CMPDT_PSEAE
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 03-AUG-2022, entry version 115.
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 / JCM
OS 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 / 1C /
RC 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., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT 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; EC=4.2.1.51;
CC 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 biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P0A9J8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
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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 AlphaFoldDB; Q9HZ67; -.
DR SMR; Q9HZ67; -.
DR STRING; 287.DR97_4770; -.
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 HOGENOM; CLU_035008_0_1_6; -.
DR InParanoid; Q9HZ67; -.
DR OMA; PLMIYRE; -.
DR PhylomeDB; Q9HZ67; -.
DR BioCyc; PAER208964:G1FZ6-3226-MON; -.
DR SABIO-RK; Q9HZ67; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IPR045865; ACT-like_dom_sf.
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 SUPFAM; SSF55021; SSF55021; 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; Cytoplasm;
KW Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis;
KW Reference proteome.
FT CHAIN 1..365
FT /note="Bifunctional chorismate mutase/prephenate
FT dehydratase"
FT /id="PRO_0000287803"
FT DOMAIN 1..96
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT DOMAIN 97..272
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 284..361
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT SITE 265
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="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
