MULTISPECIES: threonine synthase [Enterovibrio].

LOCUS       WP_017004568             427 aa            linear   BCT 28-AUG-2024
ACCESSION   WP_017004568
VERSION     WP_017004568.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio
  ORGANISM  Enterovibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 427)
  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..427
                     /organism="Enterovibrio"
                     /db_xref="taxon:188143"
     gene            1..427
                     /gene="thrC"
     Protein         1..427
                     /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=46000
     Region          2..400
                     /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(104..105,134,246..250,351,374..375)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            105
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 mklynikend eqvsfgqavk qglgrnqglf fpselpkfdd idalldkdfv trsseilsal
       61 igdeltpdtv rsmvenafqf pasvekvtdt vsalelfhgp tlafkdfggr fmaqslaavs
      121 dggkvtilta tsgdtgaava haffgmenik vvilypkgki splqeklfct lggnihtvai
      181 ngtfddcqam vkdafddael raaiglnsan sinisrlmaq icyyfeaasq ltkaqrenlv
      241 vavpsgnfgn ltagllakai glpikrfiaa tnvndtvpry lktgewtptp tiatlsnamd
      301 vsqpnnwpri eelcqlqgwg lnelgsaavt deetaetlka mfdagylcep hgaiayraln
      361 eqlqdgehgl flctahpakf kesvdeilgl diplpgplak havmdllsve qdaefaqlra
      421 ylmkvag