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Database: UniProt
Entry: A0A1H2CUR9_9ACTN
LinkDB: A0A1H2CUR9_9ACTN
Original site: A0A1H2CUR9_9ACTN 
ID   A0A1H2CUR9_9ACTN        Unreviewed;       312 AA.
AC   A0A1H2CUR9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
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=SAMN04489716_6828 {ECO:0000313|EMBL:SDT73942.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT73942.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT73942.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT73942.1,
RC   ECO:0000313|Proteomes:UP000198688};
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; LT629758; SDT73942.1; -; Genomic_DNA.
DR   BioCyc; GCF_900104725:BLU81_RS33690-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198688; Chromosome i.
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:UP000198688};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198688}.
FT   DOMAIN        7    185       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      200    277       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        178    178       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   312 AA;  32610 MW;  C15D35915D4DA8F8 CRC64;
     MPGTPARFAY LGPEGTFTEA ALRTLPAAEH GVRTPARSVP EALEAVRTGE ADAALVPLEN
     SVGGAVPVTL DELITGSPLM ITREVLLPVE FVLAARTSTP LAGIRSIAAH PQASAQCRHW
     LQANVPDAVV VDVLSNAAAA ISAATGEYDA ALCAPIGVGR NNLTVLAEKV ADRAEAVTRF
     ALLTKPGPPA PPTGDDVTSL AVSIRHDQVG ALLAVLTELA VRGVNLSRIE SRPTGEQLGT
     YVFFLDCTGH VAESRVGEAL RGLRRICAEV RFLGSYPKHR LQPEAPVAAP PGLSDDDFTD
     SAAWLTQLRT GS
//
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