MULTISPECIES: uroporphyrinogen decarboxylase [Salmonella].

LOCUS       WP_000137623             354 aa            linear   BCT 29-APR-2021
ACCESSION   WP_000137623
VERSION     WP_000137623.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            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="Salmonella"
                     /db_xref="taxon:590"
     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=39001
     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 ipdamglgly feagegprft apvtckadve klpipdpege
      121 lgyvmnavrt irrelkgevp ligfsgspwt latymveggs skaftvikkm myadpqalhl
      181 lldklaksvt lylnaqikag aqsvmifdtw ggvltgrdyq qfslyymhki vdgllrendg
      241 rrvpvtlftk gggqwleama etgcdalgld wttdiadarr rvghkvalqg nmdpsmlyap
      301 pariedevat ilagfgqgeg hvfnlghgih qdvppehaga fveavhrlsa qyhn