ID   MTNK_BACC2              Reviewed;         393 AA.
AC   B7IWE5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=BCG9842_B1098;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
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 G9842.";
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; CP001186; ACK93247.1; -; Genomic_DNA.
DR   RefSeq; WP_000542672.1; NC_011772.1.
DR   AlphaFoldDB; B7IWE5; -.
DR   SMR; B7IWE5; -.
DR   EnsemblBacteria; ACK93247; ACK93247; BCG9842_B1098.
DR   KEGG; bcg:BCG9842_B1098; -.
DR   HOGENOM; CLU_033681_0_0_9; -.
DR   OMA; EMCEITE; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000006744; 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_1000187399"
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;  44704 MW;  D7DF90C7A1F46034 CRC64;
     MGYYSLTEIT AVQYAKDHGY FEAKANVVCH EIGDGNLNYV FKLDDGEKSI IIKQALPYAK
     VVGESWPLSI KRATIESKAL QIFAQYVPDY VPAVYSHDEE LAITVIEDLS RLTITRKGLI
     GGEEYPLLSQ HIGRFLAHVL FYTSDFGLQS EEKRVLEGTF VNPDLCKITE DLVFTDPFGH
     YDTNDYEPDL QLVVDELWSD KTLKLKVAQY KYKFLTRKET LIHGDLHTGS IFSSPSETKV
     IDPEFATYGP FGFDIGQFIA NLLLNALSRE EEKRSVLFFH IEKTWSYFVE TFTKLWIGEG
     VEVYTKEKQW LPIILQNIFT DAVGFAGCEL IRRTIGLAHV ADLDEIENKE TRIQAKKQAL
     SLGKELIKYE SKSADIQLFR TLFQQTVSGG VKA