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Database: UniProt
Entry: PHEA_MYCSK
LinkDB: PHEA_MYCSK
Original site: PHEA_MYCSK 
ID   PHEA_MYCSK              Reviewed;         315 AA.
AC   A1UNA3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=Mkms_5122;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
DR   EMBL; CP000518; ABL94311.1; -; Genomic_DNA.
DR   RefSeq; WP_011562409.1; NC_008705.1.
DR   SMR; A1UNA3; -.
DR   PRIDE; A1UNA3; -.
DR   EnsemblBacteria; ABL94311; ABL94311; Mkms_5122.
DR   GeneID; 32417844; -.
DR   KEGG; mkm:Mkms_5122; -.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000638; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    315       Prephenate dehydratase.
FT                                /FTId=PRO_0000382041.
FT   DOMAIN        3    190       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      204    281       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   SITE        183    183       Essential for activity. {ECO:0000250}.
SQ   SEQUENCE   315 AA;  32736 MW;  95A1B1B47B7B2669 CRC64;
     MPRIAYLGPQ GTFTESALLQ MISGAMVPGG DADDTAVTPV PTDSTPAGLE AVRSGAADYA
     CVPIENSIEG SVLPTLDSLA VGAPLQIFAE LTLAVSFSIV VRPDHDGDVG TVAAFPVAAA
     QVRRWLAEHL PAAQLVPAHS NAAAAADVAG GRADAGISTA LAAERYGLRS LAAGVVDEPN
     ARTRFVLVGR PAPPPARTGA DRTSVALRLP NTPGALVAAM TELSIRDIDL TRIESRPTRT
     ELGTYVFFLD CVGHLEDDAV AEALKALHRR CEDVRYLGSW PTGTAAGAPP PSSDEATRWL
     TRLREGLPTP PEGGR
//
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