MTNK_BACHK
ID MTNK_BACHK Reviewed; 393 AA.
AC Q6HED2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=BT9727_3775;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017355; AAT61560.1; -; Genomic_DNA.
DR RefSeq; WP_000542720.1; NC_005957.1.
DR RefSeq; YP_038094.1; NC_005957.1.
DR AlphaFoldDB; Q6HED2; -.
DR SMR; Q6HED2; -.
DR EnsemblBacteria; AAT61560; AAT61560; BT9727_3775.
DR KEGG; btk:BT9727_3775; -.
DR PATRIC; fig|281309.8.peg.4025; -.
DR HOGENOM; CLU_033681_0_0_9; -.
DR OMA; EMCEITE; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000001301; 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_0000357336"
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; 44721 MW; 12D37D4A604F46FB CRC64;
MGYYSLTEVT AVQYAKEHGY FEKKANVVCH EIGDGNLNYV FKLDDGVKSI IIKQALPYAK
VVGESWPLSI KRATIESKAL QIFAKYVPEY VPVVYSHDEE LAVTVIEDLS RLTITRKGLI
DGEEYPLLSQ HIGRFLANVL FYTSDFGLQS EEKRVLEGTF VNPDLCKITE DLVFTDPFGH
YDTNDYESEL QLAVDELWSD KILKLKVAQY KYKFLTRKEA LIHGDLHTGS IFSSPSETKV
IDPEFATYGP FGFDIGQFIA NLLLNALSRE EEQRGVLFFH IEKTWSYFVE TFTKLWIGEG
VEAYTKEKQW LPIILQNIFT DAVGFAGCEL IRRTIGLAHV ADLEEITNKE TRIQAKKQAI
SLGKELIKYE SKNADIQLFR TLFQQTVSGG IKA
