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MULTISPECIES: fumarylacetoacetate hydrolase family protein


LOCUS       WP_002887498             254 aa            linear   BCT 02-MAR-2025
            [Klebsiella].
ACCESSION   WP_002887498
VERSION     WP_002887498.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Pollard,J.R. and Bugg,T.D.
  TITLE     Purification, characterisation and reaction mechanism of
            monofunctional 2-hydroxypentadienoic acid hydratase from
            Escherichia coli
  JOURNAL   Eur J Biochem 251 (1-2), 98-106 (1998)
   PUBMED   9492273
REFERENCE   2  (residues 1 to 254)
  AUTHORS   St-Louis,M. and Tanguay,R.M.
  TITLE     Mutations in the fumarylacetoacetate hydrolase gene causing
            hereditary tyrosinemia type I: overview
  JOURNAL   Hum Mutat 9 (4), 291-299 (1997)
   PUBMED   9101289
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Prieto,M.A., Diaz,E. and Garcia,J.L.
  TITLE     Molecular characterization of the 4-hydroxyphenylacetate catabolic
            pathway of Escherichia coli W: engineering a mobile aromatic
            degradative cluster
  JOURNAL   J Bacteriol 178 (1), 111-120 (1996)
   PUBMED   8550403
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Fernandez-Canon,J.M. and Penalva,M.A.
  TITLE     Fungal metabolic model for human type I hereditary tyrosinaemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (20), 9132-9136 (1995)
   PUBMED   7568087
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Roper,D.I., Stringfellow,J.M. and Cooper,R.A.
  TITLE     Sequence of the hpcC and hpcG genes of the meta-fission
            homoprotocatechuic acid pathway of Escherichia coli C: nearly 40%
            amino-acid identity with the analogous enzymes of the catechol
            pathway
  JOURNAL   Gene 156 (1), 47-51 (1995)
   PUBMED   7737515
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Roper,D.I. and Cooper,R.A.
  TITLE     Purification, nucleotide sequence and some properties of a
            bifunctional isomerase/decarboxylase from the homoprotocatechuate
            degradative pathway of Escherichia coli C
  JOURNAL   Eur J Biochem 217 (2), 575-580 (1993)
   PUBMED   8223600
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Harayama,S. and Rekik,M.
  TITLE     Comparison of the nucleotide sequences of the meta-cleavage pathway
            genes of TOL plasmid pWW0 from Pseudomonas putida with other
            meta-cleavage genes suggests that both single and multiple
            nucleotide substitutions contribute to enzyme evolution
  JOURNAL   Mol Gen Genet 239 (1-2), 81-89 (1993)
   PUBMED   8510667
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 :: NF013706.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01557.23
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..254
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28505
     Region          <25..248
                     /region_name="PRK15203"
                     /note="4-hydroxyphenylacetate degradation bifunctional
                     isomerase/decarboxylase; Provisional"
                     /db_xref="CDD:185125"
ORIGIN      
        1 mkqariewqg qvrdvlvner dqvrlddgtv lkegefrwlp pangtlfalg lnyadhasel
       61 efkppteplv fikapntftg hqqqsvrpdn veymhyeael vvvigktarr vseaeamdyv
      121 agytvcndya irdylenyyr pnlrvksrdt ltpigpwivs keaipdphnl alrtwvngel
      181 rqqgttadli fsipfliayl sefmtlqpgd miatgtpkgl sdvvpgdevi vevegvgrlv
      241 nhiisqqaye etls