ID U5W890_9ACTN Unreviewed; 231 AA.
AC U5W890;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Aminoglycoside phosphotransferase {ECO:0000313|EMBL:AGZ44190.1};
GN ORFNames=AFR_29645 {ECO:0000313|EMBL:AGZ44190.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ44190.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ44190.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ44190.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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DR EMBL; CP006272; AGZ44190.1; -; Genomic_DNA.
DR RefSeq; WP_023560527.1; NC_022657.1.
DR AlphaFoldDB; U5W890; -.
DR STRING; 1246995.AFR_29645; -.
DR KEGG; afs:AFR_29645; -.
DR PATRIC; fig|1246995.3.peg.6009; -.
DR eggNOG; COG3231; Bacteria.
DR HOGENOM; CLU_073027_0_1_11; -.
DR OrthoDB; 3806873at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05150; APH; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR024165; Kan/Strep_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Transferase {ECO:0000313|EMBL:AGZ44190.1}.
FT DOMAIN 21..196
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 231 AA; 25195 MW; 1DE29A58B2BEC30C CRC64;
MWEIVTTGQS GATVSRRDGV YRKTSNDPRD DLPGEAARLT WLRAHGIPAA QVLSSAPGLL
ETAEVPGLPA SDYRHGVVDA LADFTRVLHA LPIADCPFDR RLAVTIPAAL AADVDLDDLD
DERAGWTRDE LVAQLHATRP VQEDLVVCHG DLCLPNVVLD REGSQVTGLI DVGRLGVADR
WTDLALMTRS LSDPGLNPGY GPWAADRFLT RYGIAPDPAK NDFYRLLDEF F
//
