LOCUS       WP_003825942             326 aa            linear   BCT 29-DEC-2023
DEFINITION  prephenate dehydratase domain-containing protein [Bifidobacterium
            angulatum].
ACCESSION   WP_003825942
VERSION     WP_003825942.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium angulatum
  ORGANISM  Bifidobacterium angulatum
            Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
            Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Tan,K., Li,H., Zhang,R., Gu,M., Clancy,S.T. and Joachimiak,A.
  TITLE     Structures of open (R) and close (T) states of prephenate
            dehydratase (PDT)--implication of allosteric regulation by
            L-phenylalanine
  JOURNAL   J Struct Biol 162 (1), 94-107 (2008)
   PUBMED   18171624
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Zhang,S., Pohnert,G., Kongsaeree,P., Wilson,D.B., Clardy,J. and
            Ganem,B.
  TITLE     Chorismate mutase-prephenate dehydratase from Escherichia coli.
            Study of catalytic and regulatory domains using genetically
            engineered proteins
  JOURNAL   J Biol Chem 273 (11), 6248-6253 (1998)
   PUBMED   9497350
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 :: NF012998.4
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00800.22
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Bifidobacterium angulatum"
                     /db_xref="taxon:1683"
     Protein         1..326
                     /product="prephenate dehydratase domain-containing
                     protein"
                     /GO_function="GO:0004664 - prephenate dehydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009094 - L-phenylalanine biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35480
     Region          4..189
                     /region_name="PBP2_Aa-PDT_like"
                     /note="Catalytic domain of prephenate dehydratase from
                     Arthrobacter aurescens and similar proteins, subgroup 3;
                     the type 2 periplasmic binding protein fold; cd13632"
                     /db_xref="CDD:270350"
     Site            order(9,43..44)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270350"
     Site            order(43,49,63,118,120,124)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270350"
     Region          205..284
                     /region_name="ACT_CM-PDT"
                     /note="C-terminal ACT domain of the bifunctional
                     chorismate mutase-prephenate dehydratase (CM-PDT) enzyme
                     and the prephenate dehydratase (PDT) enzyme; cd04905"
                     /db_xref="CDD:153177"
     Site            order(217..220,237..240)
                     /site_type="other"
                     /note="putative L-Phe binding site [chemical binding]"
                     /db_xref="CDD:153177"
ORIGIN      
        1 mthmkltylg pegtfthqaa ieaghclktq ygidepelva apdvtsimas vqsgeswgvi
       61 awennvegyv mpnldalida hdaaglarvg invsfdafvt pgtsqigidg asvsahphgl
      121 aqckrfierh rlhpaqassn aaacrdlkpg nvalgphicg dlygleilee hvedfdgaht
      181 dflviaprgd vldyvartre refetvitfi platgpgvva nlldvlrdcg lnmtslisrp
      241 ikghdgtysf iitldaapwe prfrrmlvev aehgdwakti avyprrerpn ppvdswmlpe
      301 ggvrldssas tsdwqtaqna rrellw
//