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Database: UniProt
Entry: A0A125Q775_9BRAD
LinkDB: A0A125Q775_9BRAD
Original site: A0A125Q775_9BRAD 
ID   A0A125Q775_9BRAD        Unreviewed;       434 AA.
AC   A0A125Q775;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=S-methyl-5-thioribose kinase {ECO:0000256|ARBA:ARBA00012128};
DE            EC=2.7.1.100 {ECO:0000256|ARBA:ARBA00012128};
GN   ORFNames=AS156_14625 {ECO:0000313|EMBL:KWV50195.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV50195.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV50195.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV50195.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (NOV-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:KWV50195.1}.
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DR   EMBL; LNCU01000096; KWV50195.1; -; Genomic_DNA.
DR   RefSeq; WP_066511832.1; NZ_LNCU01000096.1.
DR   AlphaFoldDB; A0A125Q775; -.
DR   OrthoDB; 9777791at2; -.
DR   Proteomes; UP000057737; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:KWV50195.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KWV50195.1}.
FT   DOMAIN          45..305
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   434 AA;  47634 MW;  DC4118E8BDA059B5 CRC64;
     MNLQAQPGSG QSQYRILREA DLRDYLAGLP AIVAHLGGAP ADWSISEVGD GNLNLVFIVK
     GTSGGIAVKQ ALPYVRLVGE SWPLPLSRAH YEHLALVHQA RLAPKLVPAV LHHDGPLALT
     AMELLEPHII MRKGLIGATR YPRFVEDIST FLARTLFFSS DLSLTAAEKK EGIADFAGNH
     ALCKITEDLI FTDPYRVAEQ NRWTAPHLDA TAAAFRDDLD LHVAISRLKL KFMGSPEALI
     HGDLHTGSIM VAASETMVID PEFAFYGPMG FDIGAVIGNL IMAYLASAGH ERSPGERASF
     EAWLLETVEG VWTEFARKFV ALWRSEAKGD GYPVSLFAGE AGATRLEAER QAYMARLFQD
     TVGFAAAKTI RRILGLAHNI DFEWIADEKQ RAICEARALK LARSMMLETP SFTTIGAVTK
     AAREVRNWQP EFAN
//
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