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Database: UniProt
Entry: A0A1H0CJY0_9ACTN
LinkDB: A0A1H0CJY0_9ACTN
Original site: A0A1H0CJY0_9ACTN 
ID   A0A1H0CJY0_9ACTN        Unreviewed;       311 AA.
AC   A0A1H0CJY0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
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=SAMN05428965_1039 {ECO:0000313|EMBL:SDN58122.1};
OS   Geodermatophilus sp. DSM 45219.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Geodermatophilus.
OX   NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDN58122.1, ECO:0000313|Proteomes:UP000198730};
RN   [1] {ECO:0000313|EMBL:SDN58122.1, ECO:0000313|Proteomes:UP000198730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45219 {ECO:0000313|EMBL:SDN58122.1,
RC   ECO:0000313|Proteomes:UP000198730};
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; FNIQ01000001; SDN58122.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198730; 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:UP000198730};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254}.
FT   DOMAIN        8    186       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      200    277       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        179    179       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   311 AA;  31867 MW;  4651F6E0234030F9 CRC64;
     MTGTPPTRYA YLGPEGTFAE AALISAVGPG EGSRHPAAGV PAALAAVRSG DADAALVPLE
     NSVEGSVPAT MDGLADGAPL LVTREVFLTV SFVLAGRPGT TLSGVRSVAS HPHALAQTAA
     TLAELLPGIV PLPATSTAEA ARQVAAGEHD AAVCAPIAAE RYGLTALAED VADRPGAVTR
     FVLVTAPGPL PARTGNDKTS LVAVVGDRTG ALLDLLREFA VREISLTRIE SRPTRERLGV
     YSFSLDCEGH VADARVGEAL AALHRVCDEL RFLGSYPRAD GRENTPVTPV STDAAFGEAA
     GWLERVRAGA V
//
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