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Database: UniProt
Entry: A0A1M5F3E0_9BACE
LinkDB: A0A1M5F3E0_9BACE
Original site: A0A1M5F3E0_9BACE 
ID   A0A1M5F3E0_9BACE        Unreviewed;       280 AA.
AC   A0A1M5F3E0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   ORFNames=SAMN05444405_11554 {ECO:0000313|EMBL:SHF85701.1};
OS   Bacteroides luti.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHF85701.1, ECO:0000313|Proteomes:UP000184509};
RN   [1] {ECO:0000313|EMBL:SHF85701.1, ECO:0000313|Proteomes:UP000184509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26991 {ECO:0000313|EMBL:SHF85701.1,
RC   ECO:0000313|Proteomes:UP000184509};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000913};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741}.
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DR   EMBL; FQTV01000015; SHF85701.1; -; Genomic_DNA.
DR   RefSeq; WP_073403178.1; NZ_FQTV01000015.1.
DR   AlphaFoldDB; A0A1M5F3E0; -.
DR   STRING; 1297750.SAMN05444405_11554; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000184509; Unassembled WGS sequence.
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   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184509}.
FT   DOMAIN          3..181
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          198..274
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            174
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   280 AA;  31708 MW;  E59D767A39413E60 CRC64;
     MKKIAIQGTK GSFHDIAAHK LFPDEAILLI CCAHFQDVFD AVKADSQIIG LVAIENTIAG
     SLLQNHELLR KSQLQIIGEY KLRISHCLVC LPDEDWKDIV EVNSHPIALM QCQEFLDSHP
     SFKVVEAEDT AKSAEMIKKK NLRGHAAICS KAAAEIYGMK ILQEGIETNK HNFTRFLVIA
     DPWMADDFRK DKSINKANIV FSLPHTEGSL SQVLSILSFY NINLTKIQSL PIIGREWEYL
     FYVDIAFKDY LRYKQAIDAI TPLIKELRIL GEYEEGKSSI
//
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