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LOCUS WP_000213959 270 aa linear BCT 23-JUL-2024 ACCESSION WP_000213959 VERSION WP_000213959.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 270) AUTHORS Carr,P.D. and Ollis,D.L. TITLE Alpha/beta hydrolase fold: an update JOURNAL Protein Pept Lett 16 (10), 1137-1148 (2009) PUBMED 19508187 REFERENCE 2 (residues 1 to 270) AUTHORS Holmquist,M. TITLE Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms JOURNAL Curr Protein Pept Sci 1 (2), 209-235 (2000) PUBMED 12369917 REFERENCE 3 (residues 1 to 270) AUTHORS Pathak,D. and Ollis,D. TITLE Refined structure of dienelactone hydrolase at 1.8 A JOURNAL J Mol Biol 214 (2), 497-525 (1990) PUBMED 2380986 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 11123939 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..270 /organism="Salmonella" /db_xref="taxon:590" Protein 1..270 /product="dienelactone hydrolase family protein" /EC_number="3.-.-.-" /EC_number="3.1.-.-" /GO_component="GO:0005829 - cytosol [Evidence IEA]" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /calculated_mol_wt=28931 Region 43..264 /region_name="DLH" /note="Dienelactone hydrolase family; pfam01738" /db_xref="CDD:396343" ORIGIN 1 mttthpsgfa paasplaptm ihtpdgaisa gitsipsqgd dmpayyarpk asdgalpvvi 61 vvqeifgvhe hirdicrrla legylaiape lyfregdpnd fadiptllsg lvakvpdsqv 121 ladldhvasw asrnggdahr lmitgfcwgg ritwlyaahn pqlkaavawy gklvgdtsln 181 spkhpvdiat dlnapvlgly ggqdtsipqe svetmrqalr aanakaeivv ypdaghafna 241 dyrpgyheas akdgwqrmle wfaqyggkkg