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Database: UniProt
Entry: P43909
LinkDB: P43909
Original site: P43909 
ID   PHEA_LACLM              Reviewed;         279 AA.
AC   P43909; A2RMG3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   18-SEP-2019, entry version 98.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=llmg_1924;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG1363 / F15876;
RX   PubMed=7823907; DOI=10.1007/bf00290140;
RA   Griffin H.G., Gasson M.J.;
RT   "Genetic aspects of aromatic amino acid biosynthesis in Lactococcus
RT   lactis.";
RL   Mol. Gen. Genet. 246:119-127(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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;
CC         EC=4.2.1.51;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
DR   EMBL; X78413; CAA55182.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98493.1; -; Genomic_DNA.
DR   PIR; S52582; S52582.
DR   RefSeq; WP_011835672.1; NC_009004.1.
DR   SMR; P43909; -.
DR   STRING; 416870.llmg_1924; -.
DR   PRIDE; P43909; -.
DR   EnsemblBacteria; CAL98493; CAL98493; llmg_1924.
DR   KEGG; llm:llmg_1924; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; REVMSAC; -.
DR   BioCyc; LLAC416870:LLMG_RS09630-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000364; Chromosome.
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; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 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   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Phenylalanine biosynthesis.
FT   CHAIN         1    279       Prephenate dehydratase.
FT                                /FTId=PRO_0000119179.
FT   DOMAIN        2    178       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      194    272       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   SITE        171    171       Essential for activity. {ECO:0000250}.
SQ   SEQUENCE   279 AA;  31030 MW;  A11ED51557A0AD73 CRC64;
     MKIAYLGPRG SFCSVVAEAA FKSEELYSYA TILDVIEAYN EGECDFALVP IENSTEGTVN
     MSIDKIFHDS NAKVVAEFVL PISQNLLAVS KEQKIEHIYS HPQALAQTRV YLRKFYPQAQ
     VEITESTSAA AEFVKNNPDL PAAAVANSFA AKMYDLEFIA ENIQDLAGNS TRFWLLGKEK
     QSFDLNQTKD KVTLALTLPD NLPGALHKAI SVFAWRDIDM TKIESRPLRT RLGQYFFIID
     LENNATNSLK IPYALEELAG LGVNVRLLGN YSVYSLGEV
//
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