ID R5DGZ7_9FIRM Unreviewed; 401 AA.
AC R5DGZ7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=S-methyl-5-thioribose kinase {ECO:0000256|ARBA:ARBA00012128};
DE EC=2.7.1.100 {ECO:0000256|ARBA:ARBA00012128};
GN ORFNames=BN457_01045 {ECO:0000313|EMBL:CCX76087.1};
OS Dorea sp. CAG:105.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1262872 {ECO:0000313|EMBL:CCX76087.1, ECO:0000313|Proteomes:UP000017921};
RN [1] {ECO:0000313|EMBL:CCX76087.1, ECO:0000313|Proteomes:UP000017921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:105 {ECO:0000313|Proteomes:UP000017921};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX76087.1}.
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DR EMBL; CAWY010000160; CCX76087.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DGZ7; -.
DR STRING; 1262872.BN457_01045; -.
DR Proteomes; UP000017921; 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:CCX76087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017921};
KW Transferase {ECO:0000313|EMBL:CCX76087.1}.
FT DOMAIN 36..271
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 401 AA; 45889 MW; CE38D3EB5E692400 CRC64;
MDKYSKHFLL NVDTAKEYAV EKVGYFKEDE KLEAIEIGDG NINYVFKVWN PETGKSLIIK
QADTVLRSSG RPLDMHRNKI EAEILGIEGK LSEGFVPEIY LYDENMYALS MEDISAYKNL
RTEMAAGKTF PKLADDIATF MADTLLPTTD LIMNRAEKKE KVKLFTNPEL CDISEDLVFT
EPYYDYKGRN IILDQNMDFV KEKLYGDEDL HAEVGQLRDD FMNHAQALIH GDLHSGSIFV
NQEGTKVIDP EFAFYGPMGY DIGNVIGNLF FAWANKYYTD SENTEFLTWI EKTIGEVTDK
FKEKFSAKWD ALVEFPLYKT EGFKKYYTDK VMADSFGYAG TEIIRRVVGD SKVKEVTSVT
NVDQRVPMER ALIQIGIKLI KERRTLKDGA AIKAVGKEYL K
//
