>WP_083818547.1 NCBI__GCF_000223395.1:WP_083818547.1
MVVGEELGRALRELIEAAVRLEEVARRVGPPPVPEDTPGWLRPALVRLVGLAAGGSPRVSFLGPRGSFSHEAVRAVFGGAAREMPAHSISAAVTMLVEGVVDYAVVPYENSIEGPVGETLRALAESADVVRVWAEYVHPIVLVLAARSDGEVRKVYGHPHALGEARDWLERNLPHAELIPVASTSKAAEMAAREDGAAAVCSRLAAELYGLRIVAEGLATRPNFTRFLVLHHRDNPETGSKTSIVAAVRHEPGSLYRLLEVFAERRINLTMIYSYPVPGSPWSYYFFIDMEGSRRDEKIREALEEAEKRALWLRVLGSYPVLHG
>SwissProt__P27603 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 (Stutzerimonas stutzeri (Pseudomonas stutzeri))
MSEADQLKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWVLKHIMELNKGPLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVISKPMAAIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHLLVGETTKTDRITRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNADAAKRVKSEWNSAAIAGDMAAQLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVSMRNKPGALHELLMPFHSNGIDLTRIETRPSRSGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGSYPKAVL
>PDB_3mwb_B The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
VTYTFLGPQGTFTEAALMQVPGAADATRIPCTNVNTALERVRAGEADAAMVPIENSVEGGVTATLDAIATGQELRIIREA
LVPITFVLVARPGVELSDIKRISTHGHAWAQCRLWVDEHLPNADYVPGSSTAASAMGLLEDDAPYEAAICAPLIAAEQPG
LNVLAEDIGDNPDAVTRFILVSRPGALPERTGADKTTVVVPLPEDHPGALMEILDQFASRGVNLSRIESRPTLGHYFFSI
DADGHATDSRVADALAGLHRISPATRFLGSYARADKQPAVVAPHTSDAAFASAHAWVDSILKG
>biolip__3mwbA The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
VTYTFLGPQGTFTEAALMQVPGAADATRIPCTNVNTALERVRAGEADAAMVPIENSVEGGVTATLDAIATGQELRIIREALVPITFVLVARPGVELSDIKRISTHGHAWAQCRLWVDEHLPNADYVPGSSTAASAMGLLEDDAPYEAAICAPLIAAEQPGLNVLAEDIGDNPDAVTRFILVSRPGALPERTGADKTTVVVPLPEDHPGALMEILDQFASRGVNLSRIESRPTGQYLGHYFFSIDADGHATDSRVADALAGLHRISPATRFLGSYARADKQPAVVAPHTSDAAFASAHAWVDSILKG
>SwissProt__P9WIC3 Prephenate dehydratase; PDT; EC 4.2.1.51 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MVRIAYLGPEGTFTEAALVRMVAAGLVPETGPDALQRMPVESAPAALAAVRDGGADYACVPIENSIDGSVLPTLDSLAIGVRLQVFAETTLDVTFSIVVKPGRNAADVRTLAAFPVAAAQVRQWLAAHLPAADLRPAYSNADAARQVADGLVDAAVTSPLAAARWGLAALADGVVDESNARTRFVLVGRPGPPPARTGADRTSAVLRIDNQPGALVAALAEFGIRGIDLTRIESRPTRTELGTYLFFVDCVGHIDDEAVAEALKAVHRRCADVRYLGSWPTGPAAGAQPPLVDEASRWLARLRAGKPEQTLVRPDDQGAQA
>ENA__AAA88840.1 prephenate dehydratase (Amycolatopsis methanolica)
MSRIAYFGPVGTFTEQAARTFMAAGDELVAAETIPKALDAVRRGEADAACVPVENSVEGAVPATLDSLAVGEPLIGVAEALLPVHFSVLTRDDVGEIRTVASHPHALAQVRKWLEDNLPGARVVAAGSTAAAAVAVQAGEFDAAVTAPVAVEHYPLKVLATEVADVRDARTRFLLMRRPPVVLPEPTGADRTSIVAAAANRTGTLAELLTELATRGINLTRLDARPHKQNFGEYRFFIDFEGHVAEPRIADALAALRRRCRDVRFLGSFARADGVAATIEPAARNEDFTDAADWVAAVQRGEQA
>CharProtDB__CH_122622 prephenate dehydratase (Emericella nidulans)
