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KKA9_STRRI
ID   KKA9_STRRI              Reviewed;         263 AA.
AC   P13250;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Aminoglycoside 3'-phosphotransferase;
DE            EC=2.7.1.95;
DE   AltName: Full=APH(3');
DE   AltName: Full=Kanamycin kinase;
DE   AltName: Full=Ribostamycin phosphotransferase;
GN   Name=rph;
OS   Streptomyces ribosidificus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=80859;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851496; DOI=10.1016/0378-1119(88)90031-5;
RA   Hoshiko S., Nojiri C., Matsunaga K., Katsumata K., Satoh E., Nagaoka K.;
RT   "Nucleotide sequence of the ribostamycin phosphotransferase gene and of its
RT   control region in Streptomyces ribosidificus.";
RL   Gene 68:285-296(1988).
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; M22126; AAC32025.1; -; Genomic_DNA.
DR   RefSeq; WP_063842177.1; NG_047452.1.
DR   AlphaFoldDB; P13250; -.
DR   SMR; P13250; -.
DR   KEGG; ag:AAC32025; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..263
FT                   /note="Aminoglycoside 3'-phosphotransferase"
FT                   /id="PRO_0000204812"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  29575 MW;  17B1630CBD99783C CRC64;
     MESTLRRTYP HHTWHLVNEG DSGAFVYRLT GHGPELYAKI APRTPENSAF HLDGEADRLD
     WLARHGISVP RVVERGADDT TAWLVTEAVP GAAASEEWPE DERAAVVDAI AEMARTLHEL
     PVSECPFDRR LDVTGEARHN VREGLVDLDD LQEEPAGWTG DQLLAELDLT RPEKEDLVVC
     HGDLCPNNVL LDPETHRITG LIDVGRLRLA TCHADLALAA RELAIDEDPW FGPAYAERFL
     ERYGAHHVDQ EKMAFYQLLD EFF
 
 
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