ID   PHEA_MYCS2              Reviewed;         310 AA.
AC   A0R643; I7GFR7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MSMEG_6418, MSMEI_6250;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK72631.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42676.1; -; Genomic_DNA.
DR   RefSeq; WP_003897827.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890631.1; NC_008596.1.
DR   AlphaFoldDB; A0R643; -.
DR   SMR; A0R643; -.
DR   STRING; 246196.MSMEI_6250; -.
DR   PRIDE; A0R643; -.
DR   EnsemblBacteria; ABK72631; ABK72631; MSMEG_6418.
DR   EnsemblBacteria; AFP42676; AFP42676; MSMEI_6250.
DR   GeneID; 66737695; -.
DR   KEGG; msg:MSMEI_6250; -.
DR   KEGG; msm:MSMEG_6418; -.
DR   PATRIC; fig|246196.19.peg.6244; -.
DR   eggNOG; COG0077; Bacteria.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..310
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000382039"
FT   DOMAIN          3..190
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          204..281
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   SITE            183
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  32464 MW;  05E0E37D5F39C0B2 CRC64;
     MPRIAYLGPE GTFTEAALLQ MVAKGMVPGP AEDAGGFTPV RTDSTPGALS AVREGRADYA
     CVPIENSIDG TVLPTLDSLA AGSPLQIYAE LTLDVAFTIV VRPGHDGPVR TVAAFPVAAA
     QVRHWLAANL RDAEVVPAHS NAAAAHDVAE GRADAGVSTR LAAERCGLDI MAADVVDEPN
     ARTRFVLVGL PGTPPPATGA DRTAVVLRLV NEPGALVSAM TEFSIRDIDL TRIESRPTRT
     ELGTYMFFLD CAGHIDDDPV AEALKALHRR CVDVRYLGSW PTESAAGAPP PRLDEATTWL
     EGLRAGSGGA