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)

A1RZJ5

- A1RZJ5_THEPD

UniProt

A1RZJ5 - A1RZJ5_THEPD

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermofilum pendens (strain Hrk 5)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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. 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

    BioCyciTPEN368408:GHSG-1282-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:Tpen_1227Imported
    OrganismiThermofilum pendens (strain Hrk 5)Imported
    Taxonomic identifieri368408 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum
    ProteomesiUP000000641: 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

    Protein-protein interaction databases

    STRINGi368408.Tpen_1227.

    Structurei

    3D structure databases

    ProteinModelPortaliA1RZJ5.
    SMRiA1RZJ5. Positions 11-442.
    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.UniRule annotation
    Belongs to the RuBisCO large chain family. Type III subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiVIVTFRV.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProiIPR017712. RuBisCO_III.
    IPR020878. RuBisCo_large_chain_AS.
    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.
    PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1RZJ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEEFEPYGE FVVKSYLPDP DKDVIVTFRV TPSEGFTIED AAGGVAAESS    50
    VGTWTTLYQW YDKSRIDRLK GKAYYMESLG DGSYILRVAY PVELFEEGNM 100
    PAFLASVAGN IFGMRRVRSL RVEDIYLPEA FLKHFKGPSQ GVEGVRGKLK 150
    IWGRPIIGTV PKPKVGYSPE EVEKLAYEIL VGGMDFVKDD ENLAGPSYCR 200
    FEERAKAIMK AIDRAEKETG ERKAWLANIT ADVREMERRL KLVAELGNTH 250
    VMVDVVIAGW SSLTYVRDLA ADYKLAIHGH RAFHAAFTRN PYHGVSMFTL 300
    AKLYRIIGVD QLHVGTPEVG KLEAKAVDVI RMARLLREQT YKPDIEDGLH 350
    MQQPFPGIKP AFPVSSGGLH PGTLPAVIKA MGVDTVIQVG GGVVGHPDGP 400
    RAGAAAARQA VEAYLEGVPL QEYAKTHREL ARALEKWGQV IPV 443
    Length:443
    Mass (Da):48,972
    Last modified:February 6, 2007 - v1
    Checksum:i64E48C8F1DAF8288
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000505 Genomic DNA. Translation: ABL78625.1.
    RefSeqiWP_011752890.1. NC_008698.1.
    YP_920628.1. NC_008698.1.

    Genome annotation databases

    EnsemblBacteriaiABL78625; ABL78625; Tpen_1227.
    GeneIDi4601724.
    KEGGitpe:Tpen_1227.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000505 Genomic DNA. Translation: ABL78625.1 .
    RefSeqi WP_011752890.1. NC_008698.1.
    YP_920628.1. NC_008698.1.

    3D structure databases

    ProteinModelPortali A1RZJ5.
    SMRi A1RZJ5. Positions 11-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 368408.Tpen_1227.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL78625 ; ABL78625 ; Tpen_1227 .
    GeneIDi 4601724.
    KEGGi tpe:Tpen_1227.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi VIVTFRV.

    Enzyme and pathway databases

    BioCyci TPEN368408:GHSG-1282-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProi IPR017712. RuBisCO_III.
    IPR020878. RuBisCo_large_chain_AS.
    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.
    PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Hrk 5Imported.

    Entry informationi

    Entry nameiA1RZJ5_THEPD
    AccessioniPrimary (citable) accession number: A1RZJ5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 6, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 52 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