TETX_SPHSM
ID TETX_SPHSM Reviewed; 388 AA.
AC Q06DK7;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Flavin-dependent monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845};
DE AltName: Full=TetX monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845};
DE Short=TetX {ECO:0000255|HAMAP-Rule:MF_00845};
DE EC=1.14.13.231 {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000305|PubMed:26038239};
DE AltName: Full=Tetracycline resistance protein {ECO:0000303|PubMed:19187139};
GN Name=tet(X) {ECO:0000303|PubMed:19187139};
OS Sphingobacterium sp. (strain PM2-P1-29).
OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=403776;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC STRAIN=PM2-P1-29; TRANSPOSON=Tn6031;
RX PubMed=19187139; DOI=10.1111/j.1365-2672.2008.04101.x;
RA Ghosh S., Sadowsky M.J., Roberts M.C., Gralnick J.A., LaPara T.M.;
RT "Sphingobacterium sp. strain PM2-P1-29 harbours a functional tet(X) gene
RT encoding for the degradation of tetracycline.";
RL J. Appl. Microbiol. 106:1336-1342(2009).
RN [2]
RP FUNCTION IN INACTIVATING TETRACYCLINE.
RC STRAIN=PM2-P1-29; TRANSPOSON=Tn6031;
RX PubMed=26038239; DOI=10.1093/femsec/fiv059;
RA Ghosh S., LaPara T.M., Sadowsky M.J.;
RT "Transformation of tetracycline by TetX and its subsequent degradation in a
RT heterologous host.";
RL FEMS Microbiol. Ecol. 91:0-0(2015).
CC -!- FUNCTION: An FAD-requiring monooxygenase active on some tetracycline
CC antibiotic derivatives, which leads to their inactivation. Hydroxylates
CC carbon 11a of tetracycline and some analogs. {ECO:0000255|HAMAP-
CC Rule:MF_00845}.
CC -!- FUNCTION: This bacteria is able to grow in the presence of moderate
CC concentrations of tetracycline and its analogs, presumably due to the
CC presence of this protein (PubMed:19187139). Expression in E.coli leads
CC to breakdown of tetracycline; the initial products include a
CC monooxygenated compound. After 2 hours intact tetracycline is no longer
CC detectable in the culture supernatant, while degradation intermediates
CC remain detectable for at least 20 hours (PubMed:26038239).
CC {ECO:0000250|UniProtKB:Q93L51, ECO:0000269|PubMed:19187139,
CC ECO:0000269|PubMed:26038239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetracycline + H(+) + NADPH + O2 = an 11a-
CC hydroxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61444,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:144644,
CC ChEBI:CHEBI:144645; Evidence={ECO:0000255|HAMAP-Rule:MF_00845,
CC ECO:0000305|PubMed:26038239};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + tetracycline = 11a-hydroxytetracycline +
CC H2O + NADP(+); Xref=Rhea:RHEA:50004, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77932, ChEBI:CHEBI:132727;
CC EC=1.14.13.231; Evidence={ECO:0000305|PubMed:26038239};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00845};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00845}.
CC -!- DOMAIN: Consists of an N-terminal FAD-binding domain with a Rossman
CC fold and a C-terminal substrate-binding domain. {ECO:0000255|HAMAP-
CC Rule:MF_00845}.
CC -!- MISCELLANEOUS: Encoded in the mobilizable Tn6031 transposon.
CC {ECO:0000269|PubMed:19187139}.
CC -!- MISCELLANEOUS: Tetracycline antibiotics bind to the ribosomal acceptor
CC site (A-site), preventing binding of the aminoacyl-tRNA to the A-site.
CC The hydrophilic side of tetracycline makes many hydrogen-bonding
CC interactions with oxygen atoms of the ribosome's phosphate backbone.
CC {ECO:0000250|UniProtKB:Q93L51}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00845}.
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DR EMBL; EU864422; ABI95380.2; -; Genomic_DNA.
DR AlphaFoldDB; Q06DK7; -.
DR SMR; Q06DK7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00845; TetX_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR043683; TetX_monooxygenase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cytoplasm; FAD; Flavoprotein; Monooxygenase; NADP;
KW Nucleotide-binding; Oxidoreductase; Transposable element.
FT CHAIN 1..388
FT /note="Flavin-dependent monooxygenase"
FT /id="PRO_0000448379"
FT BINDING 54
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845"
SQ SEQUENCE 388 AA; 43725 MW; 16209EA7CC5A11D2 CRC64;
MTMRIDTDKQ MNLLSDKNVA IIGGGPVGLT MAKLLQQNGI DVSVYERDND REARIFGGTL
DLHKGSGQEA MKKAGLLQTY YDLALPMGVN IADKKGNILS TKNVKPENRF DNPEINRNDL
RAILLNSLEN DTVIWDRKLV MLEPGKKKWT LTFENKPSET ADLVILANGG MSKVRKFVTD
TEVEETGTFN IQADIHQPEI NCPGFFQLCN GNRLMASHQG NLLFANPNNN GALHFGISFK
TPDEWKNQTQ VDFQNRNSVV DFLLKEFSDW DERYKELIHT TLSFVGLATR IFPLEKPWKS
KRPLPITMIG DAAHLMPPFA GQGVNSGLVD ALILSDNLAD GKFNSIEEAV KNYEQQMFMY
GKEAQEESTQ NEIEMFKPDF TFQQLLNV
