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LOCUS WP_003114943 809 aa linear BCT 20-JAN-2025 ACCESSION WP_003114943 VERSION WP_003114943.1 KEYWORDS RefSeq. SOURCE Pseudomonas aeruginosa ORGANISM Pseudomonas aeruginosa Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. REFERENCE 1 (residues 1 to 809) AUTHORS Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and Prabhune,A. TITLE A new role for penicillin acylases: degradation of acyl homoserine lactone quorum sensing signals by Kluyvera citrophila penicillin G acylase JOURNAL Enzyme Microb Technol 56, 1-7 (2014) PUBMED 24564895 REFERENCE 2 (residues 1 to 809) AUTHORS Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and Quax,W.J. TITLE Molecular cloning and analysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis JOURNAL Appl Environ Microbiol 63 (9), 3412-3418 (1997) PUBMED 9292993 REFERENCE 3 (residues 1 to 809) AUTHORS Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and Moody,P.C. TITLE Penicillin acylase has a single-amino-acid catalytic centre JOURNAL Nature 373 (6511), 264-268 (1995) PUBMED 7816145 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 11457167 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..809 /organism="Pseudomonas aeruginosa" /db_xref="taxon:287" Protein 1..809 /product="penicillin acylase family protein" /EC_number="3.5.1.-" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /GO_function="GO:0016811 - hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [Evidence IEA]" /calculated_mol_wt=89580 Region 37..799 /region_name="PvdQ" /note="Acyl-homoserine lactone (AHL) acylase PvdQ [Secondary metabolites biosynthesis, transport and catabolism]; COG2366" /db_xref="CDD:441933" ORIGIN 1 msknaryawr lslgglllgl lacavyllav plgfkygeiq vghglehegr iawdaagvph 61 iraqsledgy fllgyshard rlwqmefarr yaggtlsevf gaktlpmdrf artlgfrrta 121 egiyanldap trvllqrysd ginaylelap aalplefslv rherpgpwgp vdslslhlly 181 swtlsanlgm qlqrlalaeh ldlarinevf apypgerppa trdyaslyrs lhgtpdagkl 241 lgqlpgsnve gigsnnwvvs asrsatgkpl landphlrlt npaafylasl kipglsltga 301 nfagaplfvi ghnqriawgy tntgshiqda ylervdpqdp rryltpdgyr pfetrleria 361 vrdgetvsle vrstrhgpvi sdiyeparlp qaqrdrlvia lawtgldrhd ktfpsllain 421 raegweqfld aaanfgvppq nmvyadvegn igyvsagrvp lrgadddlhg lapspgwesr 481 ydwvgyvpes akprslnpre gfiatanqri vppdnafdfg hdwvlpyryd rirewlggpg 541 qrtledslel qndefssvma sllpkmleqv sdpelrasea fallqgwnhq aaadlaapli 601 agywvraftr ellqprigtq llasgwnqrn ydgflrlild gqadlrfwcg qeqgcdlkln 661 qslrraldel raahgsapsg wkwgeahaal aehvpfhktp lralfdlknn kggdnfsvnv 721 grfdysdpan pfntriaatl rmvidladfd nsryalstrn sglpfdgatd lnelwargay 781 iriaddapda tdrqlvlrps asssgeprp