ID Q75T47_SALEN Unreviewed; 262 AA.
AC Q75T47; Q75TK7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN Name=aadA5 {ECO:0000313|EMBL:BAD07296.1};
GN ORFNames=BSD63_23490 {ECO:0000313|EMBL:ECT8140419.1}, BSD63_24025
GN {ECO:0000313|EMBL:ECT8140516.1};
OS Salmonella enteritidis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539 {ECO:0000313|EMBL:BAD07296.1};
RN [1] {ECO:0000313|EMBL:BAD07296.1}
RP NUCLEOTIDE SEQUENCE.
RA Izumiya H., Nojiri N., Tanaka R., Hashiwata Y., Watanabe H.;
RT "A class 1 integron identified in Slamonella Enteritidis.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAD02332.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=O2L-17 {ECO:0000313|EMBL:BAD02332.1};
RX PubMed=15705645; DOI=10.1093/jac/dkh534;
RA Ahmed A.M., Nakano H., Shimamoto T.;
RT "Molecular characterization of integrons in non-typhoid Salmonella serovars
RT isolated in Japan: description of an unusual class 2 integron.";
RL J. Antimicrob. Chemother. 55:371-374(2005).
RN [3] {ECO:0000313|EMBL:ECT8140419.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2014AM-0699 {ECO:0000313|EMBL:ECT8140419.1};
RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance;
RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S.,
RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AXY40433.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SH11G072 {ECO:0000313|EMBL:AXY40433.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate;
CC Xref=Rhea:RHEA:20245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58007, ChEBI:CHEBI:58605; EC=2.7.7.47;
CC Evidence={ECO:0000256|ARBA:ARBA00035070};
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DR EMBL; MH681802; AXY40433.1; -; Genomic_DNA.
DR EMBL; AB126604; BAD02332.1; -; Genomic_DNA.
DR EMBL; AB127354; BAD07296.1; -; Genomic_DNA.
DR EMBL; AAKNYV010000012; ECT8140419.1; -; Genomic_DNA.
DR EMBL; AAKNYV010000018; ECT8140516.1; -; Genomic_DNA.
DR AlphaFoldDB; Q75T47; -.
DR SMR; Q75T47; -.
DR GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd05403; NT_KNTase_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR025184; AadA_C.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF13427; AadA_C; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:AXY40433.1};
KW Transferase {ECO:0000313|EMBL:BAD07296.1}.
FT DOMAIN 29..59
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 153..255
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 262 AA; 29042 MW; 94DD4B1AD7941B1C CRC64;
MGEFFPAQVF KQLSHARAVI ERHLAATLDT IHLFGSAIDG GLKPDSDIDL LVTVSAAPND
SLRQALMLDL LKVSSPPGDG GTWRPLELTV VARSEVVPWR YPARRELQFG EWLRHDILSG
TFEPAVLDHD LAILLTKARQ HSLALLGPSA ATFFEPVPKE HFSKALFDTI AQWNAESDWK
GDERNVVLAL ARIWYSASTG LIAPKDVAAA WVSERLPAEH RPLICKARAA YLGSEDDDLA
MRVEETAAFV RYAKATIERI LR
//