MAPFKVTFLGPAASFSHQAAVETFGRSSELIPCLSFADAIAAVQRRDADYAIVPFENSTNGSVVQTLDLLVDRNGSYNDVKVCGEYYLTVHHCLLARKGFISAARRNYSSITKIYTHPQAWGQCEIFLAKYFKGVERQDVSSTSKASETVLKTTSEVNAAIASRFAGEYYGLDILEENIEDTANNTTRFLVLRNVYSTTTIQFQPELARELSKSPAVLETKKALFSFMVRQDTLGTLADALLIFKDRGLNLTSINTRPSHIQAWKYVFLVESETDQNQEVPDIMDSLRKVTENCKHLGTWANKLVST
>BRENDA__Q74NC4 prephenate dehydratase (EC 4.2.1.51) (Nanoarchaeum equitans)
MVMILIIGFGRLGQYFYNYLKRKGLNVKVYSRSIKEIEENEFSKFKYAILAIPENSYNEILSKLKENNFNGVIIDLASKKDVVIPIIEQYGFKFLSLHPLFGPSIYEEFSKIVVIKESTDKSFLQFLDFDLIEMSLEEHEKINELQVVTHLLLISYYHFARRFPIKTASAEALYRLSERLLEQNPQILLDIQKEKNAKTYRENYIKFLKEVSNNIEDYIPKERVEGFSRALLLNLSKLWNKDIRKQIMVIDKLILDLIKIRNDLAKQIKEIKELRNLPIEDKKWEIEKRNILLEFAKERELNPLYTDQLIELLISWAKHIENPKPWIGVLGPIGSFSDEVALKLNKTRLNIKYYRKISHIFDALENNEIALGIVPIENVLGGSVNETLDSLIKYNVKIVGEYIHRINLCLVGKNVKEVKRIISHPQAIAQSMEYISKKFPNAEIVYSNSTSEAISMLDEYSLAITSKTAAIFYGLKIYDEHIEDNKENKTRFIIIGKKQLPNPKYSALVFSLEDKPGSLKEVLEIFHKHNINLRKLESRPDKREIGKYLFYVESDLLNNKILEEIRAKANWVKHLGNFREINEIEFPKILD
>biolip__2qmxA The crystal structure of l-phe inhibited prephenate dehydratase from chlorobium tepidum tls
NWLIAYQGEPGAYSEIAALRFGEPLPCESFDDVFSAVTEQKADYAVIPIENSLGGSIHQNYDLLLRRPVVILAETFVKVEHCLLGLPGASVETATKAMSHPQALVQCHNFFATHPQIRAEAAYDTAGSAKMVAESRDKSALAIASKRAGELYGLDILKENLADEEWNITRFFCIAHENNPDISHLKVRPDVARQKTSIVFALPNEQGSLFRALATFALRGIDLTKIESRPSRKKAFEYLFYADFIGHREDQNVHNALENLREFATMVKVLGSYGVVNP
>SwissProt__Q58054 Prephenate dehydratase; PDT; MjPDT; EC 4.2.1.51 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii))
MNKAVIYTLPKGTYSEKATKKFLDYIDGDYKIDYCNSIYDVFERVDNNGLGVVPIENSIEGSVSLTQDLLLQFKDIKILGELALDIHHNLIGYDKNKIKTVISHPQALAQCRNYIKKHGWDVKAVESTAKAVKIVAESKDETLGAIGSKESAEHYNLKILDENIEDYKNNKTRFILIGKKVKFKYHPKNYKVSIVFELKEDKPGALYHILKEFAERNINLTRIESRPSKKRLGTYIFYIDFENNKEKLEEILKSLERHTTFINLLGKYPVFD
>BRENDA__Q8DUV6 prephenate dehydratase (EC 4.2.1.51) (Streptococcus mutans)
MKIAYLGPSGSFTHNVALHAFPAADLLPFENITEVIKAYESKQVCFAIVPVENSIEGSVHETFDYLFHQAKIEAVAEIILPIKQQLMSTSADKTIETIFSHPQAIAQGKQYIRSHYPDVKIEMTASTAYAARFVAEHPEENYAAIAPYAAADEYHLSIIAKDIQEIDENYTRFWVLGDETPTIHLKEEDQKISLALTLPDNLPGALYKALSTFAWRGIDLTKIESRPLKTILGEYFFIIDFENHNEKLVSFALEELTSIGIHYKILGKYAVYRL
>ecocyc__CHORISMUTPREPHENDEHYDRAT-MONOMER fused chorismate mutase/prephenate dehydratase (EC 5.4.99.5; EC 4.2.1.51) (Escherichia coli K-12 substr. MG1655)
MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVVPVDPT
>reanno__Cola_Echvi_0123 prephenate and/or arogenate dehydratase (EC 4.2.1.51) (Echinicola vietnamensis KMM 6221, DSM 17526)
MTSTPHQQKVAIQGIKGSYHYQVALNQFGQDIHVIECLTFSDLVKSITSNDADIGVLALENSIAGAILPNYDLMDRNNLQVIGEFYLPISHQLMVLKGQSIDDITEVRSHPMALLQCKAFFEQYPQIKLIEDLDTASVAKEISEQHLQGVGAIAGKSAAEFYGLDILASDIQTIKNNITRFCIVKNAADAKPVIGFDKASIKVTIKNEQGSLAKVLTTMSAYRLDLTKIQSLPVIDQPWHYAFFIDLLFENLEDYQQALKELKANGHQIKVLGEYKNTK