threonine synthase [Shigella flexneri].

LOCUS       WP_000781034             428 aa            linear   BCT 08-JUN-2021
ACCESSION   WP_000781034
VERSION     WP_000781034.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
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 :: TIGR00260.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..428
                     /gene="thrC"
     Protein         1..428
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47088
     Region          2..423
                     /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            order(106..107,136,248..252,353,376..377)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107203"
     Site            107
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107203"
ORIGIN      
        1 mklynlkdhn eqvsfaqavt qglgknqglf fphdlpefsl teidemlkld fvtrnakils
       61 afigdeipqe ileervraaf afpapvanve sdvgclelfh gptlafkdfg grfmaqmlth
      121 iaddkpvtil tatsgdtgaa vahafyglpn vkvvilyprg kisplqeklf ctlggnietv
      181 aidgdfdacq alvkqafdde elkvalglns ansinisrll aqicyyfeav aqlpqearnq
      241 lvvsvpsgnf gdltagllak sfglpvkrfi aatnvndtvp rflhdgqwsp katqatlsna
      301 mdvsqpnnwp rveelfrrki wqlkelgyaa vddettqqtm relkelgyts ephaavayra
      361 lrdqlnpgey glflgtahpa kfkesveail getldlpkel aeradlplls hnlpadfsal
      421 rklmmnhq