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Database: UniProt
Entry: C5IKW3_9SPHI
LinkDB: C5IKW3_9SPHI
Original site: C5IKW3_9SPHI 
ID   C5IKW3_9SPHI            Unreviewed;       264 AA.
AC   C5IKW3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Aminoglycoside adenyltransferase {ECO:0000313|EMBL:ACS28596.1};
GN   Name=aadA2 {ECO:0000313|EMBL:ACS28596.1};
OS   Sphingobacterium sp. c49.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=646391 {ECO:0000313|EMBL:ACS28596.1};
RN   [1] {ECO:0000313|EMBL:ACS28596.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C49 {ECO:0000313|EMBL:ACS28596.1};
RX   PubMed=20400569; DOI=10.1128/AEM.02964-09;
RA   Li D., Yu T., Zhang Y., Yang M., Li Z., Liu M., Qi R.;
RT   "Antibiotic resistance characteristics of environmental bacteria from an
RT   oxytetracycline production wastewater treatment plant and the receiving
RT   river.";
RL   Appl. Environ. Microbiol. 76:3444-3451(2010).
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};
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DR   EMBL; FJ950722; ACS28596.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5IKW3; -.
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:ACS28596.1}.
FT   DOMAIN          29..98
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          154..255
FT                   /note="Adenylyltransferase AadA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13427"
SQ   SEQUENCE   264 AA;  29705 MW;  6D9F0C113360E620 CRC64;
     MEGKAWTIEI PNQLSEVLSV IERHLESTLL AVHLYGSAVD GGLKPYSDID LLVTVAVKLD
     ETTRRALLND LMEASAFPGE SETLRAIEVT LVVHDDIIPW RYPAKRELQF GEWQRNDILA
     GIFEPAMIDI DLAILLTKAR EHSVALVGPA AEEFFDPVPE QDLFEALRET LKLWNSQPDW
     AGDERNVVLT LSRIWYSAIT GKIAPKDVAA DWAIKRLPAQ YQPVLLEAKQ AYLGQKEDHL
     ASRADHLEEF IRFVKGEIIK SVGK
//
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