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)

I3TDF0

- I3TDF0_THEC1

UniProt

I3TDF0 - I3TDF0_THEC1

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermogladius cellulolyticus (strain 1633)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (05 Sep 2012)
      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 sitei163 – 1631Proton acceptorUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Metal bindingi189 – 1891Magnesium; via carbamate groupUniRule annotation
    Metal bindingi191 – 1911MagnesiumUniRule annotation
    Metal bindingi192 – 1921MagnesiumUniRule annotation
    Active sitei281 – 2811Proton acceptorUniRule annotation
    Binding sitei282 – 2821SubstrateUniRule annotation
    Binding sitei314 – 3141SubstrateUniRule annotation
    Sitei322 – 3221Transition 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 annotation, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciTCEL1184251:GLMC-383-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:TCELL_0363Imported
    OrganismiThermogladius cellulolyticus (strain 1633)Imported
    Taxonomic identifieri1184251 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermogladius
    ProteomesiUP000005270: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei189 – 1891N6-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

    ProteinModelPortaliI3TDF0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni367 – 3693Substrate bindingUniRule annotation
    Regioni389 – 3924Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.
    OMAiVIVTFRV.

    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.

    I3TDF0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKEGFEPYP EYVDKKYQPD PDTHVIVTFR VKPASGFTVE DAAGGVAAES    50
    STGTWTTLFS WYDVSRVKKL SGRAYYFKDL KDGSYIVRVA YPVELFEEGN 100
    MPAFLASVAG NIFGMRRVEG LRVEDIYLPK QFLQYFKGPF KGVKGVREIF 150
    KVHDRPIVGT VPKPKVGYTP EEVEKLALEL LMGGMDYIKD DENLASPSFC 200
    RFEARAKSIM KIIDKVEKET GERKAWFANI TADVREMEKR LKLVADYGNP 250
    YIMVDVVVTG WSALTYIRDL AEEYKLAIHA HRAMHAAITR NPYHGISMFA 300
    LAKLYRFIGM DQLHIGTAGA GKLEGAKLDV VRIAKMLRAE DYQPDPDDDF 350
    HLPQKMYHIK PMMPVSSGGL HPGNLPIVIE ALGTDLVLQI GGGTIGHPDG 400
    PRAGATAVRQ ALDAIIKGIP LEEYAKDHKE LARALEKWGF AKPI 444
    Length:444
    Mass (Da):49,590
    Last modified:September 5, 2012 - v1
    Checksum:i9CCE1238EE66CCA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003531 Genomic DNA. Translation: AFK50788.1.
    RefSeqiYP_006362926.1. NC_017954.1.

    Genome annotation databases

    EnsemblBacteriaiAFK50788; AFK50788; TCELL_0363.
    GeneIDi13012650.
    KEGGithg:TCELL_0363.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003531 Genomic DNA. Translation: AFK50788.1 .
    RefSeqi YP_006362926.1. NC_017954.1.

    3D structure databases

    ProteinModelPortali I3TDF0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFK50788 ; AFK50788 ; TCELL_0363 .
    GeneIDi 13012650.
    KEGGi thg:TCELL_0363.

    Phylogenomic databases

    KOi K01601.
    OMAi VIVTFRV.

    Enzyme and pathway databases

    BioCyci TCEL1184251:GLMC-383-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 genome sequence of the hyperthermophilic cellulolytic Crenarchaeon 'Thermogladius cellulolyticus' 1633."
      Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.
      J. Bacteriol. 194:4446-4447(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1633Imported.

    Entry informationi

    Entry nameiI3TDF0_THEC1
    AccessioniPrimary (citable) accession number: I3TDF0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 5, 2012
    Last sequence update: September 5, 2012
    Last modified: October 1, 2014
    This is version 18 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