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Database: UniProt
Entry: D2NQL5_ROTMD
LinkDB: D2NQL5_ROTMD
Original site: D2NQL5_ROTMD 
ID   D2NQL5_ROTMD            Unreviewed;       315 AA.
AC   D2NQL5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   13-FEB-2019, entry version 52.
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   OrderedLocusNames=RMDY18_01090 {ECO:0000313|EMBL:BAI63941.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI63941.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI63941.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI63941.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H.,
RA   Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent
RT   apical periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI63941.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI63941.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C.,
RA   Leung K.-P., Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical
RT   Isolate with Dense Meshwork-Like Structures from a Persistent Apical
RT   Periodontitis Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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; AP011540; BAI63941.1; -; Genomic_DNA.
DR   RefSeq; WP_012902727.1; NC_013715.1.
DR   STRING; 680646.RMDY18_01090; -.
DR   EnsemblBacteria; BAI63941; BAI63941; RMDY18_01090.
DR   GeneID; 25056264; -.
DR   KEGG; rmu:RMDY18_01090; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; RMUC680646:G1G37-99-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000001883; 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; 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:UP000001883};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT   DOMAIN        2    183       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      198    275       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        176    176       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   315 AA;  33639 MW;  46C8919A8C9BDFCE CRC64;
     MRYTYLGPSG TFTESALLSV PGASDAERIP ATSVPDALAR LNAGEADAAM VPIENSVEGG
     VSATLDAIAA SEGVRIIREV LVPIRFVLVA AKPISIEDVK TISTHSHAWA QVRGWAQENV
     PTAAYLPGSS TAAAAVGLLE EGCTYDAAIC SPALLNYHPE LHVLQDNIGD NKNAVTRFVL
     LSRTADIPEP TGSDKTTLTV PLPANRAGAL LELLEQFAVR GVNLSRIESR PTGEGMGSYS
     FSIDADGHIY EARMRDALRG LHRVSPTLKF LGSYPRADHE NTEVDAIHSD GSFDAAHEWV
     ESLFPNGHPA QLQRH
//
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