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
//