ID   RIFN_AMYMS              Reviewed;         303 AA.
AC   G0FS68;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Kanosamine kinase;
DE            EC=2.7.1.179;
GN   Name=rifN; OrderedLocusNames=AMES_0628, RAM_03220;
OS   Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=713604;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699;
RX   PubMed=21914879; DOI=10.1128/jb.05819-11;
RA   Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA   Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT   "Whole genome sequence of the rifamycin B-producing strain Amycolatopsis
RT   mediterranei S699.";
RL   J. Bacteriol. 193:5562-5563(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699;
RX   PubMed=23012281; DOI=10.1128/jb.01295-12;
RA   Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.;
RT   "Complete genome sequence of Amycolatopsis mediterranei S699 based on de
RT   novo assembly via a combinatorial sequencing strategy.";
RL   J. Bacteriol. 194:5699-5700(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=S699;
RX   PubMed=12207505; DOI=10.1021/ja0206339;
RA   Arakawa K., Muller R., Mahmud T., Yu T.W., Floss H.G.;
RT   "Characterization of the early stage aminoshikimate pathway in the
RT   formation of 3-amino-5-hydroxybenzoic acid: the RifN protein specifically
RT   converts kanosamine into kanosamine 6-phosphate.";
RL   J. Am. Chem. Soc. 124:10644-10645(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of 3-amino-5-hydroxybenzoate
CC       (AHBA), a compound that then serves as the starter unit for the
CC       assembly of a polyketide during the biosynthesis of rifamycin B and
CC       other ansamycin antibiotics. Catalyzes only the phosphorylation of
CC       kanosamine to yield kanosamine 6-phosphate.
CC       {ECO:0000269|PubMed:12207505}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + kanosamine = ADP + D-kanosamine 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:35751, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:72732, ChEBI:CHEBI:72748, ChEBI:CHEBI:456216;
CC         EC=2.7.1.179; Evidence={ECO:0000269|PubMed:12207505};
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+), Cu(2+), and Fe(2+).
CC       {ECO:0000269|PubMed:12207505}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.39 mM for kanosamine (at 37 degrees Celsius and pH 7.2)
CC         {ECO:0000269|PubMed:12207505};
CC         KM=1.9 mM for ATP (at 37 degrees Celsius and pH 7.2)
CC         {ECO:0000269|PubMed:12207505};
CC         Vmax=0.6 mmol/min/mg enzyme (at 37 degrees Celsius and pH 7.2)
CC         {ECO:0000269|PubMed:12207505};
CC   -!- PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; CP002896; AEK39136.1; -; Genomic_DNA.
DR   EMBL; CP003729; AFO74164.1; -; Genomic_DNA.
DR   RefSeq; WP_013222560.1; NC_018266.1.
DR   AlphaFoldDB; G0FS68; -.
DR   SMR; G0FS68; -.
DR   STRING; 713604.RAM_03220; -.
DR   EnsemblBacteria; AEK39136; AEK39136; RAM_03220.
DR   KEGG; amm:AMES_0628; -.
DR   KEGG; amn:RAM_03220; -.
DR   PATRIC; fig|713604.12.peg.669; -.
DR   HOGENOM; CLU_036604_0_4_11; -.
DR   OMA; ARGSCEI; -.
DR   OrthoDB; 1130699at2; -.
DR   BRENDA; 2.7.1.179; 313.
DR   SABIO-RK; G0FS68; -.
DR   UniPathway; UPA01029; -.
DR   Proteomes; UP000006138; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..303
FT                   /note="Kanosamine kinase"
FT                   /id="PRO_0000425287"
SQ   SEQUENCE   303 AA;  30823 MW;  8E861C2F368E4453 CRC64;
     MGTPYHLGID VGGTKVAFRV ESGSACIEET SFSWGARHSA EDDLAQLAGH VARLRERIGT
     PLEAVGVAMP GTVGADGRVA TWPSRPEWTG VDLKTALHSL FPEAAVAWAD DGDLGALAES
     RASGCENLLY IGIGTGIGGG LVLGGVPCPG LGRGSFEIGH VIVEMGGVRC VCGRRGCLQA
     LASGPATLRR ASLLRGADVT YYRLQRALRN GEPWAADALE GSTRALAAAV TGVQELVHPD
     RVLIGGGFAA GIPEIVPSVS GFLADLVRQG QAPLPVEPAA LGGLSSLRGA VALAGLVAAG
     EVP