ID MTNK_GEOKA Reviewed; 396 AA.
AC Q5L1E5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=GK0950;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75235.1; -; Genomic_DNA.
DR RefSeq; WP_011230451.1; NC_006510.1.
DR AlphaFoldDB; Q5L1E5; -.
DR SMR; Q5L1E5; -.
DR STRING; 235909.GK0950; -.
DR KEGG; gka:GK0950; -.
DR PATRIC; fig|235909.7.peg.1038; -.
DR eggNOG; COG4857; Bacteria.
DR HOGENOM; CLU_033681_0_0_9; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000001172; 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 Gene3D; 3.90.1200.10; -; 1.
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 NCBIfam; TIGR01767; MTRK; 1.
DR PANTHER; PTHR34273; METHYLTHIORIBOSE KINASE; 1.
DR PANTHER; PTHR34273:SF2; METHYLTHIORIBOSE KINASE; 1.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF031134; MTRK; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Methionine biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Methylthioribose kinase"
FT /id="PRO_0000357344"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 115..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 250..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ SEQUENCE 396 AA; 44982 MW; 55D8C13332CD678A CRC64;
MTTVQTSVYE PLTEPKAVAL AVRLGLFRDG TPLACREIGD GNLNLVFHIV DQETKQGVII
KQALPYAKVV GESWPLTLKR AVIESNALRT FASYVPQYVP KVYYSDESLA ITVMEDLSRL
QIARKGLIEG KTYPLLSQHI GEFVAKTAFY TSDFGMNQQE KKKLAQSFVN PELCKITEDL
VFTDPFFDHE TNNFEDELRP DVEALWRDDR LHLEAAKLKR KFLTEADVLL HGDLHTGSIF
VSADETKVID PEFAFYGPIG FDLGQFFANL LLNALSRSEL ERQPLFDHID RTWDVFASVF
SNLWRTESVE TYAATPGLLE DVLRHAFIDA VGFAGCEVIR RTIGLAHVAD LDGIEHKDER
LVAKRHALRL GRRLIIERRV FTGTEDFRRL FAETEQ
//
