MULTISPECIES: 3,4-dihydroxyphenylacetate 2,3-dioxygenase

LOCUS       WP_003093449             307 aa            linear   BCT 13-MAY-2024
            [Pseudomonas].
ACCESSION   WP_003093449
VERSION     WP_003093449.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Roper,D.I. and Cooper,R.A.
  TITLE     Subcloning and nucleotide sequence of the
            3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase
            gene from Escherichia coli C
  JOURNAL   FEBS Lett 275 (1-2), 53-57 (1990)
   PUBMED   2261999
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 :: TIGR02298.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..307
                     /gene="hpaD"
     Protein         1..307
                     /product="3,4-dihydroxyphenylacetate 2,3-dioxygenase"
                     /EC_number="1.13.11.15"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0008687 - 3,4-dihydroxyphenylacetate
                     2,3-dioxygenase activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=33231
     Region          3..282
                     /region_name="HPCD"
                     /note="The Class III extradiol dioxygenase,
                     homoprotocatechuate 2,3-dioxygenase, catalyzes the key
                     ring cleavage step in the metabolism of
                     homoprotocatechuate; cd07370"
                     /db_xref="CDD:153382"
     Site            order(12..14,57,125,186,241,272..273)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153382"
     Site            order(12,57)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:153382"
ORIGIN      
        1 mgkvalaaki thvpslylse lpgprhgcrq paidghreig rrcrelgvdt ivvfdthwlv
       61 nagyhincap hfeglytsne lphfianmey gfpgnpelgr ilaegcnalg vetlahdatt
      121 lgpeygtlvp mrymnqdrhf kvvsvsalct vhylndsarl gwamrkavee hydgtvafla
      181 sgslshrfaq ngqapdfsdr iwspflevld hevvqmwqeg rwaefcgmlp eyaskghgeg
      241 fmhdtamllg algwsaydgk aevvtpyfgs sgtgqinavf pvtaqdgsai paaqagnpag
      301 ascasrl