ID A5I1A5_CLOBH Unreviewed; 403 AA.
AC A5I1A5; A7G306;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=S-methyl-5-thioribose kinase {ECO:0000256|ARBA:ARBA00012128};
DE EC=2.7.1.100 {ECO:0000256|ARBA:ARBA00012128};
GN Name=mtnK {ECO:0000313|EMBL:CAL82817.1};
GN OrderedLocusNames=CBO1267 {ECO:0000313|EMBL:CAL82817.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82817.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82817.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000256|ARBA:ARBA00010165}.
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DR EMBL; AM412317; CAL82817.1; -; Genomic_DNA.
DR RefSeq; WP_011948891.1; NC_009698.1.
DR RefSeq; YP_001253791.1; NC_009495.1.
DR RefSeq; YP_001387171.1; NC_009698.1.
DR AlphaFoldDB; A5I1A5; -.
DR GeneID; 5185522; -.
DR KEGG; cbh:CLC_1305; -.
DR KEGG; cbo:CBO1267; -.
DR PATRIC; fig|413999.7.peg.1253; -.
DR HOGENOM; CLU_033681_0_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 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 Kinase {ECO:0000313|EMBL:CAL82817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Transferase {ECO:0000313|EMBL:CAL82817.1}.
FT DOMAIN 32..266
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 403 AA; 46815 MW; 06D09EEF8791A2D5 CRC64;
MAEYKPMDCE SIIKYIKELN LDIFDEKMDL TAKEIGDGNL NLVFRVKDNN TGKSVIIKQA
LPYLRVAGEG WKLTVDRNRI EAEAMMKQDK ACPNSVPKIY YHDKDYNLYV AEDLGSMDIL
RNGLMNMKKY PKFPDQIGKF LSRNLFYTSD LGLGAVAKKS LVSKFINPEL CDITEKLVLT
DPYMNAESND INPEIMDEVK DMWGRKDFRL EVTKLKNIFM TKAEALLHGD LHTGSIFITE
DDMRVFDTEF AFYGPYGYDI GLLFANFILN YISWEGREDR SKEEIKEFRK YLLDTIEEIW
HEFEIGLKEI WDKDCKEISS TVEGYKEYYI NNLLQETIGF SACEVMRRII GMAHVPDLDV
LKDLKQKAKA QRLGLKIGQE MVMRRNKITK IEDLSVFISQ ITK
//
