CMPDT_ENTAG
ID CMPDT_ENTAG Reviewed; 387 AA.
AC Q02286;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
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;
OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1512561; DOI=10.1099/00221287-138-7-1309;
RA Xia T., Zhao G., Fischer R.S., Jensen R.A.;
RT "A monofunctional prephenate dehydrogenase created by cleavage of the 5'
RT 109 bp of the tyrA gene from Erwinia herbicola.";
RL J. Gen. Microbiol. 138:1309-1316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301.
RX PubMed=1444388; DOI=10.1128/aem.58.9.2792-2798.1992;
RA Xia T., Zhao G., Jensen R.A.;
RT "Loss of allosteric control but retention of the bifunctional catalytic
RT competence of a fusion protein formed by excision of 260 base pairs from
RT the 3' terminus of pheA from Erwinia herbicola.";
RL Appl. Environ. Microbiol. 58:2792-2798(1992).
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; X60420; CAA42949.1; -; Genomic_DNA.
DR EMBL; M74134; AAA24853.1; -; Genomic_DNA.
DR PIR; S26053; S26053.
DR AlphaFoldDB; Q02286; -.
DR SMR; Q02286; -.
DR STRING; 549.BW31_02109; -.
DR PRIDE; Q02286; -.
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; IPR010952; CM_P_1.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
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; TIGR01797; CM_P_1; 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.
FT CHAIN 1..387
FT /note="Bifunctional chorismate mutase/prephenate
FT dehydratase"
FT /id="PRO_0000119187"
FT DOMAIN 1..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT DOMAIN 105..285
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 299..376
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 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT SITE 278
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000255"
FT CONFLICT 301
FT /note="I -> K (in Ref. 2; AAA24853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43183 MW; 8C4F29C5678E42C6 CRC64;
MNPDNPLLAL RDKISAVDKK LLTLLAERRL LAVEVAQAKL ATHRPIRDVE RERALLENLI
VLGKAHNLDA HYITRLFQLV IEDSVLTQQA LLQKNLNHPH AHAARIAFLG PKGSYSHLAA
RNYASRHFDS MVECGCLKFH DIIKQVENGV ADYAVMPIEN TSSGSINDVY DLLQQTSLSI
VGELTLPIDH CVLVNGPTDL QQIETVYSHP QPFQQCSQFI NRFPHWKIEY TESTAAAMEK
VAALNSPKVA ALGSEAGGEL YQLQVLERNL ANQQQNHTRF IVLARKAIEV SDQVPAKTTL
IMATGQQAGA LVDALLVLRQ HNLIMSKLES RPINGNPWEE MFYIDVQGNL QSERMQQALQ
ELQTMTRSLK VLGCYPSENV VPAEPGR
