ID   S3AD_SHIFL              Reviewed;         262 AA.
AC   P0AG06; P04826;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase;
DE            EC=2.7.7.47 {ECO:0000269|PubMed:3517903};
DE   AltName: Full=Streptomycin 3''-adenylyltransferase;
GN   Name=aadA {ECO:0000303|PubMed:3517903};
OS   Shigella flexneri.
OG   Plasmid pCN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION IN
RP   SPECTINOMYCIN AND STREPTOMYCIN RESISTANCE, AND CATALYTIC ACTIVITY.
RC   STRAIN=Serotype 2a;
RX   PubMed=3517903; DOI=10.1016/0147-619x(86)90048-x;
RA   Chinault A.C., Blakesley V.A., Roessler E., Willis D.G., Smith C.A.,
RA   Cook R.G., Fenwick R.G. Jr.;
RT   "Characterization of transferable plasmids from Shigella flexneri 2a that
RT   confer resistance to trimethoprim, streptomycin, and sulfonamides.";
RL   Plasmid 15:119-131(1986).
CC   -!- FUNCTION: Mediates bacterial resistance to the antibiotics streptomycin
CC       and spectinomycin. {ECO:0000269|PubMed:3517903}.
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:0000269|PubMed:3517903};
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:0000305|PubMed:3517903};
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DR   EMBL; X03886; CAA27523.1; -; Genomic_DNA.
DR   RefSeq; WP_001206315.1; NZ_CP055221.1.
DR   AlphaFoldDB; P0AG06; -.
DR   SMR; P0AG06; -.
DR   GeneID; 79875491; -.
DR   OMA; SAIWIND; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Direct protein sequencing;
KW   Nucleotide-binding; Nucleotidyltransferase; Plasmid; Transferase.
FT   CHAIN           1..262
FT                   /note="Aminoglycoside (3'') (9) adenylyltransferase"
FT                   /id="PRO_0000068580"
SQ   SEQUENCE   262 AA;  29203 MW;  A2EEB1DBA6272F33 CRC64;
     MREAVIAEVS TQLSEVVGVI ERHLEPTLLA VHLYGSAVDG GLKPHSDIDL LVTVTVRLDE
     TTRRALINDL LETSASPGES EILRAVEVTI VVHDDIIPWR YPAKRELQFG EWQRNDILAG
     IFEPATIDID LAILLTKARE HSVALVGPAA EELFDPVPEQ DLFEALNETL TLWNSPPDWA
     GDERNVVLTL SRIWYSAVTG KIAPKDVAAD WAMERLPAQY QPVILEARQA YLGQEDRLAS
     RADQLEEFVH YVKGEITKVV GK
//