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Database: UniProt
Entry: Q9HZ67
LinkDB: Q9HZ67
Original site: Q9HZ67 
ID   CMPDT_PSEAE             Reviewed;         365 AA.
AC   Q9HZ67;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=P-protein {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Chorismate mutase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=CM {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=5.4.99.5 {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=PDT {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=4.2.1.51 {ECO:0000250|UniProtKB:P0A9J8};
GN   Name=pheA; OrderedLocusNames=PA3166;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC         Evidence={ECO:0000250|UniProtKB:P0A9J8};
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:0000250|UniProtKB:P0A9J8};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC       {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
DR   EMBL; AE004091; AAG06554.1; -; Genomic_DNA.
DR   PIR; G83250; G83250.
DR   RefSeq; NP_251856.1; NC_002516.2.
DR   RefSeq; WP_003091446.1; NZ_QZGE01000023.1.
DR   SMR; Q9HZ67; -.
DR   PaxDb; Q9HZ67; -.
DR   PRIDE; Q9HZ67; -.
DR   DNASU; 882699; -.
DR   EnsemblBacteria; AAG06554; AAG06554; PA3166.
DR   GeneID; 882699; -.
DR   KEGG; pae:PA3166; -.
DR   PATRIC; fig|208964.12.peg.3309; -.
DR   PseudoCAP; PA3166; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018971; -.
DR   InParanoid; Q9HZ67; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   PhylomeDB; Q9HZ67; -.
DR   BioCyc; PAER208964:G1FZ6-3226-MONOMER; -.
DR   SABIO-RK; Q9HZ67; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01807; CM_P2; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 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; Cytoplasm; Isomerase; Lyase;
KW   Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    365       Bifunctional chorismate mutase/prephenate
FT                                dehydratase.
FT                                /FTId=PRO_0000287803.
FT   DOMAIN        1     96       Chorismate mutase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00515}.
FT   DOMAIN       97    272       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      284    361       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   BINDING      11     11       Substrate.
FT                                {ECO:0000250|UniProtKB:P0A9J8}.
FT   BINDING      28     28       Substrate.
FT                                {ECO:0000250|UniProtKB:P0A9J8}.
FT   BINDING      39     39       Substrate.
FT                                {ECO:0000250|UniProtKB:P0A9J8}.
FT   BINDING      57     57       Substrate.
FT                                {ECO:0000250|UniProtKB:P0A9J8}.
FT   SITE        265    265       Essential for prephenate dehydratase
FT                                activity. {ECO:0000255}.
SQ   SEQUENCE   365 AA;  40632 MW;  0C9DE686BB1E041D CRC64;
     MADQDQLKAL RLRIDSLDEK LLELISERAR CAQDVARVKT QTLGEGEAPV FYRPEREAWV
     LKHIMQLNKG PLDNEEVARL FREIMSSCLA LEQPLKVAYL GPEGTFTQAA ALKHFGNAVI
     STPMAAIDEV FREVAAGAVN FGVVPVENST EGAVNHTLDS FLEHDMVICG EVELRIHHHL
     LVGETTKTDN ITRIYSHAQS LAQCRKWLDS HYPSVERVAV SSNADAAKRV KSEWNSAAIA
     GDMAASLYDL SKLHEKIEDR PDNSTRFLII GNQEVPPTGD DKTSIIVSMR NKPGALHELL
     VPFHNNGIDL TRIETRPSRS GKWTYVFFID FVGHHKEPLI KDVLEKIGQE AVALKVLGSY
     PKAVL
//
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