ID   Y3168_MYCTO             Reviewed;         378 AA.
AC   P9WI98; F2GJM6; L0TES4; O53318; Q7D606;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative aminoglycoside phosphotransferase;
DE            EC=2.7.1.-;
DE   AltName: Full=Putative aminoglycoside antibiotics resistance enzyme;
GN   OrderedLocusNames=MT3257;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Might catalyze the phosphorylation of aminoglycosides and
CC       confer aminoglycoside antibiotics resistance. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47596.1; -; Genomic_DNA.
DR   PIR; F70947; F70947.
DR   RefSeq; WP_003900650.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI98; -.
DR   SMR; P9WI98; -.
DR   EnsemblBacteria; AAK47596; AAK47596; MT3257.
DR   GeneID; 45427156; -.
DR   KEGG; mtc:MT3257; -.
DR   PATRIC; fig|83331.31.peg.3506; -.
DR   HOGENOM; CLU_007526_1_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; cd05154; ACAD10_11_N-like; 1.
DR   InterPro; IPR041726; ACAD10_11_N.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..378
FT                   /note="Putative aminoglycoside phosphotransferase"
FT                   /id="PRO_0000428044"
FT   ACT_SITE        249
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         134..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
SQ   SEQUENCE   378 AA;  42561 MW;  D1606BF6514E179A CRC64;
     MANEPAIGAI DRLQRSSRDV TTLPAVISRW LSSVLPGGAA PEVTVESGVD STGMSSETII
     LTARWQQDGR SIQQKLVARV APAAEDVPVF PTYRLDHQFE VIRLVGELTD VPVPRVRWIE
     TTGDVLGTPF FLMDYVEGVV PPDVMPYTFG DNWFADAPAE RQRQLQDATV AALATLHSIP
     NAQNTFSFLT QGRTSDTTLH RHFNWVRSWY DFAVEGIGRS PLLERTFEWL QSHWPDDAAA
     REPVLLWGDA RVGNVLYRDF QPVAVLDWEM VALGPRELDV AWMIFAHRVF QELAGLATLP
     GLPEVMREDD VRATYQALTG VELGDLHWFY VYSGVMWACV FMRTGARRVH FGEIEKPDDV
     ESLFYHAGLM KHLLGEEH