KHYB_ECOLX
ID KHYB_ECOLX Reviewed; 341 AA.
AC P00557;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Hygromycin-B 4-O-kinase;
DE EC=2.7.1.163;
DE AltName: Full=APH(4);
DE AltName: Full=Hygromycin B phosphotransferase;
DE AltName: Full=Hygromycin-B kinase;
GN Name=hph;
OS Escherichia coli.
OG Plasmid pKC222, and Plasmid pJR225.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pKC222;
RX PubMed=6314265; DOI=10.1093/nar/11.19.6895;
RA Kaster K.R., Burgett S.G., Rao R.N., Ingolia T.D.;
RT "Analysis of a bacterial hygromycin B resistance gene by transcriptional
RT and translational fusions and by DNA sequencing.";
RL Nucleic Acids Res. 11:6895-6911(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJR225;
RX PubMed=6319235; DOI=10.1016/0378-1119(83)90223-8;
RA Gritz L., Davies J.;
RT "Plasmid-encoded hygromycin B resistance: the sequence of hygromycin B
RT phosphotransferase gene and its expression in Escherichia coli and
RT Saccharomyces cerevisiae.";
RL Gene 25:179-188(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=6318050; DOI=10.1007/bf00327434;
RA Braeu B., Pilz U., Piepersberg W.;
RT "Genes for gentamicin-(3)-N-acetyltransferases III and IV: I. Nucleotide
RT sequence of the AAC(3)-IV gene and possible involvement of an IS140 element
RT in its expression.";
RL Mol. Gen. Genet. 193:179-187(1984).
RN [4]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC PLASMID=pJR225;
RX PubMed=6318654; DOI=10.1128/aac.24.5.689;
RA Rao R.N., Allen N.E., Hobbs J.N. Jr., Alborn W.E. Jr., Kirst H.A.,
RA Paschal J.W.;
RT "Genetic and enzymatic basis of hygromycin B resistance in Escherichia
RT coli.";
RL Antimicrob. Agents Chemother. 24:689-695(1983).
CC -!- FUNCTION: The aminoglycoside phosphotransferases achieve inactivation
CC of their antibiotic substrates by phosphorylation. Only phosphorylates
CC hygromycin and closely related compounds such as demethyl analogs and
CC destomycin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hygromycin B = 4-O-phosphohygromycin B + ADP + H(+);
CC Xref=Rhea:RHEA:26064, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57971, ChEBI:CHEBI:59917, ChEBI:CHEBI:456216;
CC EC=2.7.1.163; Evidence={ECO:0000269|PubMed:6318654};
CC -!- MISCELLANEOUS: Hygromycin B resistant E.coli were found to contain a
CC Klebsiella derived plasmid, pJR225. This plasmid contains the hph gene.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; K01193; AAA92252.1; -; Genomic_DNA.
DR EMBL; V01499; CAA24743.1; -; Genomic_DNA.
DR EMBL; X01385; CAA25643.1; -; Genomic_DNA.
DR EMBL; X89856; CAA61952.1; -; Genomic_DNA.
DR EMBL; X89857; CAA61953.1; -; Genomic_DNA.
DR PIR; A00668; WGECH.
DR PIR; S09645; S09645.
DR RefSeq; WP_000742814.1; NZ_WVVZ01000066.1.
DR RefSeq; YP_006952299.1; NC_019061.1.
DR PDB; 3TYK; X-ray; 1.95 A; A=1-341.
DR PDB; 3W0M; X-ray; 1.90 A; A=1-341.
DR PDB; 3W0N; X-ray; 1.90 A; A=1-341.
DR PDB; 3W0O; X-ray; 1.50 A; A=1-341.
DR PDB; 3W0P; X-ray; 2.00 A; A=1-341.
DR PDB; 3W0Q; X-ray; 1.80 A; A=1-341.
DR PDB; 3W0R; X-ray; 2.30 A; A=1-341.
DR PDB; 3W0S; X-ray; 1.77 A; A=1-341.
DR PDBsum; 3TYK; -.
DR PDBsum; 3W0M; -.
DR PDBsum; 3W0N; -.
DR PDBsum; 3W0O; -.
DR PDBsum; 3W0P; -.
DR PDBsum; 3W0Q; -.
DR PDBsum; 3W0R; -.
DR PDBsum; 3W0S; -.
DR AlphaFoldDB; P00557; -.
DR SMR; P00557; -.
DR KEGG; ag:CAA24743; -.
DR BRENDA; 2.7.1.163; 2026.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 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..341
FT /note="Hygromycin-B 4-O-kinase"
FT /id="PRO_0000204799"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:3W0O"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3W0O"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3W0O"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3W0O"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3W0S"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3W0O"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:3W0O"
FT HELIX 283..300
FT /evidence="ECO:0007829|PDB:3W0O"
SQ SEQUENCE 341 AA; 38033 MW; 52A9F3270647911A CRC64;
MKKPELTATS VEKFLIEKFD SVSDLMQLSE GEESRAFSFD VGGRGYVLRV NSCADGFYKD
RYVYRHFASA ALPIPEVLDI GEFSESLTYC ISRRAQGVTL QDLPETELPA VLQPVAEAMD
AIAAADLSQT SGFGPFGPQG IGQYTTWRDF ICAIADPHVY HWQTVMDDTV SASVAQALDE
LMLWAEDCPE VRHLVHADFG SNNVLTDNGR ITAVIDWSEA MFGDSQYEVA NIFFWRPWLA
CMEQQTRYFE RRHPELAGSP RLRAYMLRIG LDQLYQSLVD GNFDDAAWAQ GRCDAIVRSG
AGTVGRTQIA RRSAAVWTDG CVEVLADSGN RRPSTRPRAK E
