ID A5YVZ0_SALTM Unreviewed; 263 AA.
AC A5YVZ0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252, ECO:0000256|PIRNR:PIRNR000819};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126, ECO:0000256|PIRNR:PIRNR000819};
GN Name=aadA2 {ECO:0000313|EMBL:ABQ96627.1};
OS Salmonella typhimurium.
OG Plasmid unnamed {ECO:0000313|EMBL:ABQ96627.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371 {ECO:0000313|EMBL:ABQ96627.1};
RN [1] {ECO:0000313|EMBL:ABQ96627.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=04-9275 {ECO:0000313|EMBL:ABQ96627.1};
RC PLASMID=unnamed {ECO:0000313|EMBL:ABQ96627.1};
RX PubMed=17698627; DOI=10.1128/AAC.00603-07;
RA Fernandez A.G., Cloeckaert A., Bertini A., Praud K., Doublet B.,
RA Weill F.X., Carattoli A.;
RT "Comparative analysis of IncHI2 plasmids carrying blaCTX-M-2 or blaCTX-M-9
RT from Escherichia coli and Salmonella enterica strains isolated from poultry
RT and humans.";
RL Antimicrob. Agents Chemother. 51:4177-4180(2007).
RN [2] {ECO:0000313|EMBL:ABQ96627.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=04-9275 {ECO:0000313|EMBL:ABQ96627.1};
RC PLASMID=unnamed {ECO:0000313|EMBL:ABQ96627.1};
RA Garcia Fernandez A., Cloeckaert A., Bertini A., Praud K., Doublet B.,
RA Weill F.-X., Carattoli A.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + spectinomycin = 9-O-adenylylspectinomycin + diphosphate;
CC Xref=Rhea:RHEA:63228, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:146260, ChEBI:CHEBI:146261;
CC Evidence={ECO:0000256|ARBA:ARBA00001672,
CC ECO:0000256|PIRNR:PIRNR000819};
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,
CC ECO:0000256|PIRNR:PIRNR000819};
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DR EMBL; EF592571; ABQ96627.1; -; Genomic_DNA.
DR RefSeq; WP_032491964.1; NG_052487.1.
DR AlphaFoldDB; A5YVZ0; -.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05403; NT_KNTase_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR024172; AadA/Aad9.
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 PIRSF; PIRSF000819; Streptomycin_3-adenylyltransf; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|PIRNR:PIRNR000819};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000819};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000819};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000819};
KW Plasmid {ECO:0000313|EMBL:ABQ96627.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR000819}.
FT DOMAIN 23..97
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 153..254
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 263 AA; 29551 MW; E7AEB7184F43696F CRC64;
MREAVTIEIS NQLSEVLSAI ERHLESTLLA VHLYGSAVDG GLKPYSDIDL LVTVAVKLDE
TTRRALLNDL MEASAFPGES ETLRAIEVTL VVHDDIIPWR YPAKRELQFG EWQRNDILAG
IFEPAMIDID LAILLTKARE HSVALVGPAA EEFFDPVPEQ DLFEALRETL KLWNSQPDWA
GDERNVVLTL SRIWYSAITG KIAPKDVAAD WAIKRLPAQY QPVLLEAKQA YLGQKEDHLA
SRADHLEEFI RFVKGEIIKS VGK
//