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F9ZLP0

- F9ZLP0_ACICS

UniProt

F9ZLP0 - F9ZLP0_ACICS

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Acidithiobacillus caldus (strain SM-1)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 17 (01 Oct 2014)
      Sequence version 1 (19 Oct 2011)
      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 sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei286 – 2861Proton acceptorUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei326 – 3261Transition state stabilizerUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule 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 annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciACAL990288:GJBS-941-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:Atc_0926Imported
    OrganismiAcidithiobacillus caldus (strain SM-1)Imported
    Taxonomic identifieri990288 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
    ProteomesiUP000006135: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliF9ZLP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    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.

    F9ZLP0-1 [UniParc]FASTAAdd to Basket

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    MAGKYEAGVK EYRHTYWAPD YVPLDSDILA CFKIVPQPGV DREEAAAAVA    50
    AESSTGTWTT VWTDLLTDMD YYKGRAYRIE DVPGDDTAFY AFIAYPIDLF 100
    EEGSVVNVFT SLVGNVFGFK AVRSLRLEDV RFPLHYVMTC NGPAHGIQVE 150
    RDKMDKYGRP LLGCTIKPKL GLSAKNYGRA VYEALRGGLD FTKDDENVNS 200
    QPFMRWRDRF LFVADAIRNA EAQTGERKGH YLNVTAPSPE EMYERAEFAK 250
    ELGMPIIMHD FLTGGFCANT GLARWCRKNG VLLHIHRAMH AVIDRNPHHG 300
    IHFRVLTKAL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIPEDR 350
    SRGIFFDQDW GSMPGAFAVA SGGIHVWHMP ALVNIFGDDS VLQFGGGTLG 400
    HPWGNAAGAA ANRVALEACV EARNRGVEIE KEGKEVLMNA ARHSPELKIA 450
    LETWKEIKFE FDTVDKLDVQ NR 472
    Length:472
    Mass (Da):52,672
    Last modified:October 19, 2011 - v1
    Checksum:i6B35F9C6839946EE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002573 Genomic DNA. Translation: AEK57575.1.
    RefSeqiYP_004748275.1. NC_015850.1.

    Genome annotation databases

    EnsemblBacteriaiAEK57575; AEK57575; Atc_0926.
    GeneIDi10988712.
    KEGGiacu:Atc_0926.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002573 Genomic DNA. Translation: AEK57575.1 .
    RefSeqi YP_004748275.1. NC_015850.1.

    3D structure databases

    ProteinModelPortali F9ZLP0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEK57575 ; AEK57575 ; Atc_0926 .
    GeneIDi 10988712.
    KEGGi acu:Atc_0926.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci ACAL990288:GJBS-941-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. "Unraveling the Acidithiobacillus caldus complete genome and its central metabolisms for carbon assimilation."
      You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.
      J. Genet. Genomics 38:243-252(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SM-1Imported.

    Entry informationi

    Entry nameiF9ZLP0_ACICS
    AccessioniPrimary (citable) accession number: F9ZLP0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 17 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 proteome, Reference proteomeImported

    External Data

    Dasty 3