MULTISPECIES: diaminopropionate ammonia-lyase [Klebsiella].

LOCUS       WP_002898211             383 aa            linear   BCT 12-JAN-2021
ACCESSION   WP_002898211
VERSION     WP_002898211.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Uo,T., Yoshimura,T., Nishiyama,T. and Esaki,N.
  TITLE     Gene cloning, purification, and characterization of
            2,3-diaminopropionate ammonia-lyase from Escherichia coli
  JOURNAL   Biosci. Biotechnol. Biochem. 66 (12), 2639-2644 (2002)
   PUBMED   12596860
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 :: TIGR03528.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..383
                     /gene="dpaL"
     Protein         1..383
                     /product="diaminopropionate ammonia-lyase"
                     /EC_number="4.3.1.15"
                     /GO_function="GO:0008838 - diaminopropionate ammonia-lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41684
     Region          2..380
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     Site            57
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 msllnesvgn evlafhqkfp dyrvtplrkl eflsqrlglg sihikdeaqr fglnafkglg
       61 gsyamgkyla allerdintl sfaelnspvi karikdivfv tatdgnhgrg vawaaeqlgl
      121 ravvympkgs spvraqnirr hgaectitel nyddtvrlaa ktareqgwvl lqdtawqgye
      181 qiptwimqgy mtlaveiwqq laesgapmpt hlflqagvgs fagsimgyfi ekmqqqapti
      241 iivephkanc lyrsatindg lphsvggdms tlmaglacge pnitswpmlr dhatcfisad
      301 dclaangmrl laaprpgtde pfvsgesgai gtgvlyalmt qpayrelaes lrlnadaqvl
      361 listegdtsp dvyedivwfg rng