ID   PHEA_METJA              Reviewed;         272 AA.
AC   Q58054;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
DE   AltName: Full=MjPDT;
GN   Name=pheA; OrderedLocusNames=MJ0637;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   BIOPHYSICAL CHARACTERIZATION, SUBUNIT, MASS SPECTROMETRY, AND INHIBITION.
RX   PubMed=17115705; DOI=10.1021/bi061274n;
RA   Kleeb A.C., Kast P., Hilvert D.;
RT   "A monofunctional and thermostable prephenate dehydratase from the archaeon
RT   Methanocaldococcus jannaschii.";
RL   Biochemistry 45:14101-14110(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC   -!- ACTIVITY REGULATION: Inhibited by L-phenylalanine but not by L-tyrosine
CC       or L-tryptophan.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22 uM for prephenate;
CC       pH dependence:
CC         Optimum pH is 5-10.;
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17115705}.
CC   -!- MASS SPECTROMETRY: Mass=31413; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17115705};
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DR   EMBL; L77117; AAB98631.1; -; Genomic_DNA.
DR   PIR; E64379; E64379.
DR   RefSeq; WP_010870142.1; NC_000909.1.
DR   AlphaFoldDB; Q58054; -.
DR   SMR; Q58054; -.
DR   STRING; 243232.MJ_0637; -.
DR   PRIDE; Q58054; -.
DR   EnsemblBacteria; AAB98631; AAB98631; MJ_0637.
DR   GeneID; 1451503; -.
DR   KEGG; mja:MJ_0637; -.
DR   eggNOG; arCOG00255; Archaea.
DR   HOGENOM; CLU_035008_0_2_2; -.
DR   InParanoid; Q58054; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 47176at2157; -.
DR   PhylomeDB; Q58054; -.
DR   SABIO-RK; Q58054; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Phenylalanine biosynthesis; Reference proteome.
FT   CHAIN           1..272
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000119180"
FT   DOMAIN          4..179
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          194..269
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   SITE            172
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  31415 MW;  0A5FDCE74AB7C3AD CRC64;
     MNKAVIYTLP KGTYSEKATK KFLDYIDGDY KIDYCNSIYD VFERVDNNGL GVVPIENSIE
     GSVSLTQDLL LQFKDIKILG ELALDIHHNL IGYDKNKIKT VISHPQALAQ CRNYIKKHGW
     DVKAVESTAK AVKIVAESKD ETLGAIGSKE SAEHYNLKIL DENIEDYKNN KTRFILIGKK
     VKFKYHPKNY KVSIVFELKE DKPGALYHIL KEFAERNINL TRIESRPSKK RLGTYIFYID
     FENNKEKLEE ILKSLERHTT FINLLGKYPV FD