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: catechol 1,2-dioxygenase [Pseudomonas].


LOCUS       WP_003113307             310 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_003113307
VERSION     WP_003113307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 310)
  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..310
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..310
                     /gene="catA"
     Protein         1..310
                     /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=34029
     Region          8..290
                     /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 mtvkisqtad vqrffeeasg qlnergdprt kalvrrildd taklieemqv tpdefwkavd
       61 ylnrlgsrqe agllaaglgl ehyldlllda qdaeagltgg tprtiegply vagaplsdge
      121 armddgrdag tvmflqgrvs gpdgqplaga ivdvwhantq gtysyfdssq seynlrrrir
      181 tdadgryrar sivpsgygcp sdgptqelld rlgrhgqrpa hihffvsapg hrhlttqinl
      241 agdrylwddf ayatrdglig dlrfnddpaa ardrgveggr faeldfdfql qaspapaaer
      301 rsqrpralqg