Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: phosphotriesterase family protein [Klebsiella].


LOCUS       WP_004176149             359 aa            linear   BCT 18-FEB-2025
ACCESSION   WP_004176149
VERSION     WP_004176149.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
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 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..359
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39662
     Region          18..359
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mkgsifrhps plpvgvssgy vmtvlgplpi nemgvtlmhe hilldasgkw vppcccsdrh
       61 laempvkmen lgelslnplm srdncqlfdv dvaideltky ralggetvvd ptnigigrdp
      121 kalariarlt glniimgtgl ylepshpewv kissveqlte rliydlggae ekpevlagli
      181 geigissrft pdeekslraa grasaatgvp ievhlpgwer lghrvldile qegadlrhtv
      241 lchmnpsfad kryqrelaqr gafleydmig msyyyadesa qspsdeenar aireliddgy
      301 iqqillsqdv flktmltryg ghgygyilkh fvprlrrhgv sgeqletlmi gnpqrvfgg