ID D7GKY3_PSEAI Unreviewed; 302 AA.
AC D7GKY3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN Name=aadA6 {ECO:0000313|EMBL:CBM56262.1};
OS Pseudomonas aeruginosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287 {ECO:0000313|EMBL:CBM56262.1};
RN [1] {ECO:0000313|EMBL:CBM56262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCR-Pae161 {ECO:0000313|EMBL:CBM56262.1};
RA Toval Maldonado F.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBM56262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCR-Pae161 {ECO:0000313|EMBL:CBM56262.1};
RA Toval-Maldonado F., Rodriguez-Sanchez C., Somogyi T., Madriz V., Garcia F.;
RT "Simultaneous detection of IMP and VIM metallo-beta-lactamase genes in
RT carbapenem-resistant isolates of Pseudomonas aeruginosa from a national
RT hospital in Costa Rica.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN823040; CBM56262.1; -; Genomic_DNA.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
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 Nucleotidyltransferase {ECO:0000313|EMBL:CBM56262.1};
KW Transferase {ECO:0000313|EMBL:CBM56262.1}.
SQ SEQUENCE 302 AA; 33194 MW; 96220E6AC1F5E381 CRC64;
MLWSSNDVTQ QGSRPKTKLD IMSNAVPAEI SVQLSLALNA IERHLESTLL AVHLYGSALD
GGLKPYSDID LLVTVAARLD ETVRQALVVD LLEISASPGQ SEALRALEVT IVVHGDVVPW
RYPARRELQF GEWQRKDILA GIFEPATTDV DLAILLTKVR QHSLALAGSA AEDFFNPVPE
GDLFKALSDT LKLWNSQPDW EGDERNVVLT LSRIWYSAAT GKIAPKDIVA NWAMERLPDQ
HKPVLLEARQ AYLGQGEDCL ASRADQLAAF VHFVKHEATK LLSAMPVMSN NSFKPTPLRG
AA
//