Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

E3I482

- E3I482_RHOVT

UniProt

E3I482 - E3I482_RHOVT

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 20 (01 Oct 2014)
      Sequence version 1 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei125 – 1251Substrate; in homodimeric partnerUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Active sitei177 – 1771Proton acceptorUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule annotation
    Metal bindingi203 – 2031Magnesium; via carbamate groupUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Metal bindingi206 – 2061MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule 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

    BioCyciRVAN648757:GHZT-10-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:Rvan_0010Imported
    OrganismiRhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299)Imported
    Taxonomic identifieri648757 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeRhodomicrobium
    ProteomesiUP000001399: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliE3I482.
    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.

    E3I482-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDKSETVKG EDRYKAGVMS YKKMGYWEPD YQPKETDLIA LFRVTPQDGV    50
    DPIEASAAVA GESSTATWTV VWTDRLTASE KYRAKCYRVD PVPNAPGSYF 100
    AYIAYDLDLF EGGSISNLTA SIIGNVFGFK PLKALRLEDM RLPVAYVKTF 150
    DGPPAGIIVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD 200
    FTKDDENINS QPFMHWRERF LYCMEAVNKA QAETGEIKGS YLNITAGTME 250
    EMYKRAEYAK ELGSCIVMID LVIGYVAIQS ISKWARDNNM LLHLHRAGHS 300
    TYTRQKSHGV SFRVISKWMR LAGVDHIHAG TVVGKLEGDP LTTAGYYDIL 350
    REDFVPQNLE HGVFFDQPWA SLGKVMPVAS GGIHAGQMHQ LIHYLGEDVV 400
    LQFGGGTIGH PYGIQAGATA NRVALEAMIF ARNEGRDYLA EGPQILKDAA 450
    KTCTPLRQAL DTWGDVTFDY TSTDTPDFVP TPTAS 485
    Length:485
    Mass (Da):53,687
    Last modified:January 11, 2011 - v1
    Checksum:iCACE029CBD3E6F4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002292 Genomic DNA. Translation: ADP69301.1.
    RefSeqiYP_004010400.1. NC_014664.1.

    Genome annotation databases

    EnsemblBacteriaiADP69301; ADP69301; Rvan_0010.
    GeneIDi9930774.
    KEGGirva:Rvan_0010.
    PATRICi42667006. VBIRhoVan113057_0010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002292 Genomic DNA. Translation: ADP69301.1 .
    RefSeqi YP_004010400.1. NC_014664.1.

    3D structure databases

    ProteinModelPortali E3I482.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADP69301 ; ADP69301 ; Rvan_0010 .
    GeneIDi 9930774.
    KEGGi rva:Rvan_0010.
    PATRICi 42667006. VBIRhoVan113057_0010.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci RVAN648757:GHZT-10-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: ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299Imported.

    Entry informationi

    Entry nameiE3I482_RHOVT
    AccessioniPrimary (citable) accession number: E3I482
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 11, 2011
    Last sequence update: January 11, 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 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