ID G9FRL3_PROST Unreviewed; 263 AA.
AC G9FRL3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:AEW26716.1};
OS Providencia stuartii.
OG Plasmid IncA/C {ECO:0000313|EMBL:AEW26716.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=588 {ECO:0000313|EMBL:AEW26716.1};
RN [1] {ECO:0000313|EMBL:AEW26716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PsB/3 {ECO:0000313|EMBL:AEW26716.1};
RC PLASMID=IncA/C {ECO:0000313|EMBL:AEW26716.1};
RX PubMed=22155825; DOI=10.1128/AAC.05267-11;
RA Arpin C., Thabet L., Yassine H., Messadi A.A., Boukadida J., Dubois V.,
RA Coulange-Mayonnove L., Andre C., Quentin C.;
RT "Evolution of an Incompatibility Group IncA/C Plasmid Harboring blaCMY-16
RT and qnrA6 Genes and Its Transfer through Three Clones of Providencia
RT stuartii during a Two-Year Outbreak in a Tunisian Burn Unit.";
RL Antimicrob. Agents Chemother. 56:1342-1349(2012).
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; JN193567; AEW26716.1; -; Genomic_DNA.
DR RefSeq; WP_001209508.1; NZ_JALLDV010000066.1.
DR RefSeq; YP_005351816.1; NC_016974.1.
DR AlphaFoldDB; G9FRL3; -.
DR OMA; VRPWRYP; -.
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 Plasmid {ECO:0000313|EMBL:AEW26716.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR000819}.
FT DOMAIN 28..76
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 152..254
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 263 AA; 29360 MW; 1E9EAC8CDA103FDF CRC64;
MREVVIAEVS TQLSEVVGVI ERHLEPTLLA VHLYGSAVDG GLKPHSDIDL LVTVTVRLDE
TTRRALINDL LETSASPGES EILRAVEVTI VVHDDIIPWR YPAKRELQFG EWQRNDILAG
IFEPATIDID LAILLTKARE HSVALVGPAA EELFDPVPEQ DLFEALNETL TLWNSPPDWA
GDERNVVLTL SRIWYSAVTG KIAPKDVAAD WAMERLPAQY QPVILEARQA YLGQEEDRLA
SRADQLEEFV HYVKGEITKV VGK
//