HAMAP rule MF_00845
General rule information
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| Accession | MF_00845 |
| Dates | 6-SEP-2019 (Created)
19-NOV-2022 (Last updated, Version 5) |
| Name | TetX_monooxygenase |
| Scope(s) |
Bacteria |
| Template(s) | Q93L51 (TETX_BACT4); Q01911 (TETX_BACFG); [ Recover all ] |
| Triggered by |
HAMAP; MF_00845 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | TETX |
| Protein name | RecName: Full=Flavin-dependent monooxygenase; AltName: Full=TetX monooxygenase; Short=TetX; EC=1.14.13.-; |
Comments
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| FUNCTION | An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs. |
| CATALYTIC ACTIVITY | Reaction=a tetracycline + H(+) + NADPH + O2 = an 11a- hydroxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61444, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:144644, ChEBI:CHEBI:144645; |
| COFACTOR | Name=FAD; Xref=ChEBI:CHEBI:57692; |
| SUBUNIT | Monomer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| DOMAIN | Consists of an N-terminal FAD-binding domain with a Rossman fold and a C-terminal substrate-binding domain. |
| SIMILARITY | Belongs to the aromatic-ring hydroxylase family. TetX subfamily. |
Keywords
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Gene Ontology
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| GO:0004497; Molecular function:monooxygenase activity |
| GO:0000166; Molecular function:nucleotide binding |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF01494; FAD_binding_3; 1; |
Features
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| From: TETX_BACT4 (Q93L51) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 54 | 54 | /ligand="NADPH" /ligand_id="ChEBI:CHEBI:57783" |
R | ||||||||
| BINDING | 61 | 61 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
D | ||||||||
| BINDING | 117 | 117 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
R | ||||||||
| BINDING | 311 | 311 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
D | ||||||||
Additional information
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| Size range | 357-413 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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. |