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LOCUS WP_014343459 265 aa linear BCT 24-DEC-2024 ACCESSION WP_014343459 VERSION WP_014343459.1 KEYWORDS RefSeq. SOURCE Klebsiella pneumoniae ORGANISM Klebsiella pneumoniae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella; Klebsiella pneumoniae complex. REFERENCE 1 (residues 1 to 265) AUTHORS Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P. TITLE The ESTHER database on alpha/beta hydrolase fold proteins - An overview of recent developments JOURNAL Chem Biol Interact 383, 110671 (2023) PUBMED 37582413 REFERENCE 2 (residues 1 to 265) 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 3 (residues 1 to 265) 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 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 11457220 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: incomplete on both ends. FEATURES Location/Qualifiers source 1..265 /organism="Klebsiella pneumoniae" /db_xref="taxon:573" Protein <1..>265 /product="alpha/beta hydrolase" /EC_number="3.-.-.-" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" Region <4..265 /region_name="Fes" /note="Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; COG2382" /db_xref="CDD:441948" ORIGIN 1 milvpgsild drevahgdlr tltyhskaln aerrlyvwtp pgysgtgdpl pvlyfyhgfg 61 dsglsaidqg ripqimdnll aegkikpmlv vvpdtetdip eavaenfppq errktfypln 121 aqaadkelmq diiplidarf nvrkdadgra laglsqggyq alvsgmnhle sfgwlatfsg 181 vttttvpnag veaqlkqpda inkqlrnftv vvgekdsvtg kdiaglksel ekqqikfdyh 241 qypglnhemd vwrpayaefv qklfk