MULTISPECIES: threonine synthase [Klebsiella].

LOCUS       WP_002887863             426 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_002887863
VERSION     WP_002887863.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 426)
  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..426
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..426
                     /gene="thrC"
     Protein         1..426
                     /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=46549
     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 qglgkhqglf fphdlpefsl teiddmlaqd fvtrsakils
       61 afigdeipqd vlqqrvraaf afpapvskvq edvgclelfh gptlafkdfg grfmaqmlth
      121 iagdkpvtil tatsgdtgaa vahafyglpn vkvvilyprg kisplqeklf ctlggnietv
      181 aidgdfdacq alvkqafdde elkatlglns ansinisrll aqicyyfeaa aqlpqearnq
      241 lvisvpsgnf gdltagllak slglpikrfi aatnandtvp rylqggewap katqatlsna
      301 mdvsqpnnwp rveelfrrki wrlselgyaa vddettkaam relkaigyis ephaaiawra
      361 lrdqlqpgey glflgtahpa kfkesveeil qetlplpkel adradlplls hnlpadfaal
      421 rklmmg