ID I3I9R0_9GAMM Unreviewed; 248 AA.
AC I3I9R0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=O59_002518 {ECO:0000313|EMBL:EIK44795.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK44795.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK44795.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK44795.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIK44795.1}.
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DR EMBL; AICM01000004; EIK44795.1; -; Genomic_DNA.
DR AlphaFoldDB; I3I9R0; -.
DR STRING; 1134474.O59_002518; -.
DR PATRIC; fig|1134474.3.peg.2361; -.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_071584_0_0_6; -.
DR Proteomes; UP000003395; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EIK44795.1}.
FT DOMAIN 14..82
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 138..239
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 248 AA; 27909 MW; 8C3AB2FF97982DCA CRC64;
MLSVIERHLE STLLAVHLYG SAVDGGLKPY SDIDLLVTVA VKLDETTRRA LLNDLMEASA
FPGESETLRA IEVTLVVHDD IIPWRYPAKR ELQFGEWQRN DILAGIFEPA MIDIDLAILL
TKAREHSVAL VGPAAEEFFD PVPEQDLFEA LRETLKLWNS QPDWAGDERN VVLTLSRIWY
SAITGKIAPK DVAADWAIKR LPAQYQPVLL EAKQAYLGQK EDHLASRADH LEEFIRFVKG
EIIKSVGK
//
