ID H0FST9_RHIML Unreviewed; 258 AA.
AC H0FST9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase {ECO:0000256|ARBA:ARBA00035252};
DE EC=2.7.7.47 {ECO:0000256|ARBA:ARBA00035126};
GN ORFNames=SM0020_01020 {ECO:0000313|EMBL:EHK80039.1};
OS Sinorhizobium meliloti CCNWSX0020.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK80039.1, ECO:0000313|Proteomes:UP000004038};
RN [1] {ECO:0000313|EMBL:EHK80039.1, ECO:0000313|Proteomes:UP000004038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK80039.1,
RC ECO:0000313|Proteomes:UP000004038};
RX PubMed=22328762; DOI=10.1128/JB.06682-11;
RA Li Z., Ma Z., Hao X., Wei G.;
RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT Mine Tailings.";
RL J. Bacteriol. 194:1267-1268(2012).
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; AGVV01000001; EHK80039.1; -; Genomic_DNA.
DR RefSeq; WP_003525475.1; NZ_AGVV01000001.1.
DR AlphaFoldDB; H0FST9; -.
DR PATRIC; fig|1107881.3.peg.208; -.
DR Proteomes; UP000004038; Unassembled WGS sequence.
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 Nucleotidyltransferase {ECO:0000313|EMBL:EHK80039.1};
KW Transferase {ECO:0000313|EMBL:EHK80039.1}.
FT DOMAIN 18..77
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 152..251
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 258 AA; 28802 MW; 428ED09FEEC91E5B CRC64;
MRADRQQIDQ ALAATETIRS ILREALLAVY LHGSAVSGGL RPQSDVDLLA IVDCPVADEL
RRDLLAALLR ISGRHPRAVG TPRCIELMVF LRADIATPNF PVRAEFIYGE WLREAFESEE
LPVPVSDPEN TLVLAQARQE AVPLFGPDAK EFLPSIPPEQ VRRAMRDALP LLVDSLQGDE
RNVLLTLARM WRTSATGDFI TKDAAATWAA NQMPDQEAGT LIHAREAYLG KVRDDWENRQ
SASERTATFL RQRVLELL
//