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LOCUS WP_002882812 305 aa linear BCT 31-DEC-2024 ACCESSION WP_002882812 VERSION WP_002882812.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 305) 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 305) 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 305) 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 11171394 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..305 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..305 /product="alpha/beta hydrolase" /EC_number="3.-.-.-" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /calculated_mol_wt=33215 Region 75..280 /region_name="Abhydrolase_3" /note="alpha/beta hydrolase fold; pfam07859" /db_xref="CDD:400284" ORIGIN 1 malekgiasl veafiaagrp ssrdqhiddr ragyiasavl agetetrvrv editlegmhf 61 rvvspptadg llptliyyhg gcfvsggfat hdnqlrqlaw fsgcrviavq yrlapeypfp 121 aahddaerga tiihqhakql gvdvsritla gdsagghlal vtalrlkaka awqpaqlili 181 ypmldptasm asylsngddy vitrdtllsg yemylastpa nhpdacplwr edfnglppvh 241 iltaefdplr degevlyrrl teqgvesscq rylgvihgff qlggvsnaar damrdiawrv 301 aspgr