ID   MTNK_EXIS2              Reviewed;         389 AA.
AC   B1YIY3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Exig_0431;
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-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; CP001022; ACB59913.1; -; Genomic_DNA.
DR   RefSeq; WP_012369337.1; NC_010556.1.
DR   AlphaFoldDB; B1YIY3; -.
DR   SMR; B1YIY3; -.
DR   STRING; 262543.Exig_0431; -.
DR   EnsemblBacteria; ACB59913; ACB59913; Exig_0431.
DR   KEGG; esi:Exig_0431; -.
DR   eggNOG; COG4857; Bacteria.
DR   HOGENOM; CLU_033681_0_0_9; -.
DR   OMA; EMCEITE; -.
DR   OrthoDB; 1457558at2; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000001681; 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; Reference proteome; Transferase.
FT   CHAIN           1..389
FT                   /note="Methylthioribose kinase"
FT                   /id="PRO_0000357343"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         106..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         241..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ   SEQUENCE   389 AA;  43908 MW;  8234A8171D963C5E CRC64;
     MGYQAFTVQD AIERVRTLGL IGNEPVTAEE IGDGNLNLVF RIQAGEKRLI LKQALPYAKV
     VGESWPLSLE RAWIEQSALK EFAKVAVPFV PHVYHASKEE AFTVMEDLSH LTIVRGGLLE
     GEKYPLLAEH IGSYLARTLF YTSDFAVGPV AKKQIARQYY NPDLCDITEK LIFTDPFYDA
     ETNAIEAGLE AEVDRIWNDA ELKREVAKLE ALFITKGDAL LHGDLHTGSI FASAEETKVI
     DPEFAFYGPF GFDVGQFIAH LFFAAYPDYD RLRDERIKDI DTFWLTFAST FKALWEREAV
     EPFRKADGLV DDVLSTILQD ALGFAGCELI RRTIGLALVA DLEQISDSTV RLERKRHALR
     LGAALIKRRT ECKTFTDLRN FDVTEELSR