ID Q0PM59_VIBCL Unreviewed; 263 AA.
AC Q0PM59;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=aadA2 {ECO:0000313|EMBL:ABG88878.1};
OS Vibrio cholerae O139.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=45888 {ECO:0000313|EMBL:ABG88878.1};
RN [1] {ECO:0000313|EMBL:ABG88878.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=0419 {ECO:0000313|EMBL:ABG88878.1};
RX PubMed=18710912; DOI=10.1128/AAC.00375-08;
RA Pan J.C., Ye R., Wang H.Q., Xiang H.Q., Zhang W., Yu X.F., Meng D.M.,
RA He Z.S.;
RT "Vibrio cholerae O139 multiple-drug resistance mediated by Yersinia pestis
RT pIP1202-like conjugative plasmids.";
RL Antimicrob. Agents Chemother. 52:3829-3836(2008).
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; DQ789598; ABG88878.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0PM59; -.
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 ECO:0000313|EMBL:ABG88878.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR000819, ECO:0000313|EMBL:ABG88878.1}.
FT DOMAIN 28..97
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 153..254
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 263 AA; 29579 MW; DFBEB7184977FB26 CRC64;
MREAVTIEIS NQLSEVLSVI ERHLESTLLA VHLYGSAVDG GLKPYSDIDL LVTVAVKLDE
TTRRALLNDL MEASAFPGES ETLRAIEVTL VVHDDIIPWR YPAKRELQFG EWQRNDILAG
IFEPAMIDID LAILLTKARE HSVALVGPAA EEFFDPVPEQ DLFEALRETL KLWNSQPDWA
GDERNVVLTL SRIWYSAITG KIAPKDVAAD WAIKRLPAQY QPVLLEAKQA YLGQKEDHLA
SRADHLEEFI RFVKGEIIKS VGK
//
