Kanamycin nucleotidyltransferase

Details

Name
Kanamycin nucleotidyltransferase
Synonyms
  • 2.7.7.-
  • kan
  • Neo(R)
Gene Name
knt
Organism
Staphylococcus aureus
Amino acid sequence
>lcl|BSEQ0022440|Kanamycin nucleotidyltransferase
MNGPIIMTREERMKIVHEIKERILDKYGDDVKAIGVYGSLGRQTDGPYSDIEMMCVMSTE
EAEFSHEWTTGEWKVEVNFDSEEILLDYASQVESDWPLTHGQFFSILPIYDSGGYLEKVY
QTAKSVEAQTFHDAICALIVEELFEYAGKWRNIRVQGPTTFLPSLTVQVAMAGAMLIGLH
HRICYTTSASVLTEAVKQSDLPSGYDHLCQFVMSGQLSDSEKLLESLENFWNGIQEWTER
HGYIVDVSKRIPF
Number of residues
253
Molecular Weight
28797.38
Theoretical pI
4.44
GO Classification
Functions
nucleotidyltransferase activity
Processes
response to antibiotic
General Function
Nucleotidyltransferase activity
Specific Function
Inactivates the antibiotic kanamycin by catalyzing the transfer of a nucleotidyl group from nucleoside triphosphates such as ATP to the 4'-hydroxyl group of the aminoglycoside.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006834|708 bp
ATGAAACATGGCATTCAGTCACAAAAGGTTGTTGCTGAAGTTATTAAACAAAAGCCAACA
GTTCGTTGGTTGTTTCTCACATTAACAGTTAAAAATGTTTATGATGGCGAAGAATTAAAT
AAGAGTTTGTCAGATATGGCTCAAGGATTTCGCCGAATGATGCAATATAAAAAAATTAAT
AAAAATCTTGTTGGTTTTATGCGTGCAACGGAAGTGACAATAAATAATAAAGATAATTCT
TATAATCAGCACATGCATGTATTGGTATGTGTGGAACCAACTTATTTTAAGAATACAGAA
AACTACGTGAATCAAAAACAATGGATTCAATTTTGGAAAAAGGCAATGAAATTAGACTAT
GATCCAAATGTAAAAGTTCAAATGATTCGACCGAAAAATAAATATAAATCGGATATACAA
TCGGCAATTGACGAAACTGCAAAATATCCTGTAAAGGATACGGATTTTATGACCGATGAT
GAAGAAAAGAATTTGAAACGTTTGTCTGATTTGGAGGAAGGTTTACACCGTAAAAGGTTA
ATCTCCTATGGTGGTTTGTTAAAAGAAATACATAAAAAATTAAACCTTGATGACACAGAA
GAAGGCGATTTGATTCATACAGATGATGACGAAAAAGCCGATGAAGATGGATTTTCTATT
ATTGCAATGTGGAATTGGGAACGGAAAAATTATTTTATTAAAGAGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP05057
UniProtKB Entry NameKANU_STAAU
GenBank Protein ID46496
GenBank Gene IDX03408
General References
  1. Muller RE, Ano T, Imanaka T, Aiba S: Complete nucleotide sequences of Bacillus plasmids pUB110dB, pRBH1 and its copy mutants. Mol Gen Genet. 1986 Jan;202(1):169-71. [Article]
  2. Matsumura M, Katakura Y, Imanaka T, Aiba S: Enzymatic and nucleotide sequence studies of a kanamycin-inactivating enzyme encoded by a plasmid from thermophilic bacilli in comparison with that encoded by plasmid pUB110. J Bacteriol. 1984 Oct;160(1):413-20. [Article]
  3. Bashkirov VI, Mil'shina NV, Prozorov AA: [Nucleotide sequence and physical map of kanamycin-resistant plasmid pUB110 from Staphylococcus aureus]. Genetika. 1986 Jul;22(7):1081-92. [Article]
  4. McKenzie T, Hoshino T, Tanaka T, Sueoka N: The nucleotide sequence of pUB110: some salient features in relation to replication and its regulation. Plasmid. 1986 Mar;15(2):93-103. [Article]
  5. McKenzie T, Hoshino T, Tanaka T, Sueoka N: Correction. A revision of the nucleotide sequence and functional map of pUB110. Plasmid. 1987 Jan;17(1):83-5. [Article]
  6. Sakon J, Liao HH, Kanikula AM, Benning MM, Rayment I, Holden HM: Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution. Biochemistry. 1993 Nov 16;32(45):11977-84. [Article]
  7. Pedersen LC, Benning MM, Holden HM: Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry. 1995 Oct 17;34(41):13305-11. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01172Kanamycinapproved, investigational, vet_approvedunknownsubstrateDetails