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amidohydrolase family protein [Klebsiella pneumoniae].


LOCUS       WP_014342990             161 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_014342990
VERSION     WP_014342990.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Gao,G., Nara,T., Nakajima-Shimada,J. and Aoki,T.
  TITLE     Novel organization and sequences of five genes encoding all six
            enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi
  JOURNAL   J Mol Biol 285 (1), 149-161 (1999)
   PUBMED   9878395
REFERENCE   2  (residues 1 to 161)
  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   3  (residues 1 to 161)
  AUTHORS   Nygaard,P., Duckert,P. and Saxild,H.H.
  TITLE     Role of adenine deaminase in purine salvage and nitrogen metabolism
            and characterization of the ade gene in Bacillus subtilis
  JOURNAL   J Bacteriol 178 (3), 846-853 (1996)
   PUBMED   8550522
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Lollier,M., Jaquet,L., Nedeva,T., Lacroute,F., Potier,S. and
            Souciet,J.L.
  TITLE     As in Saccharomyces cerevisiae, aspartate transcarbamoylase is
            assembled on a multifunctional protein including a
            dihydroorotase-like cryptic domain in Schizosaccharomyces pombe
  JOURNAL   Curr Genet 28 (2), 138-149 (1995)
   PUBMED   8590465
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Jabri,E., Carr,M.B., Hausinger,R.P. and Karplus,P.A.
  TITLE     The crystal structure of urease from Klebsiella aerogenes
  JOURNAL   Science 268 (5213), 998-1004 (1995)
   PUBMED   7754395
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 :: NF014081.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01979.26
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..161
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17697
     Region          <2..160
                     /region_name="PyrC"
                     /note="Dihydroorotase [Nucleotide transport and
                     metabolism]; COG0418"
                     /db_xref="CDD:440187"
ORIGIN      
        1 mrdgnellaa titpqhlmfn rnhmlvggir phlyclpvlk rnihqqalre lvasgfsraf
       61 lgtdsaphar hrkeascgca gcfnaptalg syatvfeemn alqhfeafcs lngprfyglp
      121 vnesyvelvr eettvvdsia lpndalvpfl agetvrwtvk k