KKA3_ENTFL
ID KKA3_ENTFL Reviewed; 264 AA.
AC P0A3Y5; P00554;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase;
DE EC=2.7.1.95;
DE AltName: Full=APH(3')III;
DE AltName: Full=Kanamycin kinase, type III;
DE AltName: Full=Neomycin-kanamycin phosphotransferase type III;
GN Name=aphA;
OS Enterococcus faecalis (Streptococcus faecalis).
OG Plasmid pJH1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6313476; DOI=10.1016/0378-1119(83)90022-7;
RA Trieu-Cuot P., Courvalin P.;
RT "Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding
RT the 3'5'-aminoglycoside phosphotransferase type III.";
RL Gene 23:331-341(1983).
CC -!- FUNCTION: Resistance to kanamycin and structurally-related
CC aminoglycosides, including amikacin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate;
CC Xref=Rhea:RHEA:24256, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57909, ChEBI:CHEBI:58214, ChEBI:CHEBI:456216;
CC EC=2.7.1.95;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; V01547; CAA24789.1; -; Genomic_DNA.
DR EMBL; X99398; CAA67773.1; -; Genomic_DNA.
DR PIR; A00665; PKSOJF.
DR RefSeq; WP_001096887.1; NZ_WYAD01000043.1.
DR RefSeq; YP_783930.1; NC_008445.1.
DR PDB; 1J7I; X-ray; 3.20 A; A=1-264.
DR PDB; 1J7L; X-ray; 2.20 A; A/B=1-264.
DR PDB; 1J7U; X-ray; 2.40 A; A/B=1-264.
DR PDB; 1L8T; X-ray; 2.40 A; A=2-264.
DR PDB; 2B0Q; X-ray; 2.70 A; A=2-264.
DR PDB; 2BKK; X-ray; 2.15 A; A/C=1-264.
DR PDB; 3Q2J; X-ray; 2.15 A; A/B=1-264.
DR PDB; 3TM0; X-ray; 2.10 A; A=2-264.
DR PDBsum; 1J7I; -.
DR PDBsum; 1J7L; -.
DR PDBsum; 1J7U; -.
DR PDBsum; 1L8T; -.
DR PDBsum; 2B0Q; -.
DR PDBsum; 2BKK; -.
DR PDBsum; 3Q2J; -.
DR PDBsum; 3TM0; -.
DR AlphaFoldDB; P0A3Y5; -.
DR BMRB; P0A3Y5; -.
DR SMR; P0A3Y5; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR PRIDE; P0A3Y5; -.
DR GeneID; 63968956; -.
DR GeneID; 67042600; -.
DR KEGG; ag:CAA24789; -.
DR OrthoDB; 1457558at2; -.
DR BRENDA; 2.7.1.95; 2095.
DR SABIO-RK; P0A3Y5; -.
DR EvolutionaryTrace; P0A3Y5; -.
DR PRO; PR:P0A3Y5; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
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 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; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Kinase;
KW Nucleotide-binding; Plasmid; Transferase.
FT CHAIN 1..264
FT /note="Aminoglycoside 3'-phosphotransferase"
FT /id="PRO_0000204805"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3TM0"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3TM0"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3TM0"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:3TM0"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3TM0"
SQ SEQUENCE 264 AA; 30974 MW; 7EEA5851D3380C5A CRC64;
MAKMRISPEL KKLIEKYRCV KDTEGMSPAK VYKLVGENEN LYLKMTDSRY KGTTYDVERE
KDMMLWLEGK LPVPKVLHFE RHDGWSNLLM SEADGVLCSE EYEDEQSPEK IIELYAECIR
LFHSIDISDC PYTNSLDSRL AELDYLLNND LADVDCENWE EDTPFKDPRE LYDFLKTEKP
EEELVFSHGD LGDSNIFVKD GKVSGFIDLG RSGRADKWYD IAFCVRSIRE DIGEEQYVEL
FFDLLGIKPD WEKIKYYILL DELF
