ID A4SU28_AERS4 Unreviewed; 335 AA.
AC A4SU28;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN Name=aadA {ECO:0000313|EMBL:ABO92400.1};
GN OrderedLocusNames=ASA_P4G100 {ECO:0000313|EMBL:ABO92400.1};
OS Aeromonas salmonicida (strain A449).
OG Plasmid pAsa4 {ECO:0000313|Proteomes:UP000000225}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO92400.1, ECO:0000313|Proteomes:UP000000225};
RN [1] {ECO:0000313|Proteomes:UP000000225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RC PLASMID=pAsa4 {ECO:0000313|Proteomes:UP000000225};
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000645; ABO92400.1; -; Genomic_DNA.
DR AlphaFoldDB; A4SU28; -.
DR KEGG; asa:ASA_P4G100; -.
DR HOGENOM; CLU_071584_0_0_6; -.
DR OMA; VRPWRYP; -.
DR Proteomes; UP000000225; Plasmid pAsa4.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:ABO92400.1};
KW Transferase {ECO:0000313|EMBL:ABO92400.1}.
FT DOMAIN 100..146
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 224..326
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 335 AA; 37494 MW; 095A2D4E13D0322C CRC64;
MRSRNWSRTL TERSGGNGAV AVFMACYDCF FVQSMPRASK QQARYAVGRC LMLWSSNDVT
QQGSRPKTKL NIMREAVIAE VSTQLSEVVG VIERHLEPTL LAVHLYGSAV DGGLKPHSDI
DLLVTVTVRL DETTRRALIN DLLETSASPG ESEILRAVEV TIVVHDDIIP WRYPAKRELQ
FGEWQRNDIL AGIFEPATID IDLAILLTKA REHSVALVGP AAEELFDPVP EQDLFEALNE
TLTLWNSPPD WAGDERNVVL TLSRIWYSAV TGRIAPKDVA ADWAMERLPA QYQPVILEAR
QAYLGQEEDR LASRADQLEE FVHYVKGEIT KVVGK
//