tryptophan synthase subunit alpha [Enterovibrio norvegicus].

LOCUS       WP_017013926             273 aa            linear   BCT 02-JUN-2021
ACCESSION   WP_017013926
VERSION     WP_017013926.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio norvegicus
  ORGANISM  Enterovibrio norvegicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Dunn,M.F.
  TITLE     Allosteric regulation of substrate channeling and catalysis in the
            tryptophan synthase bienzyme complex
  JOURNAL   Arch Biochem Biophys 519 (2), 154-166 (2012)
   PUBMED   22310642
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Hyde,C.C., Ahmed,S.A., Padlan,E.A., Miles,E.W. and Davies,D.R.
  TITLE     Three-dimensional structure of the tryptophan synthase alpha 2 beta
            2 multienzyme complex from Salmonella typhimurium
  JOURNAL   J Biol Chem 263 (33), 17857-17871 (1988)
   PUBMED   3053720
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 :: TIGR00262.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Enterovibrio norvegicus"
                     /db_xref="taxon:188144"
     gene            1..273
                     /gene="trpA"
     Protein         1..273
                     /product="tryptophan synthase subunit alpha"
                     /EC_number="4.2.1.20"
                     /GO_function="GO:0004834 - tryptophan synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28633
     Region          13..268
                     /region_name="TIM-like beta/alpha barrel domains"
                     /note="A large family of domains similar to triose
                     phosphate isomerase (TIM) which, in general, share an
                     eight beta/alpha closed barrel structure; cl21457"
                     /db_xref="CDD:473867"
     Site            order(54,65,69,180,188..189,217..218,239..240)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:240075"
     Site            order(54,65,107,188)
                     /site_type="active"
                     /db_xref="CDD:240075"
     Site            order(54,65,107)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:240075"
     Site            order(59..62,64,67,70..71,109,112,134..135,137,140,160,
                     162..164,167)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:240075"
ORIGIN      
        1 maatlshrye amfenldakg egafvpfvti gdpnpeqslk iietlvanga dalelgipfs
       61 dpladgptiq gaairaldsg ttpdncfdil rqvrenhpei pmgllmyanl vfangidnfy
      121 akcadagvds vliadvpage skefrdsaak hgvhaifiap pnanedtlkt iselgggyty
      181 llsragvtga etkagqpidh llkklsdyga prpllgfgis epsqvkeait agaagaisgs
      241 avvkiiernv ddeptmlkel gefvvnlkaa tkk