ID F1AEN4_SALTM Unreviewed; 271 AA.
AC F1AEN4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase {ECO:0000256|ARBA:ARBA00017903};
DE EC=2.7.1.95 {ECO:0000256|ARBA:ARBA00012193};
GN Name=aphA1b {ECO:0000313|EMBL:ADY69175.1};
GN ORFNames=G0L49_23320 {ECO:0000313|EMBL:HAD0042490.1}, G0L49_24525
GN {ECO:0000313|EMBL:HAD0042710.1}, G0M16_25260
GN {ECO:0000313|EMBL:HAF0208534.1}, G0M16_25790
GN {ECO:0000313|EMBL:HAF0208628.1}, G4O60_005080
GN {ECO:0000313|EMBL:HAE7212809.1}, G4O60_005138
GN {ECO:0000313|EMBL:HAE7212856.1};
OS Salmonella typhimurium.
OG Plasmid pSRC125 {ECO:0000313|EMBL:ADY69175.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371 {ECO:0000313|EMBL:ADY69175.1};
RN [1] {ECO:0000313|EMBL:ADY69175.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pSRC125 {ECO:0000313|EMBL:ADY69175.1};
RX PubMed=21702681; DOI=10.1089/mdr.2011.0037;
RA Cain A.K., Hall R.M.;
RT "Transposon Tn5393e carrying the aphA1-containing transposon Tn6023
RT upstream of strAB does not confer resistance to streptomycin.";
RL Microb. Drug Resist. 17:389-394(2011).
RN [2] {ECO:0000313|EMBL:HAD0042490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14DRC {ECO:0000313|EMBL:HAF0208534.1}, 2011-60-312-1
RC {ECO:0000313|EMBL:HAE7212809.1}, and R1796
RC {ECO:0000313|EMBL:HAD0042490.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:HAD0042490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14DRC {ECO:0000313|EMBL:HAF0208534.1}, 2011-60-312-1
RC {ECO:0000313|EMBL:HAE7212809.1}, and R1796
RC {ECO:0000313|EMBL:HAD0042490.1};
RG NCBI Pathogen Detection Project;
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate;
CC Xref=Rhea:RHEA:24256, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57909, ChEBI:CHEBI:58214, ChEBI:CHEBI:456216;
CC EC=2.7.1.95; Evidence={ECO:0000256|ARBA:ARBA00001685};
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
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DR EMBL; GU562437; ADY69175.1; -; Genomic_DNA.
DR EMBL; DAANIR010000143; HAD0042490.1; -; Genomic_DNA.
DR EMBL; DAANIR010000208; HAD0042710.1; -; Genomic_DNA.
DR EMBL; DAASVO010000060; HAE7212809.1; -; Genomic_DNA.
DR EMBL; DAASVO010000083; HAE7212856.1; -; Genomic_DNA.
DR EMBL; DAATUS010000103; HAF0208534.1; -; Genomic_DNA.
DR EMBL; DAATUS010000137; HAF0208628.1; -; Genomic_DNA.
DR RefSeq; WP_000018326.1; NZ_VFYH01000067.1.
DR AlphaFoldDB; F1AEN4; -.
DR SMR; F1AEN4; -.
DR GeneID; 75009462; -.
DR PATRIC; fig|90371.1230.peg.5130; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05150; APH; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR024165; Kan/Strep_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|PIRNR:PIRNR000706};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Kinase {ECO:0000256|PIRNR:PIRNR000706};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Plasmid {ECO:0000313|EMBL:ADY69175.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:ADY69175.1}.
FT DOMAIN 32..262
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 271 AA; 30930 MW; 3B8CE6C591219263 CRC64;
MSHIQRETSC SRPRLNSNLD ADLYGYRWAR DNVGQSGATI YRLYGKPNAP ELFLKHGKGS
VANDVTDEMV RLNWLTAFMP LPTIKHFIRT PDDAWLLTTA IPGKTAFQVL EEYPDSGENI
VDALAVFLRR LHSIPVCNCP FNSDRVFRLA QAQSRMNNGL VDASDFDDER NGWPVEQVWK
EMHKLLPFSP DSVVTHGDFS LDNLIFDEGK LIGCIDVGRV GIADRYQDLA ILWNCLGEFS
PSLQKRLFQK YGIDNPDMNK LQFHLMLDEF F
//
