ID A0A0U2MU12_9BACL Unreviewed; 401 AA.
AC A0A0U2MU12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=IJ22_04260 {ECO:0000313|EMBL:ALS20815.1}, PN4B1_07460
GN {ECO:0000313|EMBL:GCL70844.1};
OS Paenibacillus naphthalenovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS20815.1, ECO:0000313|Proteomes:UP000061660};
RN [1] {ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS20815.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS20815.1};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALS20815.1, ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS20815.1,
RC ECO:0000313|Proteomes:UP000061660};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
RN [4] {ECO:0000313|EMBL:GCL70844.1, ECO:0000313|Proteomes:UP000299945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B1 {ECO:0000313|EMBL:GCL70844.1,
RC ECO:0000313|Proteomes:UP000299945};
RA Ha-Thanh L.T., Ngoc-Thi T.V., Shintani M., Moriuchi R., Dohra H.,
RA Hoang-Loc N., Kimbara K.;
RT "Isolation and characterization of a moderate thermophilic Paenibacillus
RT naphthalenovorans strain 4B1 capable of degrading dibenzofuran from dioxin-
RT contaminated soil in Vietnam.";
RL Submitted (MAR-2019) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01683}.
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DR EMBL; CP013652; ALS20815.1; -; Genomic_DNA.
DR EMBL; BJCS01000002; GCL70844.1; -; Genomic_DNA.
DR RefSeq; WP_062406903.1; NZ_CP013652.1.
DR AlphaFoldDB; A0A0U2MU12; -.
DR STRING; 162209.IJ22_04260; -.
DR KEGG; pnp:IJ22_04260; -.
DR PATRIC; fig|162209.4.peg.451; -.
DR OrthoDB; 9777791at2; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000061660; Chromosome.
DR Proteomes; UP000299945; 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:ALS20815.1};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01683};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Reference proteome {ECO:0000313|Proteomes:UP000061660};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01683}.
FT DOMAIN 32..268
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 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 401 AA; 45561 MW; 4C91A82677D6D128 CRC64;
MSAYRALTEA EAIDYARQIP DLFQKDSELT SREIGDGNLN LVFHISEPST GKSIILKQAL
PYAKVVGESW PLTLDRARIE SEALMIQESL CPDLVPHVHA YEPELALTVM QDLSDHVIMR
RGLMERNKYP LFASHIGTFL ARTLFYTSDL GMNQQDKKEQ VKRFINPELC KITEDLIFDD
PYTDSPNNNV PPAIRDAVEA VWKDTELHLE VAILREKFLT QAQALIHGDL HTGSIFIKPD
STKVIDPEFA YYGPMGFDIG AVLANLLLNY AAQEGWSPDA ASRQDYRNYL TQTIRDIWKK
FDSEFRALWD EHGVDRMSKT PGYQDLYMKR LLQDTFGYAG CKIVRRVHGL AQVADINKLE
DEAAKERAQR IALAIGTTLI KSHRKAESIE QMIEIAEKNV S
//
