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Database: UniProt
Entry: A0A1E8CZI9_9MICO
LinkDB: A0A1E8CZI9_9MICO
Original site: A0A1E8CZI9_9MICO 
ID   A0A1E8CZI9_9MICO        Unreviewed;       315 AA.
AC   A0A1E8CZI9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   31-JUL-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=BA895_13885 {ECO:0000313|EMBL:OFE17876.1};
OS   Humibacillus sp. DSM 29435.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Humibacillus.
OX   NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE17876.1, ECO:0000313|Proteomes:UP000175826};
RN   [1] {ECO:0000313|Proteomes:UP000175826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OFE17876.1}.
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DR   EMBL; MAST01000004; OFE17876.1; -; Genomic_DNA.
DR   RefSeq; WP_070190654.1; NZ_MAST01000004.1.
DR   EnsemblBacteria; OFE17876; OFE17876; BA895_13885.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000175826; 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; 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:UP000175826};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175826}.
FT   DOMAIN       12    193       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      208    285       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        186    186       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   315 AA;  33098 MW;  2446CABA10A64F20 CRC64;
     MTPPRKPAEL HRFGFLGPRG TFTQMALDAW DGAADREQVP FGSVDGALAA LRSGDIDAAM
     VPIENSVEGG VSATLDALAT GDPLVVIGEV LVPITFVLCA RPGTPIRDIR AVGTHSHAWA
     QVRGWMAANL PDAVYVPTLS TAASASMLAE PGEVMFDAGV CAPVAAADAG LVVLADDIGD
     NQAAVTRFVL VARPGTLPDP TGADKTTVVL FQRTDHSGGL LELLEQFAVR GVNLTRLESR
     PTGSAMGSYC FSIDFEGHVE DARVGETLMG LQRVCAEVRF LGSYPRADGI PSEMRVGTAD
     ADFHDASAWL GRLRS
//
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