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LOCUS WP_010989417 269 aa linear BCT 11-MAR-2024 ACCESSION WP_010989417 VERSION WP_010989417.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 269) AUTHORS Drebes,J., Kunz,M., Windshugel,B., Kikhney,A.G., Muller,I.B., Eberle,R.J., Oberthur,D., Cang,H., Svergun,D.I., Perbandt,M., Betzel,C. and Wrenger,C. TITLE Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections JOURNAL Sci Rep 6, 22871 (2016) PUBMED 26960569 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 269) AUTHORS Campobasso,N., Mathews,I.I., Begley,T.P. and Ealick,S.E. TITLE Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution JOURNAL Biochemistry 39 (27), 7868-7877 (2000) PUBMED 10891066 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF006830.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK09355 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..269 /organism="Listeria monocytogenes" /db_xref="taxon:1639" gene 1..269 /gene="thiM" Protein 1..269 /product="hydroxyethylthiazole kinase" /EC_number="2.7.1.50" /GO_function="GO:0004417 - hydroxyethylthiazole kinase activity [Evidence IEA]" /GO_process="GO:0009228 - thiamine biosynthetic process [Evidence IEA]" /calculated_mol_wt=27921 Region 5..264 /region_name="PRK09355" /note="hydroxyethylthiazole kinase; Validated" /db_xref="CDD:236477" Site order(22,24,30,34,40,42,62,64..65) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:238575" Site order(23..28,30..31,34,42..45,47..48,51..52,64..67, 100..101,187..190,238..239,241..243,245..246,249) /site_type="other" /note="multimerization interface [polypeptide binding]" /db_xref="CDD:238575" Site order(91,118,120,123,164,166,168,186,192,194) /site_type="other" /note="ATP binding site [chemical binding]" /db_xref="CDD:238575" ORIGIN 1 mfdfmtlekv rekgplvhni tnivvandsa ngllaigasp imasakeemd elakmadvlv 61 inigtldgel vtamkiagra anvagtpvvl dpvgvgatsy rrkvvqella eiqfaairgn 121 agelaaiage aweakgvdag vgsadvlsia gkvanewstv viisgevdvi sdgtrfakva 181 ngsallprit gsgcllsavc gsfiavqdda frasveacas yavaseyaem elerklpgsf 241 rplfldalas wsvektraka kiqesgehk