPVAYLKT FQGPPTGIIV ERERLDKYGR PLLGATVKPK LGLSGKNYGR 200
    VVYEGLKGGL DFLKDDENIN SQAFMHWRDR YLFAMEAVSR AQAETGEVKG 250
    HYLNVTAGTM EDMYERAEFA KELGSCIVMI DLVIGWTAIQ SMSKWARRND 300
    MILHLHRAGH GTYTRQRNHG ISFRVIAKWL RMAGVDHAHA GTAVGKLEGD 350
    PLSVQGYYNV CREARNEPDL SRGIFFDQPW AGLRKVMPVA SGGIHAGQMH 400
    QLLDLFGDDC ILQFGGGTIG HPQGIQAGAT ANRVALEAMV KARNEGRDIV 450
    NEGLDVLDAA ARFCTPLKLA LDTWRDVTFN YASTDTPDFA VTPSVAV 497
    Length:497
    Mass (Da):55,048
    Last modified:February 22, 2012 - v1
    Checksum:i370A0F2ADDB00C72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003088 Genomic DNA. Translation: AET92037.1.
    RefSeqiWP_014251670.1. NC_016625.1.
    YP_005042924.1. NC_016625.1.

    Genome annotation databases

    EnsemblBacteriaiAET92037; AET92037; BYI23_B014300.
    GeneIDi11558245.
    KEGGibyi:BYI23_B014300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003088 Genomic DNA. Translation: AET92037.1 .
    RefSeqi WP_014251670.1. NC_016625.1.
    YP_005042924.1. NC_016625.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AET92037 ; AET92037 ; BYI23_B014300 .
    GeneIDi 11558245.
    KEGGi byi:BYI23_B014300.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci BSP1097668:GKEO-5926-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi IPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    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 Genome Sequence of the Fenitrothion-Degrading Burkholderia sp. Strain YI23."
      Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y., Ka J.O.
      J. Bacteriol. 194:896-896(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: YI23Imported.

    Entry informationi

    Entry nameiG8MDQ6_9BURK
    AccessioniPrimary (citable) accession number: G8MDQ6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 22, 2012
    Last sequence update: February 22, 2012
    Last modified: October 1, 2014
    This is version 18 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 form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel".UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3