MULTISPECIES: uroporphyrinogen decarboxylase [Shigella].

LOCUS       WP_000137636             354 aa            linear   BCT 17-NOV-2023
ACCESSION   WP_000137636
VERSION     WP_000137636.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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..354
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..354
                     /gene="hemE"
     Protein         1..354
                     /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=39098
     Region          10..347
                     /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..31,36,40,46,73..79,91,96,144,154,160,207,
                     209..210,248,327)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238368"
     Site            order(27,31,77,154,209,327)
                     /site_type="active"
                     /db_xref="CDD:238368"
ORIGIN      
        1 mtelkndryl rallrqpvdv tpvwmmrqag rylpeykatr aqagdfmslc knaelacevt
       61 lqplrrypld aailfsdilt vpdamglgly feagegprft spvtckadvd klpipdpede
      121 lgyvmnavrt irhelkgevp ligfsgspwt latymveggs skaftvikkm myadpqalha
      181 lldklaksvt lylnaqikag aqavmifdtw ggvltgrdyq qfslyymhki vdgllrendg
      241 rrvpvtlftk gggqwleama etgcdalgld wttdiadarr rvgnkvalqg nmdpsmlyap
      301 parieeevat ilagfghgeg hvfnlghgih qdvppehagv fveavhrlse qyhr