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A4YNR1

- RBL1A_BRASO

UniProt

A4YNR1 - RBL1A_BRASO

Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

Organism
Bradyrhizobium sp. (strain ORS278)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (29 May 2007)
      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 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

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSP114615:GJN5-1579-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 1UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 1UniRule annotation
    Gene namesi
    Name:cbbL1UniRule annotation
    Ordered Locus Names:BRADO1659
    OrganismiBradyrhizobium sp. (strain ORS278)
    Taxonomic identifieri114615 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000001994: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chain 1PRO_0000299961Add
    BLAST

    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

    Protein-protein interaction databases

    STRINGi114615.BRADO1659.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YNR1.
    SMRiA4YNR1. Positions 13-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiLDYYLEC.
    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.

    A4YNR1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDQSITVRG KDRYKSGVME YKKMGYWEPS YQPNDTDVIA LFRVTPQDGV    50
    DPVEACAAVA GESSTATWTV VWTDRLTAAE KYRAKCYRVE PVPGSPGSYF 100
    AYIAYDLDLF EPGSIANLTA SIIGNVFGFK PLKALRLEDM RLPVAYVKTF 150
    QGPATGIVVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD 200
    FTKDDENINS QPFMHWRERF LYCMEAVNKA QAATGEIKGT YLNVTAATME 250
    DMYERAEFAK ELGSNIIMID LVIGYTAIQS MAKWSRKNDM ILHLHRAGHS 300
    TYTRQRAHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC 350
    REDFNPMRLE HGVFFDQHWA SLNKLMPVAS GGIHAGQMHQ LLDLLGEDVV 400
    LQFGGGTIGH PRGIAAGATA NRVALEAMIL ARNEGRDYVH EGPEILAKAA 450
    MTCTPLREAL EIWKDVTFNY ESTDSPDFVP TVTPAA 486
    Length:486
    Mass (Da):53,965
    Last modified:May 29, 2007 - v1
    Checksum:iD969770506D00683
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU234118 Genomic DNA. Translation: CAL75537.1.
    RefSeqiWP_011924765.1. NC_009445.1.
    YP_001203774.1. NC_009445.1.

    Genome annotation databases

    EnsemblBacteriaiCAL75537; CAL75537; BRADO1659.
    GeneIDi5115881.
    KEGGibra:BRADO1659.
    PATRICi21219543. VBIBraSp122330_1596.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU234118 Genomic DNA. Translation: CAL75537.1 .
    RefSeqi WP_011924765.1. NC_009445.1.
    YP_001203774.1. NC_009445.1.

    3D structure databases

    ProteinModelPortali A4YNR1.
    SMRi A4YNR1. Positions 13-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 114615.BRADO1659.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL75537 ; CAL75537 ; BRADO1659 .
    GeneIDi 5115881.
    KEGGi bra:BRADO1659.
    PATRICi 21219543. VBIBraSp122330_1596.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BSP114615:GJN5-1579-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: ORS278.

    Entry informationi

    Entry nameiRBL1A_BRASO
    AccessioniPrimary (citable) accession number: A4YNR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 47 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3