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Database: UniProt
Entry: Q671Q4_ACIBA
LinkDB: Q671Q4_ACIBA
Original site: Q671Q4_ACIBA 
ID   Q671Q4_ACIBA            Unreviewed;       263 AA.
AC   Q671Q4;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=aadA {ECO:0000313|EMBL:AAT51725.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:AAT51725.1};
RN   [1] {ECO:0000313|EMBL:AAT51725.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIPH 7 {ECO:0000313|EMBL:AAT51725.1};
RX   PubMed=15585503; DOI=10.1099/jmm.0.45716-0;
RA   Nemec A., Dolzani L., Brisse S., van den Broek P., Dijkshoorn L.;
RT   "Diversity of aminoglycoside-resistance genes and their association with
RT   class 1 integrons among strains of pan-European Acinetobacter baumannii
RT   clones.";
RL   J. Med. Microbiol. 53:1233-1240(2004).
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; AY577724; AAT51725.1; -; Genomic_DNA.
DR   RefSeq; WP_071846276.1; NG_052322.1.
DR   AlphaFoldDB; Q671Q4; -.
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}.
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;  29332 MW;  D2DB596B7D4025C8 CRC64;
     MREAVIAEVS TQLSEVVGVI ERHLEPTLLA VHLYGSAVDG GLKPHSDIDL LVTVTVRLDE
     TTRRALINDL LETSASPGES EILRAVEVTI VVHDDIIPWR YPAKRELQFG EWQRNDILAG
     IFEPATIDID LAILLTKARE HSVALVGPAA EELFDPVPEQ DLFEALNETL TLWNSPPDWA
     GDERNVVLTL SRIWYSAVTG QIAPKDVAAD WAMERLPAQY QPVILEARQA YLGQEEDRLA
     SRADQLEEFV HYVKGEITKV VGK
//
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