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B5IH56

- B5IH56_ACIB4

UniProt

B5IH56 - B5IH56_ACIB4

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Aciduliprofundum boonei (strain DSM 19572 / T469)
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

    Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.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
    Active sitei149 – 1491Proton acceptorUniRule annotation
    Binding sitei151 – 1511SubstrateUniRule annotation
    Metal bindingi175 – 1751Magnesium; via carbamate groupUniRule annotation
    Metal bindingi177 – 1771MagnesiumUniRule annotation
    Metal bindingi178 – 1781MagnesiumUniRule annotation
    Active sitei265 – 2651Proton acceptorUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule annotation
    Binding sitei298 – 2981SubstrateUniRule annotation
    Sitei305 – 3051Transition state stabilizerUniRule annotation

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. AMP catabolic process Source: UniProtKB-HAMAP
    2. carbon fixation Source: InterPro

    Keywords - Molecular functioni

    LyaseUniRule annotationImported, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciABOO439481:GJNL-1119-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:rbcLUniRule annotation
    Ordered Locus Names:Aboo_1084Imported
    ORF Names:ABOONEI_952Imported
    OrganismiAciduliprofundum boonei (strain DSM 19572 / T469)Imported
    Taxonomic identifieri439481 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaAciduliprofundum
    ProteomesiUP000001400: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei175 – 1751N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliB5IH56.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni347 – 3493Substrate bindingUniRule annotation
    Regioni369 – 3724Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProiIPR017712. RuBisCO_III.
    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.
    TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B5IH56-1 [UniParc]FASTAAdd to Basket

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    MTYIDLNYQP RESDLLVWFR AEPPAGKDMK YVADRIAEES SIGTWTDLKT    50
    LLPEIWEKLR ARVYEIDEKN KYVKIAYPLH LFEIKNMPAI LASVAGNVFG 100
    MKSVEALRVL DIRFPKELIQ GYLGPKYGVQ GVREMTKVYD RPFLGTIIKP 150
    KIGLPAKMHA EVAYEAWVGG LDIVKDDENL ASQEFNRFEE RLALTLEKKD 200
    IAEEETGEKK IYLVNITAPY KEMIRRAELV QDSGNEFVMI DVFISGFSAV 250
    QSYREEGFKM AIHAHRAMHA AITRNPEHGI NMLTLAKVYR LLGVDNLHIG 300
    TAVGKMEGSA KEVSEIREEI QLENVPANES RFEQKWYEIK PVLAVASGGL 350
    HPGHVPAVVD ILGKDIVIQA GGGVHGHPEG TRAGAKAMRE ALEAKMQGIP 400
    LEEYAKEHKE LREALEKFLH 420
    Length:420
    Mass (Da):47,364
    Last modified:October 14, 2008 - v1
    Checksum:iC8667540053F3B77
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001941 Genomic DNA. Translation: ADD08893.1.
    DS990535 Genomic DNA. Translation: EDY34409.1.
    RefSeqiWP_008086508.1. NZ_DS990535.1.
    YP_003483455.1. NC_013926.1.

    Genome annotation databases

    EnsemblBacteriaiADD08893; ADD08893; Aboo_1084.
    EDY34409; EDY34409; ABOONEI_952.
    GeneIDi8828042.
    KEGGiabi:Aboo_1084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001941 Genomic DNA. Translation: ADD08893.1 .
    DS990535 Genomic DNA. Translation: EDY34409.1 .
    RefSeqi WP_008086508.1. NZ_DS990535.1.
    YP_003483455.1. NC_013926.1.

    3D structure databases

    ProteinModelPortali B5IH56.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADD08893 ; ADD08893 ; Aboo_1084 .
    EDY34409 ; EDY34409 ; ABOONEI_952 .
    GeneIDi 8828042.
    KEGGi abi:Aboo_1084.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci ABOO439481:GJNL-1119-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProi IPR017712. RuBisCO_III.
    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.
    TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Electron microscopy encounters with unusual thermophiles helps direct genomic analysis of Aciduliprofundum boonei."
      Reysenbach A.L., Flores G.E.
      Geobiology 6:331-336(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: T469Imported.
    2. "Complete sequence of Aciduliprofundum boonei T469."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.
      Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: T469Imported.
    3. "Complete sequence of Aciduliprofundum boonei T469."
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.
      Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 19572 / T469Imported.

    Entry informationi

    Entry nameiB5IH56_ACIB4
    AccessioniPrimary (citable) accession number: B5IH56
    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

    Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3