Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

TetX2 protein

Gene

tetX2

Organism
Bacteroides thetaiotaomicron
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611FADCombined sources
Binding sitei117 – 1171FADCombined sources
Binding sitei139 – 1391FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei311 – 3111FADCombined sources

Regions

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

GO - Molecular functioni

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

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

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:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MTMRIDTDKQ MNLLSDKNVA IIGGGPVGLT MAKLLQQNGI DVSVYERDND
60 70 80 90 100
REARIFGGTL DLHKGSGQEA MKKAGLLQTY YDLALPMGVN IADEKGNILS
110 120 130 140 150
TKNVKPENRF DNPEINRNDL RAILLNSLEN DTVIWDRKLV MLEPGKKKWT
160 170 180 190 200
LTFENKPSET ADLVILANGG MSKVRKFVTD TEVEETGTFN IQADIHQPEI
210 220 230 240 250
NCPGFFQLCN GNRLMASHQG NLLFANPNNN GALHFGISFK TPDEWKNQTQ
260 270 280 290 300
VDFQNRNSVV DFLLKEFSDW DERYKELIHT TLSFVGLATR IFPLEKPWKS
310 320 330 340 350
KRPLPITMIG DAAHLMPPFA GQGVNSGLVD ALILSDNLAD GKFNSIEEAV
360 370 380
KNYEQQMFIY GKEAQEESTQ NEIEMFKPDF TFQQLLNV
Length:388
Mass (Da):43,708
Last modified:December 1, 2001 - v1
Checksum:iC0F8976A7A82F394
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ311171 Genomic DNA. Translation: CAC47932.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ311171 Genomic DNA. Translation: CAC47932.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ93L51.

Family and domain databases

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

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: January 7, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.