Molecule Information
General Information of the Molecule (ID: Mol00848)
Name |
Bifunctional AAC/APH (AAC/APH)
,Staphylococcus aureus
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Synonyms |
AAC(6'); 2''-aminoglycoside phosphotransferase; APH(2''); R015; VRA0030
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Molecule Type |
Protein
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Gene Name |
aacA-aphD
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Gene ID | |||||
Sequence |
MNIVENEICIRTLIDDDFPLMLKWLTDERVLEFYGGRDKKYTLESLKKHYTEPWEDEVFR
VIIEYNNVPIGYGQIYKMYDELYTDYHYPKTDEIVYGMDQFIGEPNYWSKGIGTRYIKLI FEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHEGKKEDCYLMEYRYD DNATNVKAMKYLIEHYFDNFKVDSIEIIGSGYDSVAYLVNNEYIFKTKFSTNKKKGYAKE KAIYNFLNTNLETNVKIPNIEYSYISDELSILGYKEIKGTFLTPEIYSTMSEEEQNLLKR DIASFLRQMHGLDYTDISECTIDNKQNVLEEYILLRETIYNDLTDIEKDYIESFMERLNA TTVFEGKKCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTN FGEDILRMYGNIDIEKAKEYQDIVEEYYPIETIVYGIKNIKQEFIENGRKEIYKRTYKD Click to Show/Hide
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Function |
Involved in resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region. The C-terminal region is a kinase that phosphorylates several 4,6-disubstituted aminoglycosides.
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Uniprot ID | |||||
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Type(s) of Resistant Mechanism of This Molecule
DISM: Drug Inactivation by Structure Modification
Drug Resistance Data Categorized by Drug
Approved Drug(s)
1 drug(s) in total
Plazomicin
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Disease Class: Bacterial infection | [1], [2] | |||
Resistant Disease | Bacterial infection [ICD-11: 1A00-1C4Z] | |||
Resistant Drug | Plazomicin | |||
Molecule Alteration | Expression | Up-regulation |
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Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Staphylococcus aureus ATCC 29213 | 1280 | ||
Staphylococcus aureus isolates | 1280 | |||
Experiment for Molecule Alteration |
Whole genome sequence assay | |||
Mechanism Description | AAC(6')-APH(2") is an enzyme with 6'-N-acetyltransferase and 2"-O-phosphotransferase activities.The bifunctional AAC(6')-APH(2") has the capacity to inactivate virtually all clinically important aminoglycosides through N- and O-acetylation and phosphorylation of hydroxyl groups. |
References
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