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MULTISPECIES: MBL fold metallo-hydrolase [Pseudomonas].


LOCUS       WP_003085806             213 aa            linear   BCT 01-MAR-2025
ACCESSION   WP_003085806
VERSION     WP_003085806.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Neuwald,A.F., Liu,J.S., Lipman,D.J. and Lawrence,C.E.
  TITLE     Extracting protein alignment models from the sequence database
  JOURNAL   Nucleic Acids Res 25 (9), 1665-1677 (1997)
   PUBMED   9108146
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Carfi,A., Pares,S., Duee,E., Galleni,M., Duez,C., Frere,J.M. and
            Dideberg,O.
  TITLE     The 3-D structure of a zinc metallo-beta-lactamase from Bacillus
            cereus reveals a new type of protein fold
  JOURNAL   EMBO J 14 (20), 4914-4921 (1995)
   PUBMED   7588620
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 :: NF012955.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00753.33
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..213
                     /product="MBL fold metallo-hydrolase"
                     /calculated_mol_wt=23352
     Region          10..195
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Site            order(62,64,66..67,135..136,154,195)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mstspalire tfpvgplqcn ctiigdpltr kaivvdpggd helilqrldr lglqvvsiih
       61 thahldhfla sgemkkrtga slhlhkddqf lwdnlemqcq lfgvpytpvp apdrwladde
      121 elacgcgval htpghtpgsm sfwfprakll iagdtlfrrg igrtdlwggd saaiqrsirq
      181 rlysldedat vvaghgpdtt lgeemrenpf vrg