ID   MTNK_KLEPN              Reviewed;         399 AA.
AC   Q9F0P1; Q9R4A2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Methylthioribose kinase;
DE            Short=MTR kinase;
DE            EC=2.7.1.100;
GN   Name=mtnK; Synonyms=mtrK;
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].
RA   Cornell K.A., Hinrichs D.J., Kahl N.S., Riscoe M.K.;
RT   "Cloning and expression of 5-methylthioribose kinase, a chemotherapeutic
RT   target in the methionine salvage pathway.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 3-21, FUNCTION, AND SUBUNIT.
RX   PubMed=8694776; DOI=10.1042/bj3170285;
RA   Cornell K.A., Winter R.W., Tower P.A., Riscoe M.K.;
RT   "Affinity purification of 5-methylthioribose kinase and 5-
RT   methylthioadenosine/S-adenosylhomocysteine nucleosidase from Klebsiella
RT   pneumoniae.";
RL   Biochem. J. 317:285-290(1996).
CC   -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC       methylthioribose-1-phosphate. {ECO:0000269|PubMed:8694776}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-
CC         thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:22312,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58533,
CC         ChEBI:CHEBI:78440, ChEBI:CHEBI:456216; EC=2.7.1.100;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC       thioadenosine (hydrolase route): step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8694776}.
CC   -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF212863; AAG43573.2; -; Genomic_DNA.
DR   RefSeq; WP_004151657.1; NZ_WYAL01000003.1.
DR   AlphaFoldDB; Q9F0P1; -.
DR   SMR; Q9F0P1; -.
DR   GeneID; 64296515; -.
DR   OMA; EMCEITE; -.
DR   OrthoDB; 1457558at2; -.
DR   BioCyc; MetaCyc:MON-1295; -.
DR   UniPathway; UPA00904; UER00872.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01683; Salvage_MtnK; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR009212; Methylthioribose_kinase.
DR   Pfam; PF01636; APH; 1.
DR   PIRSF; PIRSF031134; MTRK; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR01767; MTRK; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; ATP-binding; Direct protein sequencing; Kinase;
KW   Methionine biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN           1..399
FT                   /note="Methylthioribose kinase"
FT                   /id="PRO_0000357346"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         111..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  44591 MW;  75EE02F722B7D4B2 CRC64;
     MSQYHTFTAH DAVAYAQQFA GIDNPSELVS AQEVGDGNLN LVFKVFDRQG VSRAIVKQAL
     PYVRCVGESW PLTLDRARLE AQTLVAHYQH SPQHTVKIHH FDPELAVMVM EDLSDHRIWR
     GELIANVYYP QAARQLGDYL AQVLFHTSDF YLHPHEKKAQ VAQFINPAMC EITEDLFFND
     PYQIHERNNY PAELEADVAA LRDDAQLKLA VAALKHRFFA HAEALLHGDI HSGSIFVAEG
     SLKAIDAEFG YFGPIGFDIG TAIGNLLLNY CGLPGQLGIR DAAAAREQRL NDIHQLWTTF
     AERFQALAAE KTRDAALAYP GYASAFLKKV WADAVGFCGS ELIRRSVGLS HVADIDTIQD
     DAMRHECLRH AITLGRALIV LAERIDSVDE LLARVRQYS