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LOCUS WP_000847449 377 aa linear BCT 04-JUN-2024 ACCESSION WP_000847449 VERSION WP_000847449.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 377) AUTHORS Leonardi,R. and Roach,P.L. TITLE Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity JOURNAL J Biol Chem 279 (17), 17054-17062 (2004) PUBMED 14757766 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 :: TIGR02351.2 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..377 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..377 /gene="thiH" Protein 1..377 /product="2-iminoacetate synthase ThiH" /GO_function="GO:0005506 - iron ion binding [Evidence IEA]" /GO_function="GO:0016829 - lyase activity [Evidence IEA]" /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster binding [Evidence IEA]" /GO_function="GO:1904047 - S-adenosyl-L-methionine binding [Evidence IEA]" /GO_process="GO:0009228 - thiamine biosynthetic process [Evidence IEA]" /calculated_mol_wt=43192 Region 3..369 /region_name="thiH" /note="thiazole biosynthesis protein ThiH; TIGR02351" /db_xref="CDD:131404" ORIGIN 1 mktfsdrwrq ldwddirlri ngktaadver alnasqltrd dmmallspaa sgyleqlaqr 61 aqrltrqrfg ntvsfyvply lsnlcandct ycgfsmsnri krktldeadi aresaairem 121 gfehlllvtg ehqakvgmdy frrhlpalre qfsslqmevq plaeteyael kqlgldgvmv 181 yqetyheaty arhhlkgkkq dffwrletpd rlgragidki glgaliglsd swrvdcymva 241 ehllwlqqhy wqsrysvsfp rlrpctggie pasimderql vqticafrll apeielslst 301 respwfrdrv iplainnvsa fsktqpggya dnhpeleqfs phderrpeav aaaltaqglq 361 pvwkdwdsyl grasqrl