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Database: UniProt
Entry: A0A1H2S5Y0_9BACL
LinkDB: A0A1H2S5Y0_9BACL
Original site: A0A1H2S5Y0_9BACL 
ID   A0A1H2S5Y0_9BACL        Unreviewed;       289 AA.
AC   A0A1H2S5Y0;
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=SAMN05444487_102111 {ECO:0000313|EMBL:SDW26988.1};
OS   Marininema mesophilum.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Marininema.
OX   NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW26988.1, ECO:0000313|Proteomes:UP000198534};
RN   [1] {ECO:0000313|EMBL:SDW26988.1, ECO:0000313|Proteomes:UP000198534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW26988.1,
RC   ECO:0000313|Proteomes:UP000198534};
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; FNNQ01000002; SDW26988.1; -; Genomic_DNA.
DR   BioCyc; GCF_900106775:BLV90_RS02660-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198534; 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; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   PROSITE; PS51671; ACT; 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   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198534};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198534}.
FT   DOMAIN        4    187       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      203    279       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        180    180       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   289 AA;  32597 MW;  968C34A1DE0D098C CRC64;
     MNESVAYLGP RGTFTYEAAR SLFPEEGYQL VPCDSIPDVL TAVDQGEFLY GVVPVENAIE
     GSVTLTLDWL VHHVQVPITG ELVYPIAQHL MIHPNQRELP LTEVKRILSH PQAVAQCSGF
     LREHLPNATI TYVDSTADAA RKVRDHADES WVAIGSSTAH QLYGLEMVAE SIQDYHNNFT
     RFIAVGKSWT HPHSSWEHQK TSILVSLPSD YPGALHQVLQ SFVKEKINLS RIESRPTKKK
     LGTYYFFIDI EEGNHPRMKK AIADVESWGC QVRQMGSYPC YDYRKIKGS
//
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