ID B0P8K3_9FIRM Unreviewed; 407 AA.
AC B0P8K3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:EDS12249.1};
GN ORFNames=ANACOL_01092 {ECO:0000313|EMBL:EDS12249.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS12249.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS12249.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12249.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS12249.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12249.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS12249.1}.
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DR EMBL; ABGD02000007; EDS12249.1; -; Genomic_DNA.
DR RefSeq; WP_006874487.1; NZ_DS544177.1.
DR AlphaFoldDB; B0P8K3; -.
DR STRING; 169435.ERS852551_00058; -.
DR GeneID; 72464377; -.
DR eggNOG; COG4857; Bacteria.
DR HOGENOM; CLU_033681_0_0_9; -.
DR Proteomes; UP000003803; 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:EDS12249.1};
KW Transferase {ECO:0000313|EMBL:EDS12249.1}.
FT DOMAIN 35..282
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 407 AA; 46154 MW; E6906B0ED347FDD4 CRC64;
MKKYDSYFLM NLNDAKEYAL EKVTRFDWDE NSMQCKEIGD GNLNYVFRVW DGKGHSAIIK
QAGEALRISA DMHISTDRNR IESEILLLQG KLAPGYVPEI YFYDTVMCAC GMQDLSDHAI
MRTSMLQHKI YPKFAEQITT FMANTLMGTT DIVLDHKEKK ELQKKYINPE LCEITEDLVY
TEPYNNCANR NNVYPPNADF VKKELYDDAA LHLEVAKLKM DFMCNAQSLI HGDLHTGSIF
INDDTTMVFD PEFCFYGPMG YDIGNVVANI IFAWCNGDAE IAEPAERGKF CGWAEQVIVD
VVDLTMAKMK AYYTEHVTDR MAKTPGYMDY YLGTILSDTA AVTGLELIRR TVGMANVKDL
TTIADEAKRT RAERICILAA KRYIKERAAL HSGADFLKVL KDAAACL
//
