ID   PHEA_MYCTO              Reviewed;         321 AA.
AC   P9WIC2; L0TFE5; P96240; Q7D4S0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MT3946;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; AE000516; AAK48313.1; -; Genomic_DNA.
DR   PIR; C70653; C70653.
DR   RefSeq; WP_003420906.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIC2; -.
DR   SMR; P9WIC2; -.
DR   EnsemblBacteria; AAK48313; AAK48313; MT3946.
DR   KEGG; mtc:MT3946; -.
DR   PATRIC; fig|83331.31.peg.4244; -.
DR   HOGENOM; CLU_035008_0_0_11; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Amino-acid biosynthesis;
KW   Aromatic amino acid biosynthesis; Lyase; Phenylalanine biosynthesis.
FT   CHAIN           1..321
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000428032"
FT   DOMAIN          3..189
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          203..280
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   SITE            182
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  33633 MW;  A50F13226F788EE5 CRC64;
     MVRIAYLGPE GTFTEAALVR MVAAGLVPET GPDALQRMPV ESAPAALAAV RDGGADYACV
     PIENSIDGSV LPTLDSLAIG VRLQVFAETT LDVTFSIVVK PGRNAADVRT LAAFPVAAAQ
     VRQWLAAHLP AADLRPAYSN ADAARQVADG LVDAAVTSPL AAARWGLAAL ADGVVDESNA
     RTRFVLVGRP GPPPARTGAD RTSAVLRIDN QPGALVAALA EFGIRGIDLT RIESRPTRTE
     LGTYLFFVDC VGHIDDEAVA EALKAVHRRC ADVRYLGSWP TGPAAGAQPP LVDEASRWLA
     RLRAGKPEQT LVRPDDQGAQ A