MULTISPECIES: uroporphyrinogen decarboxylase [Klebsiella].

LOCUS       WP_002884329             354 aa            linear   BCT 29-APR-2021
ACCESSION   WP_002884329
VERSION     WP_002884329.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=39081
     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 spvkskadvd klpipdpeqe
      121 lgyvmnavrt irrelkgevp ligfsgspwt latymveggs skaftvikkm myaepqalha
      181 lldklaksvt lylnaqikag aqsvmifdtw ggvltgrdyq qfslyymhki vdgllreneg
      241 rrvpvtlftk gggqwleama etgcdalgld wttdiadarr rvgnkvalqg nmdpsmlyas
      301 aprieeevat ilagfgqgeg hvfnlghgih qdvdpehagv fveavhrlsa pyhq