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Database: UniProt
Entry: D7PM75_9NEIS
LinkDB: D7PM75_9NEIS
Original site: D7PM75_9NEIS 
ID   D7PM75_9NEIS            Unreviewed;       259 AA.
AC   D7PM75;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE            EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN   Name=aadA1 {ECO:0000313|EMBL:ADI46753.1};
OS   Laribacter hongkongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=168471 {ECO:0000313|EMBL:ADI46753.1};
RN   [1] {ECO:0000313|EMBL:ADI46753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LHW350 {ECO:0000313|EMBL:ADI46753.1};
RA   Feng J., Chen Q., Hu J.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI46753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LHW350 {ECO:0000313|EMBL:ADI46753.1};
RX   PubMed=21075469; DOI=10.1016/j.ijfoodmicro.2010.10.014;
RA   Feng J.L., Yan H., Chowdhury N., Neogi S.B., Yamasaki S., Shi L., Hu J.,
RA   Chen Q.;
RT   "Identification and characterization of integron-associated antibiotic
RT   resistant Laribacter hongkongensis isolated from aquatic products in
RT   China.";
RL   Int. J. Food Microbiol. 144:337-341(2011).
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};
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DR   EMBL; GU726914; ADI46753.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PM75; -.
DR   SMR; D7PM75; -.
DR   GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
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   Transferase {ECO:0000313|EMBL:ADI46753.1}.
FT   DOMAIN          24..93
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          149..250
FT                   /note="Adenylyltransferase AadA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13427"
SQ   SEQUENCE   259 AA;  29123 MW;  259A643BC501E75D CRC64;
     MTIEISNQLS EVLSVIERHL ESTLLAVHLY GSAVDGGLKP YSDIDLLVTV AVKLDETTRR
     ALLNDLMEAS AFPGESETLR AIEVTLVVHD DIIPWRYPAK RELQFGEWQR NDILAGIFEP
     AMIDIDLAIL LTKAREHSVA LVGPAAEEFF DPVPEQDLFE ALRETLKLWN SQPDWAGDER
     NVVLTLSRIW YSAITGKIAP KDVAADWAIK RLPAQYQPVL LEAKQAYLGQ KEDHLASRAD
     HLEEFIRFVK GEIIKSVGK
//
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