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Database: UniProt
Entry: D0EZK3_STEMA
LinkDB: D0EZK3_STEMA
Original site: D0EZK3_STEMA 
ID   D0EZK3_STEMA            Unreviewed;       262 AA.
AC   D0EZK3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE            EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN   Name=aadA5 {ECO:0000313|EMBL:ACX53635.1};
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324 {ECO:0000313|EMBL:ACX53635.1};
RN   [1] {ECO:0000313|EMBL:ACX53635.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=315 {ECO:0000313|EMBL:ACX53635.1};
RA   hu L., Li J., Li X.;
RT   "direct submission.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACX53635.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=315 {ECO:0000313|EMBL:ACX53635.1};
RX   PubMed=21296557; DOI=10.1016/j.ijantimicag.2010.10.025;
RA   Hu L.F., Chang X., Ye Y., Wang Z.X., Shao Y.B., Shi W., Li X., Li J.B.;
RT   "Stenotrophomonas maltophilia resistance to trimethoprim/sulfamethoxazole
RT   mediated by acquisition of sul and dfrA genes in a plasmid-mediated class 1
RT   integron.";
RL   Int. J. Antimicrob. Agents 37:230-234(2011).
RN   [3] {ECO:0000313|EMBL:AIX48133.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T-B7D {ECO:0000313|EMBL:AIX48133.1};
RA   Liang J., Lin M.;
RT   "Investigation in the Spread of Antibiotic-resistant Bacteria in the
RT   Jiulong River.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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; GQ924479; ACX53635.1; -; Genomic_DNA.
DR   EMBL; KM278176; AIX48133.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0EZK3; -.
DR   SMR; D0EZK3; -.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd05403; NT_KNTase_like; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
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   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE   4: Predicted;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ACX53635.1};
KW   Transferase {ECO:0000313|EMBL:ACX53635.1}.
FT   DOMAIN          29..59
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          153..255
FT                   /note="Adenylyltransferase AadA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13427"
SQ   SEQUENCE   262 AA;  29042 MW;  94DD4B1AD7941B1C CRC64;
     MGEFFPAQVF KQLSHARAVI ERHLAATLDT IHLFGSAIDG GLKPDSDIDL LVTVSAAPND
     SLRQALMLDL LKVSSPPGDG GTWRPLELTV VARSEVVPWR YPARRELQFG EWLRHDILSG
     TFEPAVLDHD LAILLTKARQ HSLALLGPSA ATFFEPVPKE HFSKALFDTI AQWNAESDWK
     GDERNVVLAL ARIWYSASTG LIAPKDVAAA WVSERLPAEH RPLICKARAA YLGSEDDDLA
     MRVEETAAFV RYAKATIERI LR
//
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