KKA2_KLEPN
ID KKA2_KLEPN Reviewed; 264 AA.
AC P00552; Q6LCR6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase;
DE EC=2.7.1.95;
DE AltName: Full=APH(3')-II;
DE Short=APH(3')II;
DE AltName: Full=Kanamycin kinase, type II;
DE AltName: Full=Neomycin-kanamycin phosphotransferase type II;
GN Name=neo; Synonyms=kan, nptII;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn5;
RX PubMed=6295884; DOI=10.1016/0378-1119(82)90023-3;
RA Beck E., Ludwig G., Auerswald E.A., Reiss B., Schaller H.;
RT "Nucleotide sequence and exact localization of the neomycin
RT phosphotransferase gene from transposon Tn5.";
RL Gene 19:327-336(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SM10; TRANSPOSON=Tn5;
RA Pinyon R.A., Thomas C.J.;
RT "DNA sequence of a mini-Tn5 transposon (mini-Tn5 Km).";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-264.
RC TRANSPOSON=Tn5;
RX PubMed=3889831; DOI=10.1093/nar/13.1.195;
RA Mazodier P., Cossart P., Giraud E., Gasser F.;
RT "Completion of the nucleotide sequence of the central region of Tn5
RT confirms the presence of three resistance genes.";
RL Nucleic Acids Res. 13:195-205(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH KANAMYCIN, AND ACTIVE
RP SITE.
RX PubMed=12628253; DOI=10.1016/s0022-2836(03)00121-9;
RA Nurizzo D., Shewry S.C., Perlin M.H., Brown S.A., Dholakia J.N.,
RA Fuchs R.L., Deva T., Baker E.N., Smith C.A.;
RT "The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an
RT enzyme responsible for antibiotic resistance.";
RL J. Mol. Biol. 327:491-506(2003).
CC -!- FUNCTION: Resistance to kanamycin, neomycin, paromomycin, ribostamycin,
CC butirosin and gentamicin B.
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 -!- MISCELLANEOUS: This enzyme is encoded by the kanamycin and neomycin
CC resistance transposon Tn5. Tn5 was originally isolated from
CC K.pneumoniae, but has been transferred to a number of bacteria
CC including E.coli.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; U00004; AAA73390.1; -; Unassigned_DNA.
DR EMBL; V00618; CAA23892.1; -; Genomic_DNA.
DR EMBL; U32991; AAA85506.1; -; Genomic_DNA.
DR EMBL; X01702; CAA25852.1; -; Genomic_DNA.
DR EMBL; U66885; AAC48873.1; -; Genomic_DNA.
DR PIR; A00663; PKECT5.
DR RefSeq; WP_000572405.1; NZ_VKSL01000036.1.
DR RefSeq; YP_008531444.1; NC_022333.1.
DR RefSeq; YP_788126.1; NC_008460.1.
DR PDB; 1ND4; X-ray; 2.10 A; A/B=1-264.
DR PDBsum; 1ND4; -.
DR AlphaFoldDB; P00552; -.
DR BMRB; P00552; -.
DR SMR; P00552; -.
DR GeneID; 61686716; -.
DR KEGG; ag:CAA23892; -.
DR EvolutionaryTrace; P00552; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase; Transposable element.
FT CHAIN 1..264
FT /note="Aminoglycoside 3'-phosphotransferase"
FT /id="PRO_0000204804"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12628253"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1ND4"
FT TURN 16..21
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1ND4"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1ND4"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1ND4"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1ND4"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1ND4"
SQ SEQUENCE 264 AA; 29048 MW; CB0507C1C30863BC CRC64;
MIEQDGLHAG SPAAWVERLF GYDWAQQTIG CSDAAVFRLS AQGRPVLFVK TDLSGALNEL
QDEAARLSWL ATTGVPCAAV LDVVTEAGRD WLLLGEVPGQ DLLSSHLAPA EKVSIMADAM
RRLHTLDPAT CPFDHQAKHR IERARTRMEA GLVDQDDLDE EHQGLAPAEL FARLKARMPD
GEDLVVTHGD ACLPNIMVEN GRFSGFIDCG RLGVADRYQD IALATRDIAE ELGGEWADRF
LVLYGIAAPD SQRIAFYRLL DEFF
