MULTISPECIES: catechol 1,2-dioxygenase [Klebsiella].

LOCUS       WP_004175986             308 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_004175986
VERSION     WP_004175986.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Kim,S.I., Leem,S.H., Choi,J.S., Chung,Y.H., Kim,S., Park,Y.M.,
            Park,Y.K., Lee,Y.N. and Ha,K.S.
  TITLE     Cloning and characterization of two catA genes in Acinetobacter
            lwoffii K24
  JOURNAL   J Bacteriol 179 (16), 5226-5231 (1997)
   PUBMED   9260969
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 :: TIGR02439.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..308
                     /gene="catA"
     Protein         1..308
                     /product="catechol 1,2-dioxygenase"
                     /EC_number="1.13.11.1"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0018576 - catechol 1,2-dioxygenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0019615 - catechol catabolic process,
                     ortho-cleavage [Evidence IEA]"
                     /calculated_mol_wt=34157
     Region          11..289
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Site            order(155,163,197,218,221,223,250)
                     /site_type="active"
                     /db_xref="CDD:238241"
ORIGIN      
        1 msnvfvqqpa iqkllrdsag ldvaggderf kaiihrllen ictliddynv teeefwhavn
       61 ylhelggrqe aallaaglgl ehfldlrqda idaaahretg tprtiegply vanaplaegh
      121 armddgadag evmwlhgevk dtegrpvana ivdiwhantl gnysffdpgq seynlrrrir
      181 tgadgrysvr simpsgygcp pdgptqklld rlgrhgnrpa hihffvsapg hkhltsqinl
      241 ngdkylwddf afatrdglia dpvkvtdrei iaqrnlegeh tevcfdftlc kalsadeeqr
      301 girvrake