ID C4L4H8_EXISA Unreviewed; 258 AA.
AC C4L4H8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Spectinomycin 9-adenylyltransferase {ECO:0000256|PIRNR:PIRNR000819};
GN OrderedLocusNames=EAT1b_2625 {ECO:0000313|EMBL:ACQ71541.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ71541.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ71541.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(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 ECO:0000256|PIRNR:PIRNR000819};
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DR EMBL; CP001615; ACQ71541.1; -; Genomic_DNA.
DR RefSeq; WP_015881100.1; NC_012673.1.
DR AlphaFoldDB; C4L4H8; -.
DR STRING; 360911.EAT1b_2625; -.
DR KEGG; eat:EAT1b_2625; -.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_071584_1_0_9; -.
DR OrthoDB; 5643411at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ECO:0000256|PIRNR:PIRNR000819};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000819};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000819};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000819};
KW Transferase {ECO:0000256|PIRNR:PIRNR000819}.
FT DOMAIN 15..99
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; 30008 MW; E7D7B01A4DCF8D90 CRC64;
MRQITTDVEN TIASFVRAID EFLPTVQHIY IHGSLAMGGF HPKRSDVDLL LVVSNALTRE
ERQKLIDCCL SYSNEPYPLE LSIMTMAQLE DWYHPSPFEF HYSEGWRSRF EEASREERTE
LQQGFTDPDL AAHVLVILER GITWRGQPLH KLLSGFDSAH FSDAIRADAL DCLDSIEEQT
VYSVLNLIRG LAYEQERVLL SKQEALHWLV KNGHFPGNIV EVVRKATRNY EGGSVTFHRQ
ELNEFRRYMR QQLQRKQK
//
