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Database: UniProt
Entry: A0A0F0LAX8_9MICO
LinkDB: A0A0F0LAX8_9MICO
Original site: A0A0F0LAX8_9MICO 
ID   A0A0F0LAX8_9MICO        Unreviewed;       246 AA.
AC   A0A0F0LAX8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Aminoglycoside 3'-phosphotransferase {ECO:0000313|EMBL:KJL30357.1};
DE            EC=2.7.1.95 {ECO:0000313|EMBL:KJL30357.1};
GN   Name=neo {ECO:0000313|EMBL:KJL30357.1};
GN   ORFNames=RS83_00742 {ECO:0000313|EMBL:KJL30357.1};
OS   Microbacterium oxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL30357.1, ECO:0000313|Proteomes:UP000033640};
RN   [1] {ECO:0000313|EMBL:KJL30357.1, ECO:0000313|Proteomes:UP000033640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEL4b {ECO:0000313|EMBL:KJL30357.1,
RC   ECO:0000313|Proteomes:UP000033640};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
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:KJL30357.1}.
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DR   EMBL; JYIW01000019; KJL30357.1; -; Genomic_DNA.
DR   RefSeq; WP_045278181.1; NZ_JYIW01000019.1.
DR   AlphaFoldDB; A0A0F0LAX8; -.
DR   PATRIC; fig|82380.11.peg.768; -.
DR   OrthoDB; 3806873at2; -.
DR   Proteomes; UP000033640; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW   Transferase {ECO:0000313|EMBL:KJL30357.1}.
FT   DOMAIN          55..238
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ   SEQUENCE   246 AA;  27079 MW;  7CBE38EDCAFF5DDA CRC64;
     MVIPSASVPN ASVEVPDRVR ELARGAALTP VWLNGIGGLT FRTDDARYIK WGPLDLEASM
     RDEAERMRWA RHWIAAPEVI AQGENDAEEW LVTVALDAHS AVDPRWKGEP ELAVRAVGQA
     LRALHDALPV DECPWEWSVE ARIANAAERG VIVPAELREA PPIDRLVVCH GDACMPNTLL
     DDAGRPAGVV DLAALGTADR WADIAVASMS TVWNFGEGWE DTLIDAYGIA PDLERIAYYR
     RLWNET
//
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