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B5EQF7

- B5EQF7_ACIF5

UniProt

B5EQF7 - B5EQF7_ACIF5

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (14 Oct 2008)
      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

    LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciAFER380394:GHE0-2710-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:Lferr_2660Imported
    OrganismiAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))Imported
    Taxonomic identifieri380394 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
    ProteomesiUP000001856: Chromosome

    PTM / Processingi

    Amino acid modifications

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

    Proteomic databases

    PRIDEiB5EQF7.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi380394.Lferr_2660.

    Structurei

    3D structure databases

    ProteinModelPortaliB5EQF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiMETWKEV.
    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.

    B5EQF7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKTYNAGV KDYRNTYWEP DYSVKDTDIL AVFKITPQAG VDREEAAAAV    50
    AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFIAYPIDL 100
    FEEGSVVNVF TSLVGNVFGF KAVRALRLED VRFPIAYVKT CGGPPHGIQV 150
    ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR ACYEGLRGGL DFTKDDENVN 200
    SQPFMRWRQR FDFVMEAIQK AEAETGERKG HYLNVTAPTP EEMYKRAEYA 250
    KEIGAPIIMH DYITGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH 300
    GIHFRVLTKI LRLSGGDHLH SGTVVGKLEG DREATLGWID IMRDRFIKED 350
    RSRGIFFDQD WGSMPGVMPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL 400
    GHPWGNAAGA AANRVALEAC VEARNRGVAI EKEGKAVLTE AAKHSPELKI 450
    AMETWKEIKF EFDTVDKLDV AHK 473
    Length:473
    Mass (Da):52,702
    Last modified:October 14, 2008 - v1
    Checksum:iD95289292292471A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001132 Genomic DNA. Translation: ACH84854.1.
    RefSeqiYP_002221061.1. NC_011206.1.

    Genome annotation databases

    EnsemblBacteriaiACH84854; ACH84854; Lferr_2660.
    GeneIDi6878659.
    KEGGiafe:Lferr_2660.
    PATRICi20662910. VBIAciFer6930_2636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001132 Genomic DNA. Translation: ACH84854.1 .
    RefSeqi YP_002221061.1. NC_011206.1.

    3D structure databases

    ProteinModelPortali B5EQF7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 380394.Lferr_2660.

    Proteomic databases

    PRIDEi B5EQF7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH84854 ; ACH84854 ; Lferr_2660 .
    GeneIDi 6878659.
    KEGGi afe:Lferr_2660.
    PATRICi 20662910. VBIAciFer6930_2636.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci AFER380394:GHE0-2710-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. "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 53993Imported.

    Entry informationi

    Entry nameiB5EQF7_ACIF5
    AccessioniPrimary (citable) accession number: B5EQF7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 14, 2008
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 40 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 proteomeImported

    External Data

    Dasty 3