diaminopimelate decarboxylase [Escherichia coli].

LOCUS       WP_001120698             420 aa            linear   BCT 29-JUN-2021
ACCESSION   WP_001120698
VERSION     WP_001120698.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 :: TIGR01048.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..420
                     /gene="lysA"
     Protein         1..420
                     /product="diaminopimelate decarboxylase"
                     /EC_number="4.1.1.20"
                     /GO_function="GO:0008836 - diaminopimelate decarboxylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009089 - lysine biosynthetic process via
                     diaminopimelate [Evidence IEA]"
                     /calculated_mol_wt=46090
     Region          2..411
                     /region_name="lysA"
                     /note="diaminopimelate decarboxylase; TIGR01048"
                     /db_xref="CDD:273415"
     Site            order(52,54,73,100,142,189,191,194,226..227,268..271,307,
                     311,342,378,382,386)
                     /site_type="active"
                     /db_xref="CDD:143501"
     Site            order(52,54,73,100,142,189,191,194,226..227,268..271,342,
                     378)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143501"
     Site            order(54,191,194,271,307,311,342..343,378,382,386)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143501"
     Site            order(54,342)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143501"
     Site            order(59..60,75..76,78..79,102..104,108,122,125,162..165,
                     286,288,295,297,339..344,346,381..383,385..388,391)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143501"
ORIGIN      
        1 mphslfstdt dltaenllrl paefgcpvwv ydaqiirrqi aalkqfdvvr faqkacsnih
       61 ilrlmreqgv kvdsvslgei eralaagynp qthpddivft advidqatle rvselqipvn
      121 agsvdmfdql gqvspghrvw lrvnpgfghg hsqktntgge nskhgiwytd lpaaldviqr
      181 hhlqlvgihm higsgvdyah leqvcgamvr qviefgqdlq aisaggglsi pyqqgeeavd
      241 tehyyglwna areqiarhlg hpvkleiepg rflvaqsgvl itqvrsvkqm gsrhfvlvda
      301 gfndlmrpam ygsyhhisal aadgrsleha ptvetvvagp lcesgdvftq qeggnvepra
      361 lpevkagdyl vlhdtgayga smssnynsrp llpevlfdng qarlirrrqt ieellalell