ID A0A1M5T3I1_9BURK Unreviewed; 270 AA.
AC A0A1M5T3I1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase {ECO:0000256|ARBA:ARBA00017903};
DE EC=2.7.1.95 {ECO:0000256|ARBA:ARBA00012193};
GN ORFNames=SAMN05428948_4097 {ECO:0000313|EMBL:SHH45307.1};
OS Massilia sp. CF038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1881045 {ECO:0000313|EMBL:SHH45307.1, ECO:0000313|Proteomes:UP000184361};
RN [1] {ECO:0000313|EMBL:SHH45307.1, ECO:0000313|Proteomes:UP000184361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF038 {ECO:0000313|EMBL:SHH45307.1,
RC ECO:0000313|Proteomes:UP000184361};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQWU01000003; SHH45307.1; -; Genomic_DNA.
DR RefSeq; WP_073221298.1; NZ_FQWU01000003.1.
DR AlphaFoldDB; A0A1M5T3I1; -.
DR OrthoDB; 3806873at2; -.
DR Proteomes; UP000184361; 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 PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR PANTHER; PTHR21310:SF41; BLR5425 PROTEIN; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000184361};
KW Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:SHH45307.1}.
FT DOMAIN 39..262
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 270 AA; 29422 MW; DA22763A3A693D80 CRC64;
MDHDREEMCV PQPIPANIAS LVDGYAWARD TVGESGGTVY RLHGKSDAPD LFLKHGQGVF
ADDVIGEMAR LRWLAGHIAV PAIVQFVATP DGAWLLMSAM PGKTAYQLMS DQAGSGNAVV
DALADFLRRL HAIPVAACPF TSAHAHRLHL ARARIDAGLV DADDFDDERA GWSAEQVWDA
MQDLLPLAPD LVVTHGDYSL DNVFIVDGKV SGCIDAGRVG IADRYQDLAI AWNCLSEFGP
ALQKRFLQQY GVTQPDQARL AFHLMLDELF
//
