ID W4B0S7_9BACL Unreviewed; 405 AA.
AC W4B0S7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Methylthioribose kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE Short=MTR kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE EC=2.7.1.100 {ECO:0000256|HAMAP-Rule:MF_01683};
GN Name=mtnK {ECO:0000256|HAMAP-Rule:MF_01683,
GN ECO:0000313|EMBL:ETT36731.1};
GN ORFNames=C161_09478 {ECO:0000313|EMBL:ETT36731.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT36731.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT36731.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT36731.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01683}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01683}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000256|ARBA:ARBA00010165, ECO:0000256|HAMAP-Rule:MF_01683}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT36731.1}.
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DR EMBL; ASPR01000014; ETT36731.1; -; Genomic_DNA.
DR RefSeq; WP_036669902.1; NZ_ASPR01000014.1.
DR AlphaFoldDB; W4B0S7; -.
DR PATRIC; fig|1226754.4.peg.1938; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000019041; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01683};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:ETT36731.1};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01683};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:ETT36731.1}.
FT DOMAIN 32..264
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 111..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 246..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
SQ SEQUENCE 405 AA; 45766 MW; 3F5D0A325A3F5241 CRC64;
MSQYRPFTPQ DAIELAKTLP GPFAADANLD CHEIGDGNLN LVFHITDQNS DKSIIIKQAL
PYAKVVGESW PLSLVRARIE REILQEEYRL CPGMVPEVYH YDDDLALTVM EDLSDHVIMR
KGLIEGVSYP LFAQHIGEFM ARTLFFTSDL GMDQQLKKEQ QGRFINPDQC KITEDLIFDE
PYRIAEKNNY DVSIEDEAEA LRTDGELHLE VALLREKFLT HGQALLHGDL HTGSIFVTPE
STKVIDPEFA YYGPIGFDVG AVLANLLLNY ASLPGWIQNE TALRERETLM LNMVRDVWTE
FESRFRALWV NDLVDPMAKT PGYQDLYVQQ LFRDSIGFAG AKMVRRIVGL AHVADIDTIP
NATEREHAQR KALSIGKALI KNNRRLNTIG EVLDIVSTAV TTTKA
//
