Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.190 - aminoglycoside 2''-phosphotransferase and Organism(s) Enterococcus faecalis and UniProt Accession P0A0C2

for references in articles please use BRENDA:EC2.7.1.190
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Enterococcus faecalis
UNIPROT: P0A0C2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Enterococcus faecalis
The enzyme appears in selected viruses and cellular organisms
Synonyms
aph(2'')-id, aph(2''), aminoglycoside kinase, aph(2'')-ia, aph(2'')-iva, aac6-aph2, aph(2'')-iiia, aminoglycoside 2''-phosphotransferase, aph(2'')-if, gentamicin phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional 6'-aminoglycoside acetyltransferase/2"-aminoglycoside phosphotransferase
-
bifunctional AAC/APH
-
aminoglycoside (2'') kinase
-
-
-
-
APH(2'')
-
-
-
-
aphD
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:gentamicin 2''-O-phosphotransferase
Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
x * 56000, SDS-PAGE, x * 56850, calculated
56850
x * 56000, SDS-PAGE, x * 56850, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 56000, SDS-PAGE, x * 56850, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
The N-terminal region contains a sequence homologous to the chloramphenicol acetyltransferase of Bacillus pumUus, and the C-terminal region contains a sequence homologous to the aminoglycoside phosphotransferase of Streptomyces fradiae. It is possible to obtain gene segments independently specifying the acetyltransferase and phosphotransferase activities
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ferretti, J.; Gilmore, K.; Courvalin, P.
Nucleotide sequence analysis of the gene specifying the bifunctional 6-aminoglycoside acetyltransferase 2-aminoglycoside phosphotransferase enzyme in Streptococcus faecalis and identification and cloning of gene regions specifying the two activities
J. Bacteriol.
167
631-638
1986
Enterococcus faecalis (P0A0C2), Enterococcus faecalis ATCC 700802 (P0A0C2)
Manually annotated by BRENDA team