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Database: UniProt
Entry: A5U9G7
LinkDB: A5U9G7
Original site: A5U9G7 
ID   PHEA_MYCTA              Reviewed;         321 AA.
AC   A5U9G7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MRA_3878;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ75667.1; -; Genomic_DNA.
DR   RefSeq; WP_003420906.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U9G7; -.
DR   SMR; A5U9G7; -.
DR   STRING; 419947.MRA_3878; -.
DR   EnsemblBacteria; ABQ75667; ABQ75667; MRA_3878.
DR   KEGG; mra:MRA_3878; -.
DR   eggNOG; COG0077; Bacteria.
DR   HOGENOM; CLU_035008_0_0_11; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000001988; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Phenylalanine biosynthesis.
FT   CHAIN           1..321
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000382043"
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
//
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