AC   MF_00845;
DC   Protein; auto
TR   HAMAP; MF_00845; -; 1; level=0
XX
Names: TetX_monooxygenase
XX
ID   TETX
DE   RecName: Full=Flavin-dependent monooxygenase;
DE   AltName: Full=TetX monooxygenase;
DE            Short=TetX;
DE            EC=1.14.13.-;
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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.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Consists of an N-terminal FAD-binding domain with a Rossman
CC       fold and a C-terminal substrate-binding domain.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX
CC       subfamily.
XX
DR   Pfam; PF01494; FAD_binding_3; 1; trigger=no
XX
KW   Cytoplasm
KW   FAD
KW   Flavoprotein
KW   Monooxygenase
KW   NADP
KW   Nucleotide-binding
KW   Oxidoreductase
XX
GO   GO:0004497; F:monooxygenase activity
GO   GO:0000166; F:nucleotide binding
GO   GO:0005737; C:cytoplasm
XX
FT   From: TETX_BACT4 (Q93L51)
FT   BINDING         54
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT   Condition: R
FT   BINDING         61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: D
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: R
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: D
XX
Size: 357-413;
Related: None;
Template: Q93L51; Q01911;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Other TetX proteins able to modify tetracycline and its analogs
 have been isolated from Mycobacterium abscessus and soil bacteria. These
 proteins are not members of this family. The proteins from soil bacteria
 modify a different position on the antibiotic and generate a different
 product.
XX
# Revision 1.5 2022/11/19
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