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Q37G91

- RBL1B_RHOPS

UniProt

Q37G91 - RBL1B_RHOPS

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Rhodopseudomonas palustris (strain BisB5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      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

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciRPAL316057:GHDC-3784-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 2UniRule annotation
    Gene namesi
    Name:cbbL2UniRule annotation
    Ordered Locus Names:RPD_3722
    OrganismiRhodopseudomonas palustris (strain BisB5)
    Taxonomic identifieri316057 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    ProteomesiUP000001818: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Ribulose bisphosphate carboxylase large chain 2PRO_0000251459Add
    BLAST

    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

    Protein-protein interaction databases

    STRINGi316057.RPD_3722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ37G91.
    SMRiQ37G91. Positions 22-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiCTPLKQA.
    OrthoDBiEOG6ZKXMS.

    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.

    Q37G91-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDSITVRGK DRYKSGVMEY KKMGYWEPDY VPKDTDVIAL FRVTPQDGVD    50
    PIEASAAVAG ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQYFA 100
    YIAYDLDLFE NGSIANLSAS IIGNVFGFKP LKALRLEDMR LPIAYVKTFQ 150
    GPATGIVVER ERMDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF 200
    TKDDENINSQ PFMHWRERFL YCMEAVNKAQ AASGEIKGTY LNVTAGTMEE 250
    MYERAEFAKQ LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST 300
    YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPS TTKGYYDICR 350
    EDYNPANLEH GLFFDQPWAS LNKLMPVASG GIHAGQMHQL LDLLGEDVVL 400
    QFGGGTIGHP MGIAAGATAN RVALEAMILA RNEGRDYVHE GPEILAKAAQ 450
    TCTPLKAALD TWKNVSFNYE STDTPDYAPT PSVSM 485
    Length:485
    Mass (Da):53,733
    Last modified:December 6, 2005 - v1
    Checksum:i6667A5C476EA33F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000283 Genomic DNA. Translation: ABE40943.1.
    RefSeqiWP_011504108.1. NC_007958.1.
    YP_570844.1. NC_007958.1.

    Genome annotation databases

    EnsemblBacteriaiABE40943; ABE40943; RPD_3722.
    GeneIDi4024238.
    KEGGirpd:RPD_3722.
    PATRICi23282605. VBIRhoPal120395_3856.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000283 Genomic DNA. Translation: ABE40943.1 .
    RefSeqi WP_011504108.1. NC_007958.1.
    YP_570844.1. NC_007958.1.

    3D structure databases

    ProteinModelPortali Q37G91.
    SMRi Q37G91. Positions 22-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 316057.RPD_3722.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE40943 ; ABE40943 ; RPD_3722 .
    GeneIDi 4024238.
    KEGGi rpd:RPD_3722.
    PATRICi 23282605. VBIRhoPal120395_3856.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi CTPLKQA.
    OrthoDBi EOG6ZKXMS.

    Enzyme and pathway databases

    BioCyci RPAL316057:GHDC-3784-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: BisB5.

    Entry informationi

    Entry nameiRBL1B_RHOPS
    AccessioniPrimary (citable) accession number: Q37G91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3