MULTISPECIES: porphobilinogen synthase [Salmonella].

LOCUS       WP_000130724             324 aa            linear   BCT 20-JUN-2019
ACCESSION   WP_000130724
VERSION     WP_000130724.1
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 :: NF009923.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK13384
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..324
                     /gene="hemB"
     Protein         1..324
                     /product="porphobilinogen synthase"
                     /EC_number="4.2.1.24"
                     /GO_function="GO:0004655 - porphobilinogen synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35417
     Region          4..319
                     /region_name="ALAD_PBGS"
                     /note="Porphobilinogen synthase (PBGS), which is also
                     called delta-aminolevulinic acid dehydratase (ALAD),
                     catalyzes the condensation of two 5-aminolevulinic acid
                     (ALA) molecules to form the pyrrole porphobilinogen (PBG),
                     which is the second step in the...; cl00338"
                     /db_xref="CDD:469728"
     Site            order(9,12..13,24,48,51,140..141,168..169,198..200,219,
                     222,228,231..232,250..254,278,296,300,303)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238226"
     Site            order(118,120,122,130,165,195,201,204..205,210,216,220,
                     247,270,273,312)
                     /site_type="active"
                     /db_xref="CDD:238226"
     Site            order(195,247)
                     /site_type="active"
                     /note="Schiff base residues [active]"
                     /db_xref="CDD:238226"
ORIGIN      
        1 mtdlihrprr lrksaalram feettlslnd lvlpifveee lddykaidam pgvmripekq
       61 lareierian agirsvmtfg ishhtddtgs dtwkedglva rmsrickqtv pemivmsdtc
      121 fceytshghc gvlcehgvdn datlanlgkq aviaaaagad fiapsaamdg qvqairqald
      181 aagftdtaim systkfassf ygpfreaagt alkgdrktyq mnpmnrreai reslldeaqg
      241 adclmvkpag ayldvlreir ertelplgay qvsgeyamik faamagaide ekvvleslgs
      301 ikragadlif syfaldlaek nilr