ID   MTNK_ENT38              Reviewed;         399 AA.
AC   A4W7Z0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Ent638_1139;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP59820.1; -; Genomic_DNA.
DR   RefSeq; WP_012016540.1; NC_009436.1.
DR   AlphaFoldDB; A4W7Z0; -.
DR   SMR; A4W7Z0; -.
DR   STRING; 399742.Ent638_1139; -.
DR   EnsemblBacteria; ABP59820; ABP59820; Ent638_1139.
DR   KEGG; ent:Ent638_1139; -.
DR   eggNOG; COG4857; Bacteria.
DR   HOGENOM; CLU_033681_0_0_6; -.
DR   OMA; EMCEITE; -.
DR   OrthoDB; 1457558at2; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000000230; 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_0000357340"
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;  44748 MW;  9D3218698CD6854D CRC64;
     MSQYRTFTAQ DAVEYAKQFG GLDNPSSLVE AQEIGDGNLN LVFKIFDAQG VSRIIVKQAL
     PYVRCVGESW PLTLDRARLE AQTLVEHYQH SPQHTVKIHH YDPELAVMVM EDLSSHKIWR
     GELISGVYYP QASRQLGEYL AHTLFHTSDF YLHPHAKKAQ VAKYINPEMC EITEDLFFND
     PYQIHERNNY PAELEADVAA LRSDDQLKIA VASLKHRFFS QAEALLHGDI HSGSIFVAED
     SLKAIDAEFG YYGPIGFDIG TAIGNLLLNF CGLPGHLGIR DAAAAREQRL TDIQELWNTF
     SERFQALATE KTRDAALSVP GYASQFLKKV WTDAIGFCGT ELIRRSVGLS HVADIDTIKD
     DAMRHECLRH AITLGKALIV IADRIDSAEA LVARVRQYS