Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

D7D9Q5

- D7D9Q5_STAHD

UniProt

D7D9Q5 - D7D9Q5_STAHD

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (10 Aug 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei162 – 1621Proton acceptorUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Metal bindingi188 – 1881Magnesium; via carbamate groupUniRule annotation
    Metal bindingi190 – 1901MagnesiumUniRule annotation
    Metal bindingi191 – 1911MagnesiumUniRule annotation
    Active sitei280 – 2801Proton acceptorUniRule annotation
    Binding sitei281 – 2811SubstrateUniRule annotation
    Binding sitei313 – 3131SubstrateUniRule annotation
    Sitei321 – 3211Transition state stabilizerUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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

    BioCyciSHEL591019:GC4A-1449-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:Shell_1412Imported
    OrganismiStaphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8)Imported
    Taxonomic identifieri591019 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus
    ProteomesiUP000002573: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei188 – 1881N6-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

    ProteinModelPortaliD7D9Q5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni366 – 3683Substrate bindingUniRule annotation
    Regioni388 – 3914Substrate bindingUniRule annotation

    Sequence similaritiesi

    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.
    HAMAPiMF_01133. RuBisCO_L_type3.
    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.

    D7D9Q5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHTFEPYHS YVDKNYVPDP DNDIIAVFRI KPAKGFTIED AAGGVAAESS    50
    TGTWTTLYPW YDTERVRKLS GKAYYFKDLG DGSWIVRIAY PAELFEEANM 100
    PGLLASIAGN VFGMKRVEGL RLEDIYLPKK FLQYFKGPSK GVDGVRKIFG 150
    INDRPIVGTV PKPKVGYSPE EVEKLAYELL VGGIDYIKDD ENMTSPSFCR 200
    FSERAKHIMR AIDRAEKETG ERKVWFANIT SDIREMEKRL KLVADYGNPY 250
    VMVDVVVTGW SALTYIRDLA EEYGLAIHAH RAMHSAFTRN PYHGISMYVL 300
    AKLYRIIGVD QLHIGTAGVG KLEGGKIEVI RYARILREKH FKPDPDDIFH 350
    LEQEMHHIKP AMPVSSGGLH PGNLPGVIEA LGTELILQIG GGVLGHPDGP 400
    RAGAMAVRQS LEAILKGVPL DEYAKTHREL ARALEKWGFA KPI 443
    Length:443
    Mass (Da):49,518
    Last modified:August 10, 2010 - v1
    Checksum:i4C7B43A1C1960033
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002051 Genomic DNA. Translation: ADI32501.1.
    RefSeqiYP_003669400.1. NC_014205.1.

    Genome annotation databases

    EnsemblBacteriaiADI32501; ADI32501; Shell_1412.
    GeneIDi9234703.
    KEGGishc:Shell_1412.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002051 Genomic DNA. Translation: ADI32501.1 .
    RefSeqi YP_003669400.1. NC_014205.1.

    3D structure databases

    ProteinModelPortali D7D9Q5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADI32501 ; ADI32501 ; Shell_1412 .
    GeneIDi 9234703.
    KEGGi shc:Shell_1412.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci SHEL591019:GC4A-1449-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01133. RuBisCO_L_type3.
    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. "Complete sequence of Staphylothermus hellenicus DSM 12710."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.
      Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8Imported.

    Entry informationi

    Entry nameiD7D9Q5_STAHD
    AccessioniPrimary (citable) accession number: D7D9Q5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: August 10, 2010
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 29 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 proteomeImported

    External Data

    Dasty 3