PHEA_LACLA
ID PHEA_LACLA Reviewed; 279 AA.
AC Q9CEU2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=LL1742; ORFNames=L0055;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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.
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DR EMBL; AE005176; AAK05840.1; -; Genomic_DNA.
DR PIR; F86842; F86842.
DR RefSeq; NP_267898.1; NC_002662.1.
DR RefSeq; WP_010906115.1; NC_002662.1.
DR AlphaFoldDB; Q9CEU2; -.
DR SMR; Q9CEU2; -.
DR STRING; 272623.L0055; -.
DR PaxDb; Q9CEU2; -.
DR EnsemblBacteria; AAK05840; AAK05840; L0055.
DR KEGG; lla:L0055; -.
DR PATRIC; fig|272623.7.peg.1868; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_2_9; -.
DR OMA; PLMIYRE; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000002196; 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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; SSF55021; 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; Lyase;
KW Phenylalanine biosynthesis; Reference proteome.
FT CHAIN 1..279
FT /note="Prephenate dehydratase"
FT /id="PRO_0000119178"
FT DOMAIN 2..178
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 194..270
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 171
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 279 AA; 30966 MW; 0F2A839340C69AFC CRC64;
MKIAYLGPRG SFCSVVAETA FVSEELFAYD SILDVIEAYD EGKCDFALVP IENSTEGTVN
MSIDKIFHDS KATVVAEFVL PISQNLLALS KEGKIEHIYS HPQALAQTRN YLREHYPQAK
VEITDSTSAA AEFVKNHPDL PIAAVANSYA AKMYDLEIVA KNIQDLAGNS TRFWLLGKEK
KSFDLLKTGE KVSLALTLPD NLPGALHKAI SVFAWRDIDM TKIESRPLRT RLGQYFFNID
LVNNEKNNLK IPYALEELSG LGVKVRLLGN YAVYSLGEG