KHYB_STRHY
ID KHYB_STRHY Reviewed; 332 AA.
AC P09979;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Hygromycin-B 7''-O-kinase;
DE EC=2.7.1.119;
DE AltName: Full=APH(7'');
DE AltName: Full=Hygromycin B phosphotransferase;
DE AltName: Full=Hygromycin-B kinase;
GN Name=hyg;
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3005976; DOI=10.1093/nar/14.4.1565;
RA Zalacain M., Gonzalez A., Guerrero M.C., Mattaliano R.J., Malpartida F.,
RA Jimenez A.;
RT "Nucleotide sequence of the hygromycin B phosphotransferase gene from
RT Streptomyces hygroscopicus.";
RL Nucleic Acids Res. 14:1565-1581(1986).
CC -!- FUNCTION: The aminoglycoside phosphotransferases achieve inactivation
CC of their antibiotic substrates by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hygromycin B = 7''-O-phosphohygromycin B + ADP + H(+);
CC Xref=Rhea:RHEA:23388, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57929, ChEBI:CHEBI:57971, ChEBI:CHEBI:456216;
CC EC=2.7.1.119;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; X03615; CAA27276.1; -; Genomic_DNA.
DR PIR; A23507; WGSMHH.
DR RefSeq; WP_063842185.1; NG_047472.1.
DR PDB; 6IY9; X-ray; 2.40 A; A/B=1-332.
DR PDBsum; 6IY9; -.
DR AlphaFoldDB; P09979; -.
DR SMR; P09979; -.
DR KEGG; ag:CAA27276; -.
DR BioCyc; MetaCyc:MON-14574; -.
DR BRENDA; 2.7.1.119; 6043.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008904; F:hygromycin-B 7''-O-phosphotransferase 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 InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR016259; Hygromycin-B_Kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000707; Hygromycin-B_kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..332
FT /note="Hygromycin-B 7''-O-kinase"
FT /id="PRO_0000204800"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:6IY9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 137..155
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6IY9"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6IY9"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6IY9"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6IY9"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:6IY9"
SQ SEQUENCE 332 AA; 37054 MW; E1D614095C5D2F4C CRC64;
MTQESLLLLD RIDSDDSYAS LRNDQEFWEP LARRALEELG LPVPPVLRVP GESTNPVLVG
EPDPVIKLFG EHWCGPESLA SESEAYAVLA DAPVPVPRLL GRGELRPGTG AWPWPYLVMS
RMTGTTWRSA MDGTTDRNAL LALARELGRV LGRLHRVPLT GNTVLTPHSE VFPELLRERR
AATVEDHRGW GYLSPRLLDR LEDWLPDVDT LLAGREPRFV HGDLHGTNIF VDLAATEVTG
IVDFTDVYAG DSRYSLVQLH LNAFRGDREI LAALLDGAQW KRTEDFAREL LAFTFLHDFE
VFEETPLDLS GFTDPEELAQ FLWGPPDTAP GA
