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Database: UniProt
Entry: A0A221VWE2_9PSEU
LinkDB: A0A221VWE2_9PSEU
Original site: A0A221VWE2_9PSEU 
ID   A0A221VWE2_9PSEU        Unreviewed;       333 AA.
AC   A0A221VWE2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-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   ECO:0000313|EMBL:ASO17787.1};
GN   ORFNames=AHOG_00570 {ECO:0000313|EMBL:ASO17787.1};
OS   Actinoalloteichus hoggarensis.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinoalloteichus.
OX   NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO17787.1, ECO:0000313|Proteomes:UP000204221};
RN   [1] {ECO:0000313|EMBL:ASO17787.1, ECO:0000313|Proteomes:UP000204221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO17787.1,
RC   ECO:0000313|Proteomes:UP000204221};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943,
RT   type strain of Actinoalloteichus hoggarensis.";
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}.
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DR   EMBL; CP022521; ASO17787.1; -; Genomic_DNA.
DR   KEGG; ahg:AHOG_00570; -.
DR   KO; K04518; -.
DR   BioCyc; GCF_002234535:AHOG_RS00550-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000204221; Chromosome.
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:UP000204221};
KW   Lyase {ECO:0000256|RuleBase:RU361254, ECO:0000313|EMBL:ASO17787.1};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT   DOMAIN        3    202       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      216    294       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        195    195       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   333 AA;  35027 MW;  105D303F8965A4D0 CRC64;
     MRRILYLGPE GTFTEQAART LVSRVYPDAT VGAAQAVLSV AAGPDADLVL APAVTVRAAM
     VEVSAGRAEA VVAPVENSVE GSVPATLDAL VDADPVVAVA ETVLPVRFSV LAAPGTTPER
     VRTVATHPHA AAQVREWLAR ELPDAVVVSA TSTAAAAVEV LAGRADAAVT APLAAERYAL
     DVLASDVADV RDAVTSFRLL RSPGRVPEPT GVDRTSLVVT VDDRIGTLAD LLTELATRGV
     NLTRIESRPT RDRLGRYRFF LDLDGHVAER RVADAMAALR RRSQEVRFLG SFPRARIAGR
     AVAAEISPPD AYSDAAFAEA AAWVQSLQEG SRA
//
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