ABC-type ferric hydroxamate transporter
| ABC-type ferric hydroxamate transporter | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The translocase as folded by AlphaFold | |||||||||
| Identifiers | |||||||||
| EC no. | 7.2.2.16 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The ABC-type ferric hydroxamate transporter, (known also as the iron(III) hydroxamate ABC transporter and ATP phosphohydrolase [ABC-type, iron(III) hydroxamate-importing]) is a translocase enzyme expressed in the cell membranes of bacterial and animal cells.[1] The enzyme possesses an ATP Cassette, indicated by the presence of two similar triphosphate-binding residues and two functional integral membrane domains. It has been observed as a bacterial protein that binds with an extracellular binding protein and facilitates the import of IronFe3+-complexed hydroxamate siderophores (ion-chelating complexes like coprogen, ferrichrome and the ferric hydroxamate antibiotic, albomycin).[2] The enzyme catalyzes the following chemical reaction
- ATP + H20 + Iron-Hydroxamate complex hydroxamate-binding protein (side 1) = ADP + phosphate + Iron-Hydroxamate complex hydroxamate-binding protein (side 2)
Note that 'side 1' and 'side 2' correspond to different compartments, or sides of the cell membrane through which the enzyme translocates.[3] The enzyme is involved in various important pathways, including toluene degradation, androgen and estrogen metabolism, biotin biosynthesis, cellulose degradation, cysteine metabolism and lipid metabolism. In e. coli, the enzyme is encoded by b0151(fhuC)
References
[edit]- ^ None. "KEGG ENZYME 7.2.2.16". KEGG. Database. Retrieved 28 April 2025.
- ^ "ENZYME ENTRY". Expasy. Database. Retrieved 28 April 2025.
- ^ "EC class 7". ExplorEnz - The Enzyme Database. Retrieved 24 October 2019.