MULTISPECIES: uroporphyrinogen decarboxylase [Pseudomonas].

LOCUS       WP_003114569             355 aa            linear   BCT 29-APR-2021
ACCESSION   WP_003114569
VERSION     WP_003114569.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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 :: TIGR01464.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..355
                     /gene="hemE"
     Protein         1..355
                     /product="uroporphyrinogen decarboxylase"
                     /EC_number="4.1.1.37"
                     /GO_function="GO:0004853 - uroporphyrinogen decarboxylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=38661
     Region          10..348
                     /region_name="URO-D"
                     /note="Uroporphyrinogen decarboxylase (URO-D) is a dimeric
                     cytosolic enzyme that decarboxylates the four acetate side
                     chains of uroporphyrinogen III (uro-III) to create
                     coproporphyrinogen III, without requiring any prosthetic
                     groups or cofactors. This reaction...; cd00717"
                     /db_xref="CDD:238368"
     Site            order(26..31,36,40,46,74..80,92,97,145,155,161,208,
                     210..211,249,328)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238368"
     Site            order(27,31,78,155,210,328)
                     /site_type="active"
                     /db_xref="CDD:238368"
ORIGIN      
        1 mtalkndrfl rallkqpvdv tpvwmmrqag rylpeyratr akagdfmslc mnpelacevt
       61 lqpldrypql daailfsdil tipdamgqgl yfetgegprf rkvvssladi ealpvpdpeq
      121 dlgyvmdavr tirrelngrv pligfsgspw tlatymvegg sskdfrkska mlydnpkamh
      181 alldklaqsv tsylngqiha gaqavqifds wggslsaaay qefslaymrk ivdglirehd
      241 grrvpvilft kggglwlesm aevgaealgl dwtcdigsar arvgervalq gnmdpsvlya
      301 npaairaeva rilaaygkgt ghvfnlghgi tpevdpahag affeavhels aqyhg