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Database: UniProt
Entry: A0A1I4BNR9_9BACL
LinkDB: A0A1I4BNR9_9BACL
Original site: A0A1I4BNR9_9BACL 
ID   A0A1I4BNR9_9BACL        Unreviewed;       292 AA.
AC   A0A1I4BNR9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 6.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=SAMN03159341_101126 {ECO:0000313|EMBL:SFK69501.1};
OS   Paenibacillus sp. 1_12.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFK69501.1, ECO:0000313|Proteomes:UP000198699};
RN   [1] {ECO:0000313|EMBL:SFK69501.1, ECO:0000313|Proteomes:UP000198699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_12 {ECO:0000313|EMBL:SFK69501.1,
RC   ECO:0000313|Proteomes:UP000198699};
RA   de Groot N.N.;
RL   Submitted (OCT-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;
CC         EC=4.2.1.51; Evidence={ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|RuleBase:RU361254}.
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DR   EMBL; FOTE01000001; SFK69501.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198699; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198699};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198699}.
FT   DOMAIN        3    188       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      204    281       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        181    181       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   292 AA;  32872 MW;  64F436E97F32F10D CRC64;
     MKRIALLGPG TYTEESARHF LDSADCEYVH CKLIDDVFMS TVNGITDYSV IPIENTFDGS
     VSLHLDWLVH EVNLPMQAEW IYPISIQLMA WQAPGETLET SCSSLKKIVS HGVTLTQCRK
     FLRQYLPHVE LEQVSSNGEA ARLVQELGNP EVAALAPRSA GALYGLQIWA QDVQDHQNNF
     TRFVLVGQAP IELKDNYRSH KTTILVTLPE DYPGALHQVL SAFAWRRINL SKIESRPTKK
     KLGNYYFYID IDATLDSVLL PSALQEIEAI GCQVRILGCY PTYSYKPTHS EV
//
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