PHEA_AMYME
ID PHEA_AMYME Reviewed; 304 AA.
AC Q44104;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; Synonyms=pdt;
OS Amycolatopsis methanolica.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1814;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7592448; DOI=10.1128/jb.177.22.6666-6669.1995;
RA Vrijbloed J.W., van Hylckama Vlieg J., van der Put N.M., Hessels G.I.,
RA Dijkhuizen L.;
RT "Molecular cloning with a pMEA300-derived shuttle vector and
RT characterization of the Amycolatopsis methanolica prephenate dehydratase
RT gene.";
RL J. Bacteriol. 177:6666-6669(1995).
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; L47666; AAA88840.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44104; -.
DR SMR; Q44104; -.
DR PRIDE; Q44104; -.
DR SABIO-RK; Q44104; -.
DR UniPathway; UPA00121; UER00345.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; 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; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Phenylalanine biosynthesis.
FT CHAIN 1..304
FT /note="Prephenate dehydratase"
FT /id="PRO_0000119175"
FT DOMAIN 3..178
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 193..271
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 171
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 304 AA; 32321 MW; E19052658CC9E52F CRC64;
MSRIAYFGPV GTFTEQAART FMAAGDELVA AETIPKALDA VRRGEADAAC VPVENSVEGA
VPATLDSLAV GEPLIGVAEA LLPVHFSVLT RDDVGEIRTV ASHPHALAQV RKWLEDNLPG
ARVVAAGSTA AAAVAVQAGE FDAAVTAPVA VEHYPLKVLA TEVADVRDAR TRFLLMRRPP
VVLPEPTGAD RTSIVAAAAN RTGTLAELLT ELATRGINLT RLDARPHKQN FGEYRFFIDF
EGHVAEPRIA DALAALRRRC RDVRFLGSFA RADGVAATIE PAARNEDFTD AADWVAAVQR
GEQA