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E1TEV1

- E1TEV1_BURSG

UniProt

E1TEV1 - E1TEV1_BURSG

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Burkholderia sp. (strain CCGE1003)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (30 Nov 2010)
      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 sitei139 – 1391Substrate; in homodimeric partnerUniRule annotation
    Binding sitei189 – 1891SubstrateUniRule annotation
    Active sitei191 – 1911Proton acceptorUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Metal bindingi217 – 2171Magnesium; via carbamate groupUniRule annotation
    Metal bindingi219 – 2191MagnesiumUniRule annotation
    Metal bindingi220 – 2201MagnesiumUniRule annotation
    Active sitei309 – 3091Proton acceptorUniRule annotation
    Binding sitei310 – 3101SubstrateUniRule annotation
    Binding sitei342 – 3421SubstrateUniRule annotation
    Sitei349 – 3491Transition state stabilizerUniRule annotation
    Binding sitei394 – 3941SubstrateUniRule 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

    BioCyciBSP640512:GBXV-5514-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
    Ordered Locus Names:BC1003_5439Imported
    OrganismiBurkholderia sp. (strain CCGE1003)Imported
    Taxonomic identifieri640512 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
    ProteomesiUP000001550: Chromosome 2

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei217 – 2171N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliE1TEV1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.

    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.

    E1TEV1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDFSQPAIE SLHKPRNAGN PRERYAAGVM KYREMGYWQP DYTPKDTDVI    50
    ALFRITPQPG VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV 100
    DPVPASSASE PQYFAYIAYE LDLFEEGSVA NLTASIIGNV FGFKPLKALR 150
    LEDMRIPVAY LKTFQGPPTG IVVERERLDK YGRPLLGATV KPKLGLSGKN 200
    YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFSMEA VNRAQAETGE 250
    VKGHYLNVTA GTMEDMYERA EFARELGSCI VMIDLVVGWT AIQSMGRWAR 300
    KNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL 350
    EGDPLTVQGF YNVCREARNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG 400
    QMHQLLDLFG DDAILQFGGG TIGHPGGIQA GAVANRVALE AMVKARNEGR 450
    DIREEGPDIL EAAARWCGPL KQALDTWRDV TFNYASTDSP DFAATPTAA 499
    Length:499
    Mass (Da):55,227
    Last modified:November 30, 2010 - v1
    Checksum:i4C25DD925848040E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002218 Genomic DNA. Translation: ADN61357.1.
    RefSeqiWP_013342882.1. NC_014540.1.
    YP_003910648.1. NC_014540.1.

    Genome annotation databases

    EnsemblBacteriaiADN61357; ADN61357; BC1003_5439.
    GeneIDi9764153.
    KEGGibgf:BC1003_5439.
    PATRICi42217762. VBIBurSp98639_5838.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002218 Genomic DNA. Translation: ADN61357.1 .
    RefSeqi WP_013342882.1. NC_014540.1.
    YP_003910648.1. NC_014540.1.

    3D structure databases

    ProteinModelPortali E1TEV1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADN61357 ; ADN61357 ; BC1003_5439 .
    GeneIDi 9764153.
    KEGGi bgf:BC1003_5439.
    PATRICi 42217762. VBIBurSp98639_5838.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci BSP640512:GBXV-5514-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CCGE1003Imported.

    Entry informationi

    Entry nameiE1TEV1_BURSG
    AccessioniPrimary (citable) accession number: E1TEV1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 30, 2010
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 28 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 proteomeImported

    External Data

    Dasty 3