Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_001195634 262 aa linear BCT 17-JAN-2025 ACCESSION WP_001195634 VERSION WP_001195634.1 KEYWORDS RefSeq. SOURCE Escherichia ORGANISM Escherichia Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 262) 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 262) 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..262 /organism="Escherichia" /db_xref="taxon:561" gene 1..262 /gene="thiM" Protein 1..262 /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=27224 Region 15..259 /region_name="HK" /note="Hydroxyethylthiazole kinase family; pfam02110" /db_xref="CDD:396609" Site order(30,32,38,42,48,50,70,72..73) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:238575" Site order(31..36,38..39,42,50..53,55..56,59..60,72..75, 108..109,194..197,243..244,246..248,250..251,254) /site_type="other" /note="multimerization interface [polypeptide binding]" /db_xref="CDD:238575" Site order(99,125,127,130,171,173,175,193,199,201) /site_type="other" /note="ATP binding site [chemical binding]" /db_xref="CDD:238575" ORIGIN 1 mqvdllssaq sahtlhlfhq hsplvhcmtn dvvqtftant llalgaspam vieteeasqf 61 aaiasallin vgtltqpraq amraaveqak ssqtpwtldp vavgaldyrr hfchellsfk 121 paairgnase imalagvang grgvdttdaa vnaipaaqtl aretgaivvv tgevdyvtdg 181 hravgihggd plmtkvvgtg calsavvaac calpgdmlen vasachwmkq ageravarse 241 gpgsfvphfl dalwqltqev qa