ID G0XBF1_ECOLX Unreviewed; 301 AA.
AC G0XBF1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN Name=aadA {ECO:0000313|EMBL:ADM62839.1};
GN ORFNames=pAPEC1990_61_125 {ECO:0000313|EMBL:ADM62839.1};
OS Escherichia coli.
OG Plasmid pAPEC1990_61 {ECO:0000313|EMBL:ADM62839.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ADM62839.1};
RN [1] {ECO:0000313|EMBL:ADM62839.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=APEC1990_61 {ECO:0000313|EMBL:ADM62839.1};
RC PLASMID=pAPEC1990_61 {ECO:0000313|EMBL:ADM62839.1};
RA Fernandez-Alarcon C.L., Johnson T.J., Nolan L.K., Singer R.S.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM62839.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=APEC1990_61 {ECO:0000313|EMBL:ADM62839.1};
RC PLASMID=pAPEC1990_61 {ECO:0000313|EMBL:ADM62839.1};
RX PubMed=21858108; DOI=10.1371/journal.pone.0023415;
RA Fernandez-Alarcon C., Singer R.S., Johnson T.J.;
RT "Comparative Genomics of Multidrug Resistance-Encoding IncA/C Plasmids from
RT Commensal and Pathogenic Escherichia coli from Multiple Animal Sources.";
RL PLoS ONE 6:E23415-E23415(2011).
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 -!- 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};
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DR EMBL; HQ023863; ADM62839.1; -; Genomic_DNA.
DR RefSeq; YP_006952971.1; NC_019066.1.
DR AlphaFoldDB; G0XBF1; -.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
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 Plasmid {ECO:0000313|EMBL:ADM62839.1}.
FT DOMAIN 64..113
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 190..292
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 301 AA; 33707 MW; EBF24D7FF933E38E CRC64;
MPRASKQQAR YAVGRCLMLW SSNDVTQQGS RPKTKLDIMR VAVTIEISNQ LSEVLSVIER
HLEPTLLAVH LYGSAVDGGL KPHSDIDLLV TVTVRLDETT RRALINDLLE TSASPGESEI
LRAVEVTIVV HDDIIPWRYP AKRELQFGEW QRNDILAGIF EPATIDIDLA ILLTKAREHS
VALVGPAAEE LFDPVPEQDL FEALNETLTL WNSPPDWAGD ERNVVLTLSR IWYSAVTGKI
APKDVAADWA MERLPAQYQP VILEARQAYL GQEEDRLASR ADQLEEFVHY VKGEITKVVG
K
//