CMPDT_PSEST
ID CMPDT_PSEST Reviewed; 365 AA.
AC P27603; Q9RI01;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000305};
DE AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000305};
DE AltName: Full=P-protein {ECO:0000303|PubMed:1919506};
DE Includes:
DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:1919506};
DE Short=CM {ECO:0000303|PubMed:1919506};
DE EC=5.4.99.5 {ECO:0000269|PubMed:1919506};
DE Includes:
DE RecName: Full=Prephenate dehydratase {ECO:0000303|PubMed:1919506};
DE Short=PDT {ECO:0000303|PubMed:1919506};
DE EC=4.2.1.51 {ECO:0000269|PubMed:1919506};
GN Name=pheA {ECO:0000303|PubMed:1919506};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 10701 / JCM 21571 / JM300;
RX PubMed=1919506; DOI=10.1099/00221287-137-6-1293;
RA Fischer R.S., Zhao G., Jensen R.A.;
RT "Cloning, sequencing, and expression of the P-protein gene (pheA) of
RT Pseudomonas stutzeri in Escherichia coli: implications for evolutionary
RT relationships in phenylalanine biosynthesis.";
RL J. Gen. Microbiol. 137:1293-1301(1991).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=DSM 10701 / JCM 21571 / JM300;
RX PubMed=10368439; DOI=10.1007/pl00006523;
RA Xie G., Bonner C.A., Jensen R.A.;
RT "A probable mixed-function supraoperon in Pseudomonas exhibits gene
RT organization features of both intergenomic conservation and gene
RT shuffling.";
RL J. Mol. Evol. 49:108-121(1999).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate and the decarboxylation/dehydration of prephenate to
CC phenylpyruvate. {ECO:0000269|PubMed:1919506}.
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:0000269|PubMed:1919506};
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:0000269|PubMed:1919506};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
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DR EMBL; AF038578; AAD47360.1; -; Genomic_DNA.
DR PIR; A44764; A44764.
DR AlphaFoldDB; P27603; -.
DR SMR; P27603; -.
DR STRING; 32042.PstZobell_08696; -.
DR eggNOG; COG0077; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
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; IEA:UniProtKB-EC.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis.
FT CHAIN 1..365
FT /note="Bifunctional chorismate mutase/prephenate
FT dehydratase"
FT /id="PRO_0000119190"
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; 40744 MW; 88E2457FDB132FD4 CRC64;
MSEADQLKAL RVRIDSLDER ILDLISERAR CAQEVARVKT ASWPKAEEAV FYRPEREAWV
LKHIMELNKG PLDNEEMARL FREIMSSCLA LEQPLRVAYL GPEGTFSQAA ALKHFGHSVI
SKPMAAIDEV FREVVAGAVN FGVVPVENST EGAVNHTLDS FLEHDIVICG EVELRIHHHL
LVGETTKTDR ITRIYSHAQS LAQCRKWLDA HYPNVERVAV SSNADAAKRV KSEWNSAAIA
GDMAAQLYGL SKLAEKIEDR PVNSTRFLII GSQEVPPTGD DKTSIIVSMR NKPGALHELL
MPFHSNGIDL TRIETRPSRS GKWTYVFFID CMGHHQDPLI KNVLEKIGHE AVALKVLGSY
PKAVL
