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Database: UniProt
Entry: A0A268S7B1_9BACL
LinkDB: A0A268S7B1_9BACL
Original site: A0A268S7B1_9BACL 
ID   A0A268S7B1_9BACL        Unreviewed;       293 AA.
AC   A0A268S7B1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=CHI14_28210 {ECO:0000313|EMBL:PAF28399.1};
OS   Paenibacillus sp. 7516.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF28399.1, ECO:0000313|Proteomes:UP000216732};
RN   [1] {ECO:0000313|EMBL:PAF28399.1, ECO:0000313|Proteomes:UP000216732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7516 {ECO:0000313|EMBL:PAF28399.1,
RC   ECO:0000313|Proteomes:UP000216732};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria
RT   from heroin.";
RL   Submitted (JUL-2017) 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}.
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:PAF28399.1}.
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DR   EMBL; NPBI01000045; PAF28399.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000216732; 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:UP000216732};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216732}.
FT   DOMAIN        2    190       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      206    283       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        183    183       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   293 AA;  32610 MW;  E9AFA51D55CF8E82 CRC64;
     MKRIAVLPEG SVSHEAVEFL FNGEPLELLH SKLISDVFRA TDSGKSQYSV IPIENTIEGS
     VSLHMDWLVN EVDIPMQAEW VYPSIQNVIG HGSEFADGSG AYDFSKITKI MSHPVAIPQC
     HNFIRLHSPE AELEGVNSTA EAVELVKKNP GKGWAAIGTR LAAQKHGLDI MAERVTDHDN
     NYTRFVLIGH EPVQIQREPD HVKTSLLVTL PEDAPGALHQ VLSAFAWRKL NLTRLESRPT
     KKRLGSYYFY IDVEETVESV LLTAAMAEIE ALNCQVRVLG SYPCYTYPSL KTT
//
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