threonine synthase [Listeria monocytogenes].

LOCUS       WP_003729257             351 aa            linear   BCT 11-APR-2024
ACCESSION   WP_003729257
VERSION     WP_003729257.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 351)
  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..351
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..351
                     /gene="thrC"
     Protein         1..351
                     /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=36832
     Region          6..320
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(25,30..31,53,76,92,95..96,102,119..125,127..129,
                     141..142,172,276..278,280..281,316)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(59,85,185..189,314)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            59
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mykgllekyk eylpvtdktp mislaegntp liplpnlske lgvtlygkye glnptgsfkd
       61 rgmvmavaka keegaeavic astgntsaaa aayatraglk ayivipegkv algklaqavm
      121 ygadiisiqg nfdealksvr elaeteavtl vnsvnpyrle gqktaafeic eqlgsapdvl
      181 aipvgnagni saywkgfkew neakasglpr mhgfeaegaa aivqgkpidn petiatairi
      241 gnpaswglae aardesggyi hsvtddeivn aykkiaaqdg vfiepgsaas lagviqhvan
      301 gtikkgetvv cvftgnglkd pdtamsvhei pishvddiea mrthlrsgvk a