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Database: UniProt
Entry: A0A1Q5U1Z9_9GAMM
LinkDB: A0A1Q5U1Z9_9GAMM
Original site: A0A1Q5U1Z9_9GAMM 
ID   A0A1Q5U1Z9_9GAMM        Unreviewed;       384 AA.
AC   A0A1Q5U1Z9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:OKP06523.1};
GN   ORFNames=Xentx_02045 {ECO:0000313|EMBL:OKP06523.1};
OS   Xenorhabdus thuongxuanensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP06523.1, ECO:0000313|Proteomes:UP000186277};
RN   [1] {ECO:0000313|EMBL:OKP06523.1, ECO:0000313|Proteomes:UP000186277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30TX1 {ECO:0000313|EMBL:OKP06523.1,
RC   ECO:0000313|Proteomes:UP000186277};
RA   Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT   "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp.
RT   nov., isolated from Steinernema species.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OKP06523.1}.
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DR   EMBL; MKGR01000013; OKP06523.1; -; Genomic_DNA.
DR   RefSeq; WP_074020135.1; NZ_MKGR01000013.1.
DR   Proteomes; UP000186277; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01797; CM_P_1; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 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   Complete proteome {ECO:0000313|Proteomes:UP000186277}.
FT   DOMAIN        1     90       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      103    283       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      297    374       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   BINDING       9      9       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      26     26       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      37     37       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      50     50       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      82     82       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      86     86       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        276    276       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   384 AA;  43203 MW;  640E131CAF1EEEFF CRC64;
     MERDLVSLRE EISHIDAELL DLLAKRRKLA SDIAQTKLHD NRPIRDKNRE RELLGILIDK
     GKSRGLDGFY ITRLFQMIIE DSVLTQQALL QQHLNQTPYD SARITFLGPK GSYSHIAARQ
     FAARHFNQLV ECSCHKFSDI FSLVEIGQAD YGILPLENTS SGAINEVYDL LQHTPLSLVG
     EITLPINHCL LITGQTDISR IKTVYSHSQP FQQCSQYLNK YPDWNIVYCE STAAAMQKVA
     ELNSPEIAAL GSEAGGAFYG LHVLENNLAN QQENSTRFIV VSRKSIDVSE QVPAKTTFIM
     STGQQAGALV DALIILKKHD IPMSKLESRP INGKPWEEMF YIDVQANQRS IKMQQALKEL
     TKITHFLKVL GSYPSENVIP IDPI
//
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