Aminoglycoside 2'-N-acetyltransferase
Details
- Name
- Aminoglycoside 2'-N-acetyltransferase
- Synonyms
- 2.3.1.-
- AAC(2')-Ic
- Gene Name
- aac
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051146|Aminoglycoside 2'-N-acetyltransferase MHTQVHTARLVHTADLDSETRQDIRQMVTGAFAGDFTETDWEHTLGGMHALIWHHGAIIA HAAVIQRRLIYRGNALRCGYVEGVAVRADWRGQRLVSALLDAVEQVMRGAYQLGALSSSA RARRLYASRGWLPWHGPTSVLAPTGPVRTPDDDGTVFVLPIDISLDTSAELMCDWRAGDV W
- Number of residues
- 181
- Molecular Weight
- 20037.53
- Theoretical pI
- Not Available
- GO Classification
- Functionsaminoglycoside 2'-N-acetyltransferase activity / aminoglycoside N-acetyltransferase activityProcessesaminoglycoside antibiotic catabolic process / response to antibioticComponentsplasma membrane
- General Function
- May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system (PubMed:9159528).
- Specific Function
- Aminoglycoside 2'-n-acetyltransferase activity
- Pfam Domain Function
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WQG9 UniProtKB Entry Name AAC2_MYCTU - General References
- Ainsa JA, Perez E, Pelicic V, Berthet FX, Gicquel B, Martin C: Aminoglycoside 2'-N-acetyltransferase genes are universally present in mycobacteria: characterization of the aac(2')-Ic gene from Mycobacterium tuberculosis and the aac(2')-Id gene from Mycobacterium smegmatis. Mol Microbiol. 1997 Apr;24(2):431-41. [Article]
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL: Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat Struct Biol. 2002 Sep;9(9):653-8. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01842 3'-Phosphate-Adenosine-5'-Diphosphate experimental unknown Details DB01992 Coenzyme A investigational, nutraceutical unknown Details DB03615 Ribostamycin approved, experimental unknown Details DB01172 Kanamycin approved, investigational, vet_approved unknown substrate Details DB01992 Coenzyme A investigational, nutraceutical unknown ligand Details DB03615 Ribostamycin approved, experimental unknown substrate Details