ID C0ZL37_BREBN Unreviewed; 409 AA.
AC C0ZL37;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:BAH45864.1};
GN Synonyms=ykrT {ECO:0000313|EMBL:BAH45864.1};
GN OrderedLocusNames=BBR47_48870 {ECO:0000313|EMBL:BAH45864.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH45864.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH45864.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) 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; AP008955; BAH45864.1; -; Genomic_DNA.
DR RefSeq; WP_015893119.1; NC_012491.1.
DR AlphaFoldDB; C0ZL37; -.
DR STRING; 358681.BBR47_48870; -.
DR KEGG; bbe:BBR47_48870; -.
DR eggNOG; COG4857; Bacteria.
DR HOGENOM; CLU_033681_0_0_9; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000001877; 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 {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:BAH45864.1};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01683};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:BAH45864.1}.
FT DOMAIN 31..263
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 245..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
SQ SEQUENCE 409 AA; 46161 MW; 641C52184EAAAC9F CRC64;
MAYRALTEQE AVEYVKGIPG LFSEGAELTS REIGDGNLNL VFDIQEPATG KSVIVKQALP
FARVVGESWP LTIDRARIES EALRIQHKYV PDLVPQVYHF DGELALTVME NVGDHIIMRK
GLIEGKRYPL FAKQIGRFLA QTLFFTSDLG AHPYDKKTLV GTFINPELCK ITEDLVFTDP
YENAPTNDFN PLIRREVEAI WNNRPLKLEI AKLKYDFLTR SEALLHGDLH TGSIFITENS
LKAIDPEFAY YGPIGFDIGA IIANLLLNYA GQHGLQKDQG EREAYREYLL ETVEDVWNEF
VSQFVQLWHK HAKERSAHVE GLWQSYVKRL IQDTAGYAGC KILRRVIGLA GVADLNAIED
DQTRAEAERL ALSIGEALIL GRSGIEESTD ITDIVRTITE RYYQEATTV
//
