MULTISPECIES: biliverdin-producing heme oxygenase [Pseudomonas].

FASTA View on NCBI
LOCUS       WP_003159301             195 aa            linear   BCT 27-FEB-2025
ACCESSION   WP_003159301
VERSION     WP_003159301.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Wilks,A.
  TITLE     Heme oxygenase: evolution, structure, and mechanism
  JOURNAL   Antioxid Redox Signal 4 (4), 603-614 (2002)
   PUBMED   12230872
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Ryter,S.W. and Tyrrell,R.M.
  TITLE     The heme synthesis and degradation pathways: role in oxidant
            sensitivity. Heme oxygenase has both pro- and antioxidant
            properties
  JOURNAL   Free Radic Biol Med 28 (2), 289-309 (2000)
   PUBMED   11281297
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Maines,M.D.
  TITLE     Heme oxygenase: function, multiplicity, regulatory mechanisms, and
            clinical applications
  JOURNAL   FASEB J 2 (10), 2557-2568 (1988)
   PUBMED   3290025
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10471538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..195
                     /product="biliverdin-producing heme oxygenase"
                     /EC_number="1.14.14.18"
                     /GO_function="GO:0004392 - heme oxygenase (decyclizing)
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006788 - heme oxidation [Evidence IEA]"
                     /calculated_mol_wt=21333
     Region          6..193
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(13,20,23..24,117..118,121..122,124..125,128..129,
                     156,184,187)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350857"
     Region          110..136
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350857"
ORIGIN      
        1 mspspspala alrdatrdlh aeldrrsplg dddlddrayl dhagrilgwl epleralrdn
       61 rsgwpaalra darlvkstwl esdllaggms raqvealprc adlpnatraa evfgvayvme
      121 gatlggayly krlaprlpgl plqwlqgygq atgvrwqefl eqlarqidsp eaiglaqdaa
      181 qatflsfrrw vldea