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A5FWR1

- RBL_ACICJ

UniProt

A5FWR1 - RBL_ACICJ

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Acidiphilium cryptum (strain JF-5)
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 (12 Jun 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 sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Active sitei184 – 1841Proton acceptorUniRule annotation
    Binding sitei186 – 1861SubstrateUniRule annotation
    Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
    Metal bindingi212 – 2121MagnesiumUniRule annotation
    Metal bindingi213 – 2131MagnesiumUniRule annotation
    Active sitei302 – 3021Proton acceptorUniRule annotation
    Binding sitei303 – 3031SubstrateUniRule annotation
    Binding sitei335 – 3351SubstrateUniRule annotation
    Sitei342 – 3421Transition state stabilizerUniRule annotation
    Binding sitei387 – 3871SubstrateUniRule 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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciACRY349163:GHET-836-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:Acry_0824
    OrganismiAcidiphilium cryptum (strain JF-5)
    Taxonomic identifieri349163 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
    ProteomesiUP000000245: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493Ribulose bisphosphate carboxylase large chainPRO_0000355747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi349163.Acry_0824.

    Structurei

    3D structure databases

    ProteinModelPortaliA5FWR1.
    SMRiA5FWR1. Positions 30-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    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.

    A5FWR1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR    50
    ITPQDGVDPV EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP 100
    NAPGQYFAYI AYDLALFEPG SIANLTASII GNVFGFKPLK ALRLEDMRLP 150
    VAYVKTFDGP ATGIVVERER LDKFGRPLLG ATVKPKLGLS GRNYGRVVYE 200
    ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA TGEVKGTYLN 250
    VTAGTMEDMY ERASFAHELG SSIIMIDLVI GYTAIQSMSK WARKHDMILH 300
    LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT 350
    RGFYDILRED YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH 400
    HLGEDVVLQF GGGTIGHPQG IAAGAMANRV ALEAMILARN EGRDYLAEGP 450
    QILNDAARHC LPLRQALDTW GEVTFNYAST DTPDFVPTAM PAY 493
    Length:493
    Mass (Da):54,797
    Last modified:June 12, 2007 - v1
    Checksum:i8794E5C4AC943AD6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000697 Genomic DNA. Translation: ABQ30043.1.
    RefSeqiYP_001233962.1. NC_009484.1.

    Genome annotation databases

    EnsemblBacteriaiABQ30043; ABQ30043; Acry_0824.
    GeneIDi5161365.
    KEGGiacr:Acry_0824.
    PATRICi20646630. VBIAciCry6074_1312.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000697 Genomic DNA. Translation: ABQ30043.1 .
    RefSeqi YP_001233962.1. NC_009484.1.

    3D structure databases

    ProteinModelPortali A5FWR1.
    SMRi A5FWR1. Positions 30-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349163.Acry_0824.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ30043 ; ABQ30043 ; Acry_0824 .
    GeneIDi 5161365.
    KEGGi acr:Acry_0824.
    PATRICi 20646630. VBIAciCry6074_1312.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ACRY349163:GHET-836-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: JF-5.

    Entry informationi

    Entry nameiRBL_ACICJ
    AccessioniPrimary (citable) accession number: A5FWR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: June 12, 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