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Bifunctional AAC/APH [Includes: 6'-aminoglycoside N-acetyltransferase (EC 2.3.1.-) (AAC(6')); Aminoglycoside 2''-phosphotransferase (EC 2.7.1.190) (2''-aminoglycoside phosphotransferase) (APH(2''))]

 AACA_ENTFA              Reviewed;         479 AA.
P0A0C2; P14507;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
22-NOV-2017, entry version 82.
RecName: Full=Bifunctional AAC/APH;
Includes:
RecName: Full=6'-aminoglycoside N-acetyltransferase;
EC=2.3.1.-;
AltName: Full=AAC(6');
Includes:
RecName: Full=Aminoglycoside 2''-phosphotransferase {ECO:0000305};
EC=2.7.1.190 {ECO:0000269|PubMed:23115238};
AltName: Full=2''-aminoglycoside phosphotransferase;
AltName: Full=APH(2'');
Name=aacA-aphD; OrderedLocusNames=EF_A0061;
Enterococcus faecalis (strain ATCC 700802 / V583).
Plasmid pIP800, and Plasmid pTEF1.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
Enterococcus.
NCBI_TaxID=226185;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pIP800;
PubMed=3015884; DOI=10.1128/jb.167.2.631-638.1986;
Ferretti J.J., Gilmore K.S., Courvalin P.;
"Nucleotide sequence analysis of the gene specifying the bifunctional
6'-aminoglycoside acetyltransferase 2'-aminoglycoside
phosphotransferase enzyme in Streptococcus faecalis and identification
and cloning of gene regions specifying the two activities.";
J. Bacteriol. 167:631-638(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700802 / V583; PLASMID=pTEF1;
PubMed=12663927; DOI=10.1126/science.1080613;
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
Fraser C.M.;
"Role of mobile DNA in the evolution of vancomycin-resistant
Enterococcus faecalis.";
Science 299:2071-2074(2003).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=23115238; DOI=10.1074/jbc.M112.416453;
Frase H., Toth M., Vakulenko S.B.;
"Revisiting the nucleotide and aminoglycoside substrate specificity of
the bifunctional aminoglycoside acetyltransferase(6')-
Ie/aminoglycoside phosphotransferase(2'')-Ia enzyme.";
J. Biol. Chem. 287:43262-43269(2012).
-!- FUNCTION: Involved in resistance to gentamicin, tobramycin, and
kanamycin. Tobramycin and kanamycin resistance is due to the ACC
activity, specified by N-terminal region. The C-terminal region is
a kinase that phosphorylates several 4,6-disubstituted
aminoglycosides. {ECO:0000269|PubMed:23115238}.
-!- CATALYTIC ACTIVITY: GTP + gentamicin = GDP + gentamicin 2''-
phosphate. {ECO:0000269|PubMed:23115238}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3 uM for GTP {ECO:0000269|PubMed:23115238};
KM=0.3 uM for dibekacin {ECO:0000269|PubMed:23115238};
KM=0.8 uM for arbekacin {ECO:0000269|PubMed:23115238};
KM=33 uM for amikacin {ECO:0000269|PubMed:23115238};
KM=0.6 uM for gentamicin C {ECO:0000269|PubMed:23115238};
KM=0.8 uM for sisomicin {ECO:0000269|PubMed:23115238};
KM=0.41 uM for netilmicin {ECO:0000269|PubMed:23115238};
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: In the C-terminal section; belongs to the
aminoglycoside phosphotransferase family. {ECO:0000305}.
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EMBL; M13771; AAA26865.1; -; Genomic_DNA.
EMBL; AE016833; AAO83055.1; -; Genomic_DNA.
PIR; A26048; A26048.
RefSeq; NP_816984.1; NC_004669.1.
RefSeq; WP_001028144.1; NZ_KE136530.1.
ProteinModelPortal; P0A0C2; -.
SMR; P0A0C2; -.
EnsemblBacteria; AAO83055; AAO83055; EF_A0061.
GeneID; 1202231; -.
GeneID; 31633730; -.
KEGG; ag:AAA26865; -.
KEGG; efa:EFA0061; -.
PATRIC; fig|226185.45.peg.2781; -.
KO; K19883; -.
OMA; YDGRDKK; -.
BioCyc; MetaCyc:MONOMER-19347; -.
SABIO-RK; P0A0C2; -.
PRO; PR:P0A0C2; -.
Proteomes; UP000001415; Plasmid pTEF1.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR002575; Aminoglycoside_PTrfase.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
Pfam; PF01636; APH; 1.
SUPFAM; SSF55729; SSF55729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Antibiotic resistance; ATP-binding;
Complete proteome; Cytoplasm; Kinase; Multifunctional enzyme;
Nucleotide-binding; Plasmid; Reference proteome; Transferase;
Transposable element.
CHAIN 1 479 Bifunctional AAC/APH.
/FTId=PRO_0000204796.
DOMAIN 8 180 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 110 153 Acetyl-CoA binding site. {ECO:0000250}.
ACT_SITE 374 374 Proton acceptor; for phosphotransferase
activity. {ECO:0000250}.
BINDING 393 393 Aminoglycoside substrate. {ECO:0000250}.
SEQUENCE 479 AA; 56855 MW; 744D93D76299CFCE CRC64;
MNIVENEICI RTLIDDDFPL MLKWLTDERV LEFYGGRDKK YTLESLKKHY TEPWEDEVFR
VIIEYNNVPI GYGQIYKMYD ELYTDYHYPK TDEIVYGMDQ FIGEPNYWSK GIGTRYIKLI
FEFLKKERNA NAVILDPHKN NPRAIRAYQK SGFRIIEDLP EHELHEGKKE DCYLMEYRYD
DNATNVKAMK YLIEHYFDNF KVDSIEIIGS GYDSVAYLVN NEYIFKTKFS TNKKKGYAKE
KAIYNFLNTN LETNVKIPNI EYSYISDELS ILGYKEIKGT FLTPEIYSTM SEEEQNLLKR
DIASFLRQMH GLDYTDISEC TIDNKQNVLE EYILLRETIY NDLTDIEKDY IESFMERLNA
TTVFEGKKCL CHNDFSCNHL LLDGNNRLTG IIDFGDSGII DEYCDFIYLL EDSEEEIGTN
FGEDILRMYG NIDIEKAKEY QDIVEEYYPI ETIVYGIKNI KQEFIENGRK EIYKRTYKD


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