MTNK_BACC7
ID MTNK_BACC7 Reviewed; 393 AA.
AC B7HN10;
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=BCAH187_A4160;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
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; CP001177; ACJ77857.1; -; Genomic_DNA.
DR RefSeq; WP_000542705.1; NC_011658.1.
DR AlphaFoldDB; B7HN10; -.
DR SMR; B7HN10; -.
DR EnsemblBacteria; ACJ77857; ACJ77857; BCAH187_A4160.
DR KEGG; bcr:BCAH187_A4160; -.
DR HOGENOM; CLU_033681_0_0_9; -.
DR OMA; EMCEITE; -.
DR OrthoDB; 1457558at2; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000002214; 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_1000187402"
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; 44709 MW; 165D40838E92ED31 CRC64;
MGYYSLTEVT AVQYAKEHGY FEKKANVVCH EIGDGNLNYV FKLDDGEKSI IIKQALPYAK
VVGESWPLSI KRATIESKAL QIFAKYVPEY VPVVYSHDEE LAVTIIEDLS KLTITRKGLI
DGEEYPLLSQ HIGRFLANVL FYTSDFGLQS EEKRVLEGTF VNPDLCKITE DLVFTDPFGH
YDTNDYESEL QLAVDELWSD KTLKLKVAQY KYKFLTRKEA LIHGDLHTGS IFSSPSETKV
IDPEFATYGP FGFDIGQFIA NLLLNALSRE EEQRSVLFFH IEKTWSYFVD TFTKLWIGEG
VEAYTKEKQW LPIILQNIFT DVVGFAGCEL IRRTIGLAHV ADLDEIANKE TRIQAKKQAL
SLGRELIKYE SKNADIQLFR ALFQQTVSGG VKA