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Database: UniProt
Entry: H0FST9_RHIML
LinkDB: H0FST9_RHIML
Original site: H0FST9_RHIML 
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
//
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