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Database: UniProt
Entry: A0A1G9M5X3_9ACTN
LinkDB: A0A1G9M5X3_9ACTN
Original site: A0A1G9M5X3_9ACTN 
ID   A0A1G9M5X3_9ACTN        Unreviewed;       305 AA.
AC   A0A1G9M5X3;
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=SAMN05216298_4867 {ECO:0000313|EMBL:SDL69692.1};
OS   Glycomyces sambucus.
OC   Bacteria; Actinobacteria; Glycomycetales; Glycomycetaceae; Glycomyces.
OX   NCBI_TaxID=380244 {ECO:0000313|EMBL:SDL69692.1, ECO:0000313|Proteomes:UP000198662};
RN   [1] {ECO:0000313|EMBL:SDL69692.1, ECO:0000313|Proteomes:UP000198662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDL69692.1,
RC   ECO:0000313|Proteomes:UP000198662};
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; FNGF01000008; SDL69692.1; -; Genomic_DNA.
DR   BioCyc; GCF_900102815:BLS99_RS22855-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198662; 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:UP000198662};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198662}.
FT   DOMAIN        2    178       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      193    270       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        171    171       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   305 AA;  31862 MW;  1E8AFA3EA84B7595 CRC64;
     MEFAYLGPRG TFTEAALRRL PAAKGAAAVP LPSIPEILDA VRRGEVDAGF VPIENSQEGT
     VTLTVDELVG GDPLVIAGEV VLPVTFVLAS AKAPAAIATV ASHPHAIAQV RGFLRRELPN
     AVVHQALSTA QAAQRVADGE FDACVCAPFT AEAAGLPVQA FDIGDSSGAE TRFVHVVRPT
     APPEPSGNDI TSLVVSIDHD RVGALLAVLT ELAIRGINLT RIESRPTGEG LGRYAFFLDC
     TGHLADPRMG EALTGLRRIC ADVRYLGSYP RDHSDRPVPP PAGLGDTDFA DAAAWLDRLR
     GGGAA
//
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