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E6VIT9

- E6VIT9_RHOPX

UniProt

E6VIT9 - E6VIT9_RHOPX

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodopseudomonas palustris (strain DX-1)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (08 Mar 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 sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Active sitei176 – 1761Proton acceptorUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Active sitei294 – 2941Proton acceptorUniRule annotation
    Binding sitei295 – 2951SubstrateUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Sitei334 – 3341Transition state stabilizerUniRule annotation
    Binding sitei379 – 3791SubstrateUniRule 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, PhotosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciRPAL652103:GHQR-4008-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:Rpdx1_3960Imported
    OrganismiRhodopseudomonas palustris (strain DX-1)Imported
    Taxonomic identifieri652103 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    ProteomesiUP000001402: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliE6VIT9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    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.

    E6VIT9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNETTTIRGK DRYKSGVMEY KKMGYWEPDY EPKDTDVIAL FRVTPQDGVD    50
    PIEAAAAVAG ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQYFA 100
    YIAYDLDLFE PGSISNLTAS IIGNVFGFKP LKALRLEDMR LPIAYVKTFQ 150
    GPATGIVVER ERMDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF 200
    TKDDENINSQ PFMHWRERFQ YCMEAVNKAQ AQTGEIKGTY LNVTAATMED 250
    MYERAEYAKE LGSIIVMIDL VIGYTAIQSM AKWARKNDMI LHLHRAGHST 300
    YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR 350
    EDFNPMALEN GLFFDQHWAS LNKLMPVASG GIHAGQMHQL LHLLGEDVVL 400
    QFGGGTIGHP MGIAAGATAN RVALEAMILA RNEGRDYLHE GPEILAKAAQ 450
    TCTPLKAALD TWKNVTFNYE STDTPDYAPT PSVSV 485
    Length:485
    Mass (Da):53,885
    Last modified:March 8, 2011 - v1
    Checksum:i29FD9930F05EBC20
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002418 Genomic DNA. Translation: ADU45516.1.
    RefSeqiWP_013503625.1. NC_014834.1.
    YP_004110249.1. NC_014834.1.

    Genome annotation databases

    EnsemblBacteriaiADU45516; ADU45516; Rpdx1_3960.
    GeneIDi10066193.
    KEGGirpx:Rpdx1_3960.
    PATRICi45348364. VBIRhoPal82507_4025.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002418 Genomic DNA. Translation: ADU45516.1 .
    RefSeqi WP_013503625.1. NC_014834.1.
    YP_004110249.1. NC_014834.1.

    3D structure databases

    ProteinModelPortali E6VIT9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADU45516 ; ADU45516 ; Rpdx1_3960 .
    GeneIDi 10066193.
    KEGGi rpx:Rpdx1_3960.
    PATRICi 45348364. VBIRhoPal82507_4025.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci RPAL652103:GHQR-4008-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 sequence of Rhodopseudomonas palustris DX-1."
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C., Woyke T.
      Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DX-1Imported.

    Entry informationi

    Entry nameiE6VIT9_RHOPX
    AccessioniPrimary (citable) accession number: E6VIT9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 8, 2011
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 22 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