ID A0A0K9H1Y3_9BACI Unreviewed; 432 AA.
AC A0A0K9H1Y3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=S-methyl-5-thioribose kinase {ECO:0000256|ARBA:ARBA00012128};
DE EC=2.7.1.100 {ECO:0000256|ARBA:ARBA00012128};
GN ORFNames=AC623_02310 {ECO:0000313|EMBL:KMY52964.1};
OS Bacillus sp. FJAT-27231.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY52964.1, ECO:0000313|Proteomes:UP000037077};
RN [1] {ECO:0000313|Proteomes:UP000037077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000256|ARBA:ARBA00010165}.
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:KMY52964.1}.
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DR EMBL; LFZU01000001; KMY52964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9H1Y3; -.
DR STRING; 1679168.AC623_02310; -.
DR PATRIC; fig|1679168.3.peg.476; -.
DR Proteomes; UP000037077; Unassembled WGS sequence.
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:KMY52964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037077};
KW Transferase {ECO:0000313|EMBL:KMY52964.1}.
FT DOMAIN 40..274
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 432 AA; 49044 MW; 9064C246394EC4AC CRC64;
MEGTHLKDFT SAYFTMNEAD VVEYVQNRLS VFNDAADLEC REIGDGNLNY VFKVVDRKSG
ESIIIKQAGP VARISDAFKV SPDRNRIESE ILALQGELAP GFVPKVYAYD PVMNCCVMDD
LSDHEIMRSA LLNYKKFPLF ADHITTFLAR TLLLTSDVVM GHKEKKERVQ QFTNPELCEI
TEDLVYTEPF YDCEQNDVFE GTKEFAREVI WNDEKLKLET AKLKFDFMTK AQSLLHGDLH
TGSIFIKEDS TKIIDPEFAF YGPAGYDIGN VVANLIFAYV HAHYTIEETE ARADYLPYLE
ETIVQVVELF SEKFLQLWNE TATEQTATLP KFKEWYLESI LEDTAAVTGL ELCRRVIGIA
HVKDLTSISD AENRTAAEKI CLTAGKTFIL ERTSIRTGDD FVKVLRRSVN QFSKGEINDD
NTNSSHSIST AR
//
