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Database: UniProt
Entry: G0XBF1_ECOLX
LinkDB: G0XBF1_ECOLX
Original site: G0XBF1_ECOLX 
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
//
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