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MULTISPECIES: Vmh family MBL fold metallo-hydrolase [Klebsiella].


LOCUS       WP_004189881             283 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_004189881
VERSION     WP_004189881.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Lu,W.J., Hsu,P.H. and Lin,H.V.
  TITLE     A Novel Cooperative Metallo-beta-Lactamase Fold Metallohydrolase
            from Pathogen Vibrio vulnificus Exhibits beta-Lactam
            Antibiotic-Degrading Activities
  JOURNAL   Antimicrob Agents Chemother 65 (9), e0032621 (2021)
   PUBMED   34228542
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 :: NF040580.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..283
                     /product="Vmh family MBL fold metallo-hydrolase"
                     /calculated_mol_wt=30709
     Region          1..283
                     /region_name="MBL_fold_Vmh"
                     /note="Vmh family MBL fold metallo-hydrolase; NF040580"
                     /db_xref="CDD:468554"
ORIGIN      
        1 mklsalavat alfsgavfaa pltlqtynpq ekglfavnst lvsgpheavl fdaqfsvkdg
       61 eklvemikkn gkplsrivit sgdpdfyfgl eplvkafpqa evvatpevvk hiaatkaakl
      121 aywgpqmkdg aptqvyvpqa leansftidg ekvtimqphd yaafvwiran ktilggtgva
      181 wgmhlwtadt qtpasrqqwr ntldqmialh pqrvipghyl gtppegdsav rftktylqqf
      241 eqalkthsds agvikameaq wpglaetssl elsakvntge mkw