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Database: UniProt
Entry: Q745J2
LinkDB: Q745J2
Original site: Q745J2 
ID   PHEA_MYCPA              Reviewed;         315 AA.
AC   Q745J2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MAP_0193;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02510.1; -; Genomic_DNA.
DR   RefSeq; WP_003872300.1; NC_002944.2.
DR   AlphaFoldDB; Q745J2; -.
DR   SMR; Q745J2; -.
DR   STRING; 262316.MAP_0193; -.
DR   EnsemblBacteria; AAS02510; AAS02510; MAP_0193.
DR   KEGG; mpa:MAP_0193; -.
DR   eggNOG; COG0077; Bacteria.
DR   HOGENOM; CLU_035008_0_0_11; -.
DR   OMA; PLMIYRE; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000580; 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; Reference proteome.
FT   CHAIN           1..315
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000382038"
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   315 AA;  32562 MW;  EA769DB9CEFE73F0 CRC64;
     MARIAYLGPE GTFTEAALRQ ITAAGLVPGQ GADGVRPTPV DGTPAALDAV RDGAADYACV
     PIENSIDGSV TPTLDSLAIG SPLQVFAETT LDVAFSIVVK PGLSAADVRT LAAIGVAAAQ
     VRQWVAANLA GAQLRPAYSN ADAAQQVAEG RADAAVTSPL AAARWGLDTL ADGVVDEPNA
     RTRFVLVGPP APPPARTGAD RTSVVLRIDN APGALLAALA EFGIRGIDLT RIESRPTRTG
     LGIYRFFADC VGHIDDEPVA EALKALHRRC ADVRYLGSWP TGTPAGALPP STEEAVRWLA
     AVRDGKPEPP GESRR
//
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