ID A0A150N4V5_9BACI Unreviewed; 400 AA.
AC A0A150N4V5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=B4110_0990 {ECO:0000313|EMBL:KYD31676.1};
OS Parageobacillus toebii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD31676.1, ECO:0000313|Proteomes:UP000075324};
RN [1] {ECO:0000313|EMBL:KYD31676.1, ECO:0000313|Proteomes:UP000075324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4110 {ECO:0000313|EMBL:KYD31676.1,
RC ECO:0000313|Proteomes:UP000075324};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KYD31676.1}.
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DR EMBL; LQYW01000032; KYD31676.1; -; Genomic_DNA.
DR RefSeq; WP_062677647.1; NZ_LQYW01000032.1.
DR AlphaFoldDB; A0A150N4V5; -.
DR PATRIC; fig|153151.4.peg.2079; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000075324; 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:KYD31676.1};
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:KYD31676.1}.
FT DOMAIN 35..267
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 115..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 250..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
SQ SEQUENCE 400 AA; 45203 MW; 0851B18FBB321370 CRC64;
MSVSHPSVYE PLTEQGAISL AVRLGLFPEG TPLACREIGD GNLNLVFRVV DQQTKKGIIV
KQALPYAKVV GESWPLTLKR AVIESNALRT FASYVPQYVP KVYYSDESLA ITVMEDLSHL
QIARKGLIEG KTYPLLSQHI GEFIAKTSFY TSDFGMNQQE KKQLAQSFVN PELCKITEDL
VFTDPFFNHE TNNFEDELRD DVEALWNDDK LRLEVAKLKR KFLTEGDALI HGDLHTGSIF
ASDEETKIID PEFAFYGPFG FDIGQFFANL LLNALSRPEQ QQEPLFAHID KTWDVFATIF
SDLWRTHNVE PYAKTEGLLE DVLHHTFIDA IGFAGCEVIR RTIGLAHVAD LDGIEDKEER
LQAKRYALRL GRSLILQRET LSSTKEIRSL FAQTVLAATN
//
