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Annotation rule MF_00845 |
Accession | MF_00845 |
Dates | 6-SEP-2019 (Created) 18-NOV-2019 (Last updated, Version 3) |
Name | TetX_monooxygenase |
Scope | Bacteria |
Templates | Q93L51 (TETX_BACT4); Q01911 (TETX_BACFG): [Recover all] |
Triggered by |
Identifier |
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Protein name |
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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 | RHEA:61444: a tetracycline + H(+) + NADPH + O2 = an 11a-hydroxytetracycline + H2O + NADP(+) |
Cofactor | FAD |
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. |
Pfam | PF01494; FAD_binding_3; 1; |
From: TETX_BACT4 (Q93L51) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 54 | 54 | NADPH | R | ||||||||
BINDING | 61 | 61 | FAD | D | ||||||||
BINDING | 117 | 117 | FAD | R | ||||||||
BINDING | 311 | 311 | FAD | D |
Size range | 357-413 amino acids |
Related rules | None |
Fusion | 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. |