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Database: UniProt
Entry: A0A1Z4JIB4_LEPBY
LinkDB: A0A1Z4JIB4_LEPBY
Original site: A0A1Z4JIB4_LEPBY 
ID   A0A1Z4JIB4_LEPBY        Unreviewed;       281 AA.
AC   A0A1Z4JIB4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
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=NIES2135_33040 {ECO:0000313|EMBL:BAY56470.1};
OS   Leptolyngbya boryana NIES-2135.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY56470.1, ECO:0000313|Proteomes:UP000217895};
RN   [1] {ECO:0000313|EMBL:BAY56470.1, ECO:0000313|Proteomes:UP000217895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY56470.1,
RC   ECO:0000313|Proteomes:UP000217895};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-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; AP018203; BAY56470.1; -; Genomic_DNA.
DR   RefSeq; WP_017288047.1; NZ_AP018203.1.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000217895; 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; 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:UP000217895};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217895}.
FT   DOMAIN        4    187       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      198    273       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        180    180       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   281 AA;  30550 MW;  56AEA8E37C08CC1E CRC64;
     MTISIAHLGP HGTYAETAAL KYLNWFTKSH DQAALLCPYP SITQSLEAVA KEEVQVAVAP
     IENSIEGSVT MTLDALWRLD TLRIQHAIVL PIHHALLSIA SDFSEIQTVY SHPQALAQCQ
     NWLDRNLPSA QVIAANSTTE ALQHLGEDQT IAAISSQRAA QLYSLPVLAS PINDHPENCT
     RFIVVSLDPS PGGSRTSIAF SVSANQPGVL VKPLQIFAEK GINLSRIESR PTKRSLGDYV
     FFVDLEADTR QDAIQSALAE LEHCTETLKI FGSYDVLPAI G
//
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