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Database: UniProt
Entry: A5YVZ0_SALTM
LinkDB: A5YVZ0_SALTM
Original site: A5YVZ0_SALTM 
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
//
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