ID B0VNI2_ACIBS Unreviewed; 262 AA.
AC B0VNI2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN OrderedLocusNames=ABSDF0145 {ECO:0000313|EMBL:CAO99552.1};
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAO99552.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAO99552.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAO99552.1,
RC ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(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};
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DR EMBL; CU468230; CAO99552.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VNI2; -.
DR KEGG; abm:ABSDF0145; -.
DR HOGENOM; CLU_071584_0_0_6; -.
DR OMA; QQDWDIV; -.
DR BioCyc; ABAU509170:GCL9-127-MONOMER; -.
DR Proteomes; UP000001741; Chromosome.
DR GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
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; IPR041633; Polbeta.
DR Pfam; PF13427; AadA_C; 1.
DR Pfam; PF18765; Polbeta; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAO99552.1};
KW Transferase {ECO:0000313|EMBL:CAO99552.1}.
FT DOMAIN 12..84
FT /note="Polymerase beta nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF18765"
FT DOMAIN 147..247
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 262 AA; 30264 MW; 01E312B10D319F8A CRC64;
MSDFIQLEYL QEKLQQLLAE SLFAIYLYGS AVDGGLGPES DLDVLVVVTQ PLTSALREQL
AQELLKISQP VGELQRPLEV TILLKDEIQS GNYPLSYEMQ FGEWLREELK EGGTLSSQKD
PDISILLRKA RFHHTVLFGP ALDQWAPEIS DQELWQAMSD TYPEIVAHWD EDADERNQIL
ALCRIYFSLV MKDIASKDNA ARWVMPQLPP EQKFVLQRLI QEYRGEIGKQ NWQEEHYALQ
PIVNFLSSKI EEQFEQKRNL IT
//