ID Q1DBM4_MYXXD Unreviewed; 272 AA.
AC Q1DBM4;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Aminoglycoside-3'-adenylyltransferase {ECO:0000313|EMBL:ABF86466.1};
GN OrderedLocusNames=MXAN_1698 {ECO:0000313|EMBL:ABF86466.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86466.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86466.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF86466.1; -; Genomic_DNA.
DR RefSeq; WP_011551808.1; NC_008095.1.
DR AlphaFoldDB; Q1DBM4; -.
DR STRING; 246197.MXAN_1698; -.
DR EnsemblBacteria; ABF86466; ABF86466; MXAN_1698.
DR GeneID; 41359136; -.
DR KEGG; mxa:MXAN_1698; -.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_071584_0_0_7; -.
DR OrthoDB; 7058480at2; -.
DR Proteomes; UP000002402; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 29..96
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 153..253
FT /note="Adenylyltransferase AadA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13427"
SQ SEQUENCE 272 AA; 30121 MW; 1B0C8BB14F730DA9 CRC64;
MNASVPTEIT HQVSSACSVI GRHLASSLQA IHLFGSAVDG GLKPHSDIDL LVTVSAPLTE
AVRHALLKEL LSVSTWPMTR ESLRPLEVTV VVRDAVVPWR YPPSRELQFG EWLRGEMEAG
HVQPAIVDPD LTILLAKARR HSICLLGEPA TDLFDPVPRT DLARAFYDTA LQWNEPADWR
GDERTVVLAL ARIWFSLSTG GIAPKDVAAQ WVIERLPDEH QSIMRSARAS YLGETQDDLA
RRGPEVAAFV HCARTAIERM YLEWQSGNPA AR
//
