ID   MTNK_KLEP3              Reviewed;         399 AA.
AC   B5XZW3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Methylthioribose kinase {ECO:0000255|HAMAP-Rule:MF_01683};
DE            Short=MTR kinase {ECO:0000255|HAMAP-Rule:MF_01683};
DE            EC=2.7.1.100 {ECO:0000255|HAMAP-Rule:MF_01683};
GN   Name=mtnK {ECO:0000255|HAMAP-Rule:MF_01683}; OrderedLocusNames=KPK_3950;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC       methylthioribose-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01683}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01683};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01683}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01683}.
CC   -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01683}.
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DR   EMBL; CP000964; ACI11507.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XZW3; -.
DR   SMR; B5XZW3; -.
DR   EnsemblBacteria; ACI11507; ACI11507; KPK_3950.
DR   KEGG; kpe:KPK_3950; -.
DR   HOGENOM; CLU_033681_0_0_6; -.
DR   OMA; EMCEITE; -.
DR   OrthoDB; 1457558at2; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000001734; Chromosome.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Kinase; Methionine biosynthesis;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..399
FT                   /note="Methylthioribose kinase"
FT                   /id="PRO_1000187404"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         111..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         246..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ   SEQUENCE   399 AA;  44567 MW;  672575B1E6CB8F98 CRC64;
     MSQYHTFTAH DAVAYAQQFA GIDNPSELVS AQEVGDGNLN LVFKVFDRQG VSRAIVKQAL
     PYVRCVGESW PLTLDRARLE AQTLVAHYQH SPQHTVKIHH FDPELAVMVM EDLSDHRIWR
     GELIANVYYP QAARQLGDYL AQVLFHTSDF YLHPHEKKAQ VAQFSNPAMC EITEDLFFND
     PYQIHERNNY PAELETDVAA LRDDAQLKLA VAALKHRFFA HAEALLHGDI HSGSIFVAEG
     SLKAIDAEFG YFGPIGFDIG TAIGNLLLNY CGLPGQLGIR DAAAAREQRL NDIHQLWTTF
     AERFQALAAE KTRDAALAYP GYASAFLKKV WADAVGFCGS ELIRRSVGLS HVADIDTIQD
     DAMRHECLRH AITLGKALIV LAERIDSVDE LLARVRQYS