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A4YQD3

- RBL1B_BRASO

UniProt

A4YQD3 - RBL1B_BRASO

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Bradyrhizobium sp. (strain ORS278)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (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 sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Metal bindingi197 – 1971MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei327 – 3271Transition state stabilizerUniRule annotation
    Binding sitei372 – 3721SubstrateUniRule 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:GJN5-2154-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:BRADO2274
    OrganismiBradyrhizobium sp. (strain ORS278)
    Taxonomic identifieri114615 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000001994: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 479479Ribulose bisphosphate carboxylase large chain 2PRO_0000299962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiA4YQD3.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi114615.BRADO2274.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YQD3.
    SMRiA4YQD3. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiMSIFKGV.
    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.

    A4YQD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKSYQAGV KEYRKTYWTP EYVPLDTDLL AVFKIVAQAG VPREEAAAAV    50
    AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL 100
    FEEGSVVNVL TSLVGNVFGF KAVRSLRLED IRFPLAYVKT CGGPPNGIQL 150
    ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN 200
    SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP EEMYKRAEFA 250
    KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH 300
    GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN 350
    RARGIFFDQD WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL 400
    GHPWGNAAGA HANRVALEAC VEARNQGRPV EREGREILTE AAQHSPELKI 450
    AMETWKEIKF EFDVVDKLDT GPMLRVVNA 479
    Length:479
    Mass (Da):53,334
    Last modified:May 29, 2007 - v1
    Checksum:i7518D7CC0AE30D6C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU234118 Genomic DNA. Translation: CAL76109.1.
    RefSeqiWP_011925328.1. NC_009445.1.
    YP_001204346.1. NC_009445.1.

    Genome annotation databases

    EnsemblBacteriaiCAL76109; CAL76109; BRADO2274.
    GeneIDi5115889.
    KEGGibra:BRADO2274.
    PATRICi21220737. VBIBraSp122330_2191.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU234118 Genomic DNA. Translation: CAL76109.1 .
    RefSeqi WP_011925328.1. NC_009445.1.
    YP_001204346.1. NC_009445.1.

    3D structure databases

    ProteinModelPortali A4YQD3.
    SMRi A4YQD3. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 114615.BRADO2274.

    Proteomic databases

    PRIDEi A4YQD3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL76109 ; CAL76109 ; BRADO2274 .
    GeneIDi 5115889.
    KEGGi bra:BRADO2274.
    PATRICi 21220737. VBIBraSp122330_2191.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BSP114615:GJN5-2154-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 nameiRBL1B_BRASO
    AccessioniPrimary (citable) accession number: A4YQD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 46 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