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LOCUS WP_000860179 252 aa linear BCT 19-MAY-2021 ACCESSION WP_000860179 VERSION WP_000860179.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 252) AUTHORS Light,S.H., Minasov,G., Shuvalova,L., Duban,M.E., Caffrey,M., Anderson,W.F. and Lavie,A. TITLE Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates JOURNAL J Biol Chem 286 (5), 3531-3539 (2011) PUBMED 21087925 REMARK Erratum:[J Biol Chem. 2015 Jul 31;290(31):19008. PMID: 26232400] 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 :: TIGR01093.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..252 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..252 /gene="aroD" Protein 1..252 /product="type I 3-dehydroquinate dehydratase" /EC_number="4.2.1.10" /GO_function="GO:0003855 - 3-dehydroquinate dehydratase activity [Evidence IEA]" /GO_process="GO:0009423 - chorismate biosynthetic process [Evidence IEA]" /calculated_mol_wt=27359 Region 1..252 /region_name="aroD" /note="type I 3-dehydroquinate dehydratase; PRK02412" /db_xref="CDD:235036" Site order(21,46,48,82,143,170,213,232..233,236) /site_type="active" /db_xref="CDD:188633" Site 170 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:188633" Site order(182,186,189,214..215,219,241,245,248) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:188633" ORIGIN 1 mktvtvkdlv igtgapkiiv slmakdiarv ksealayrea dfdilewrvd hfadlsnves 61 vmaaakilre tmpekpllft frsakeggeq aisteayial nraaidsglv dmidlelftg 121 ddqvketvay ahahdvkvvm snhdfhktpe aeeiiarlrk mqsfdadipk ialmpqstsd 181 vlallaatle mqeqyadrpi itmsmaktgv isrlagevfg saatfgavkk asapgqisvn 241 dlrtvltilh qa