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Database: UniProt
Entry: B0BL05_ECOLX
LinkDB: B0BL05_ECOLX
Original site: B0BL05_ECOLX 
ID   B0BL05_ECOLX            Unreviewed;       259 AA.
AC   B0BL05;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=aadA1 {ECO:0000313|EMBL:CAP69683.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:CAP69683.1};
RN   [1] {ECO:0000313|EMBL:CAP69683.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=73 {ECO:0000313|EMBL:CAP69683.1};
RX   PubMed=18550679; DOI=10.1093/jac/dkn233;
RA   Kadlec K., Schwarz S.;
RT   "Analysis and distribution of class 1 and class 2 integrons and associated
RT   gene cassettes among Escherichia coli isolates from swine, horses, cats and
RT   dogs collected in the BfT-GermVet monitoring study.";
RL   J. Antimicrob. Chemother. 62:469-473(2008).
RN   [2] {ECO:0000313|EMBL:CAP69683.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=73 {ECO:0000313|EMBL:CAP69683.1};
RA   Schwarz S.P.;
RL   Submitted (JAN-2008) 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; AM932671; CAP69683.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0BL05; -.
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   Transferase {ECO:0000256|PIRNR:PIRNR000819, ECO:0000313|EMBL:CAP69683.1}.
FT   DOMAIN          24..72
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          148..250
FT                   /note="Adenylyltransferase AadA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13427"
SQ   SEQUENCE   259 AA;  28773 MW;  AEAC4DA6670141C5 CRC64;
     MIAEVSTQLS EVVGVIERHL EPTLLAVHLC GSAVDGGLKP HSDIDLLVTV TVRLDETTRR
     ALINDLLETS ASPGESEILR AVEVTIVVHD DIIPWRYPAK RELQFGEWQR NDILAGIFEP
     ATIDIDLAIL LTKAREHSVA LVGPAAEELF DPVPEQDLFE ALNETLTLWN SPPDWAGAER
     NVVLTLSRIW YSAVTGKIAP KDVAADWAME RLPAQYQPVI LEARQAYLGQ EEDRLASRAD
     QLEEFVHYVK GEITKVVGK
//
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