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Database: UniProt
Entry: A0A2D0KQ49_9GAMM
LinkDB: A0A2D0KQ49_9GAMM
Original site: A0A2D0KQ49_9GAMM 
ID   A0A2D0KQ49_9GAMM        Unreviewed;       258 AA.
AC   A0A2D0KQ49;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aminoglycoside 3'-phosphotransferase {ECO:0000256|ARBA:ARBA00017903};
DE            EC=2.7.1.95 {ECO:0000256|ARBA:ARBA00012193};
GN   ORFNames=Xsto_01900 {ECO:0000313|EMBL:PHM65542.1};
OS   Xenorhabdus stockiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM65542.1, ECO:0000313|Proteomes:UP000222366};
RN   [1] {ECO:0000313|EMBL:PHM65542.1, ECO:0000313|Proteomes:UP000222366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM65542.1,
RC   ECO:0000313|Proteomes:UP000222366};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHM65542.1}.
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DR   EMBL; NJAJ01000015; PHM65542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0KQ49; -.
DR   Proteomes; UP000222366; Unassembled WGS sequence.
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   Transferase {ECO:0000256|PIRNR:PIRNR000706}.
FT   DOMAIN          29..243
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ   SEQUENCE   258 AA;  29262 MW;  866436BAB08AF7AB CRC64;
     MLPKLPPSID CFIGNSALIP DKIGESPCRV YSFIRGNDRF FLKYSPSVYA NTTYSVMREA
     SVLNWLADRL NVAEVVCVAK NSGGEFMISR AVPGKPLYER LNAGQPVLEL FHEAVRQMQS
     VPIVDCPFDS GAGFRLNELE YFLNHGLCAE QYDLEQWPGI TTPQSLLKHL HATLPSEERV
     FSHGDLCDSN IFVDEHDYLY FIDLGRGGVA DRWLDIAFVH RNLREEISVN IAAEFLTTLG
     DFDNVAKREF FEQLDELF
//
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