ID   MTNK_BACC0              Reviewed;         393 AA.
AC   B7JL13;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, 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};
GN   OrderedLocusNames=BCAH820_4054;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK91031.1; -; Genomic_DNA.
DR   RefSeq; WP_000542709.1; NC_011773.1.
DR   AlphaFoldDB; B7JL13; -.
DR   SMR; B7JL13; -.
DR   EnsemblBacteria; ACK91031; ACK91031; BCAH820_4054.
DR   KEGG; bcu:BCAH820_4054; -.
DR   HOGENOM; CLU_033681_0_0_9; -.
DR   OMA; EMCEITE; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000001363; 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..393
FT                   /note="Methylthioribose kinase"
FT                   /id="PRO_1000187398"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         107..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         242..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ   SEQUENCE   393 AA;  44726 MW;  33F15CC26F71DAF3 CRC64;
     MGYYSLTEVT AVQYAKEHGY FEKKANVVCH EIGDGNLNYV FKLDDGEKSI IIKQALPYAK
     VVGESWPLSI KRATIESKAL QIFAKYVPEY VPVVYSHDEE LAVTVIEDLS RLTITRKGLI
     DGEEYPLLSQ HIGHFLANVL FYTSDFGLQS EEKRVLEGTF VNPDLCKITE DLVFTDPFGH
     YDTNDYEPEL QLTIDELWSD KTLKLKVAQY KYKFLTRKEA LIHGDLHTGS IFSSPSETKV
     IDPEFATYGP FGFDIGQLIA NLLLNALSRE EEQRGVLFFH IEKTWSYFVE TFTKLWIGEG
     VEAYTKEKQW LPIILQNIFT DAVGFAGCEL IRRTIGLAHV ADLDEITNKE TRIQAKKQAL
     SLGKELIKYE SKNADIQLFR TLFQQTVSGG IKA