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Q93L51

- Q93L51_BACT4

UniProt

Q93L51 - Q93L51_BACT4

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Protein
Submitted name: TetX2 protein
Gene
tetX2
Organism
Bacteroides thetaiotaomicron
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Sulfate 3
Binding sitei61 – 611FADImported
Binding sitei117 – 1171FADImported
Binding sitei139 – 1391FAD; via amide nitrogen and carbonyl oxygenImported
Binding sitei311 – 3111FADImported

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272FADImported
Nucleotide bindingi46 – 472FADImported
Nucleotide bindingi321 – 3244FADImported

GO - Molecular functioni

  1. nucleotide binding Source: UniProtKB-KW
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Ligandi

    FADImported, Flavoprotein, Nucleotide-bindingImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    TetX2 proteinImported
    Gene namesi
    Name:tetX2Imported
    OrganismiBacteroides thetaiotaomicronImported
    Taxonomic identifieri818 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XDOX-ray2.09A/B/C/D11-388[»]
    2XYOX-ray3.00A/B/C/D11-388[»]
    2Y6QX-ray2.37A/B/C/D11-388[»]
    2Y6RX-ray3.10A/B/C/D11-388[»]
    3P9UX-ray2.81A/B/C/D11-388[»]
    3V3NX-ray2.70A/B/C/D11-388[»]
    3V3OX-ray2.90A/B/C/D11-388[»]
    4A6NX-ray2.30A/B/C/D11-388[»]
    4A99X-ray2.18A/B/C/D11-388[»]
    4GUVX-ray2.73A/B/C/D11-388[»]
    ProteinModelPortaliQ93L51.

    Miscellaneous databases

    EvolutionaryTraceiQ93L51.

    Family & Domainsi

    Family and domain databases

    InterProiIPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    [Graphical view]
    PRINTSiPR00420. RNGMNOXGNASE.

    Sequencei

    Sequence statusi: Complete.

    Q93L51-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMRIDTDKQ MNLLSDKNVA IIGGGPVGLT MAKLLQQNGI DVSVYERDND    50
    REARIFGGTL DLHKGSGQEA MKKAGLLQTY YDLALPMGVN IADEKGNILS 100
    TKNVKPENRF DNPEINRNDL RAILLNSLEN DTVIWDRKLV MLEPGKKKWT 150
    LTFENKPSET ADLVILANGG MSKVRKFVTD TEVEETGTFN IQADIHQPEI 200
    NCPGFFQLCN GNRLMASHQG NLLFANPNNN GALHFGISFK TPDEWKNQTQ 250
    VDFQNRNSVV DFLLKEFSDW DERYKELIHT TLSFVGLATR IFPLEKPWKS 300
    KRPLPITMIG DAAHLMPPFA GQGVNSGLVD ALILSDNLAD GKFNSIEEAV 350
    KNYEQQMFIY GKEAQEESTQ NEIEMFKPDF TFQQLLNV 388
    Length:388
    Mass (Da):43,708
    Last modified:December 1, 2001 - v1
    Checksum:iC0F8976A7A82F394
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311171 Genomic DNA. Translation: CAC47932.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311171 Genomic DNA. Translation: CAC47932.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XDO X-ray 2.09 A/B/C/D 11-388 [» ]
    2XYO X-ray 3.00 A/B/C/D 11-388 [» ]
    2Y6Q X-ray 2.37 A/B/C/D 11-388 [» ]
    2Y6R X-ray 3.10 A/B/C/D 11-388 [» ]
    3P9U X-ray 2.81 A/B/C/D 11-388 [» ]
    3V3N X-ray 2.70 A/B/C/D 11-388 [» ]
    3V3O X-ray 2.90 A/B/C/D 11-388 [» ]
    4A6N X-ray 2.30 A/B/C/D 11-388 [» ]
    4A99 X-ray 2.18 A/B/C/D 11-388 [» ]
    4GUV X-ray 2.73 A/B/C/D 11-388 [» ]
    ProteinModelPortali Q93L51.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q93L51.

    Family and domain databases

    InterProi IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view ]
    Pfami PF01494. FAD_binding_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00420. RNGMNOXGNASE.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the 13-kilobase ermF region of the Bacteroides conjugative transposon CTnDOT."
      Whittle G., Hund B.D., Shoemaker N.B., Salyers A.A.
      Appl. Environ. Microbiol. 67:3488-3495(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase."
      Volkers G., Palm G.J., Weiss M.S., Wright G.D., Hinrichs W.
      FEBS Lett. 585:1061-1066(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD.
    3. "Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline degrading monooxygenase at 2.8 A resolution."
      Walkiewicz K., Davlieva M., Wu G., Shamoo Y.
      Proteins 79:2335-2340(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD.
    4. "Crystal structure of TetX2 T280A: an adaptive mutant in complex with minocycline."
      Walkiewicz K., Shamoo Y.
      Submitted (DEC-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD.
    5. "Crystal structure of TetX2 T280A: an adaptive mutant in complex with tigecycline."
      Walkiewicz K., Shamoo Y.
      Submitted (DEC-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD.
    6. "Putative dioxygen-binding sites and recognition of tigecycline and minocycline in the tetracycline-degrading monooxygenase TetX."
      Volkers G., Damas J.M., Palm G.J., Panjikar S., Soares C.M., Hinrichs W.
      Acta Crystallogr. D 69:1758-1767(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD.

    Entry informationi

    Entry nameiQ93L51_BACT4
    AccessioniPrimary (citable) accession number: Q93L51
    Entry historyi
    Integrated into UniProtKB/TrEMBL: December 1, 2001
    Last sequence update: December 1, 2001
    Last modified: September 3, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3

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