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Database: UniProt
Entry: S9QU46_9RHOB
LinkDB: S9QU46_9RHOB
Original site: S9QU46_9RHOB 
ID   S9QU46_9RHOB            Unreviewed;       418 AA.
AC   S9QU46;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=S-methyl-5-thioribose kinase {ECO:0000256|ARBA:ARBA00012128};
DE            EC=2.7.1.100 {ECO:0000256|ARBA:ARBA00012128};
GN   ORFNames=ruthe_02775 {ECO:0000313|EMBL:EPX83158.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX83158.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX83158.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX83158.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
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:EPX83158.1}.
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DR   EMBL; AOLV01000033; EPX83158.1; -; Genomic_DNA.
DR   RefSeq; WP_021098847.1; NZ_KE557324.1.
DR   AlphaFoldDB; S9QU46; -.
DR   STRING; 1123069.ruthe_02775; -.
DR   PATRIC; fig|1123069.3.peg.2752; -.
DR   HOGENOM; CLU_033681_0_0_5; -.
DR   OrthoDB; 9777791at2; -.
DR   Proteomes; UP000015346; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPX83158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW   Transferase {ECO:0000313|EMBL:EPX83158.1}.
FT   DOMAIN          36..285
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   418 AA;  46220 MW;  5AEEAC2F623DEC35 CRC64;
     MEERPYEALT VETLARRLGD LPALRDRIGD PAGWRVREVG DGNLNLVFIV EGDRGGLVVK
     QALPYVRLVG ESWPLPLRRS FFEYHALRRQ QARDPGSVPD VLHFDEGQAL VVMEYLDGHI
     ILRRALIAGT RHAGLGERLG LFCARTLFRG SDLHLPAAER KADLALFAGN VDLCAITEAL
     VFTEPYFAAP MNRHTPGLDP IAAELRADAA LKLAAQRLKT AFAARAETLL HGDLHTGSVM
     VRGDQVRIID PEFAVYGPMG FDIGMLIANF LMAHCAQPGH GRDRADYQAW ILSVIRAIWT
     SFAAEFARLW RTERTGMLFP RTLFEDQGQS WAADAACSGW LGQVWRDTLG FAGLECHRRI
     LGLAHNADFE SIADEGLRAA CEAKALVLGR TLLLGQDDIA GIDALIDLAR DIAERDWL
//
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