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Database: UniProt
Entry: Q44104
LinkDB: Q44104
Original site: Q44104 
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
//
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