We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - P0A9J8 (CMPDT_ECOLI)
Protein
Bifunctional chorismate mutase/prephenate dehydratase
Gene
pheA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
1 PublicationCatalytic activityi
Activity regulationi
Both activities are inhibited by L-phenylalanine.1 Publication
Kineticsi
kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.1 Publication
- KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius)1 Publication
- KM=1.0 mM for prephenate (at pH 7.8 and at 37 degrees Celsius)1 Publication
- KM=147 µM for chorismate (at pH 4.9)1 Publication
- KM=296 µM for chorismate (at pH 7.5)1 Publication
pH dependencei
Optimum pH is 7.3 for chorismate mutase activity.1 Publication
: L-phenylalanine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.Curated This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylpyruvate from prephenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.
Pathwayi: prephenate biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.Curated This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 11 | Substrate1 Publication | 1 | |
Binding sitei | 28 | Substrate1 Publication | 1 | |
Binding sitei | 39 | Substrate1 Publication | 1 | |
Binding sitei | 48 | Substrate1 Publication | 1 | |
Binding sitei | 52 | Substrate1 Publication | 1 | |
Binding sitei | 84 | Substrate1 Publication | 1 | |
Binding sitei | 88 | Substrate1 Publication | 1 | |
Sitei | 278 | Essential for prephenate dehydratase activitySequence analysis | 1 |
GO - Molecular functioni
- chorismate mutase activity Source: EcoCyc
- prephenate dehydratase activity Source: EcoCyc
GO - Biological processi
- chorismate metabolic process Source: InterPro
- L-phenylalanine biosynthetic process Source: EcoCyc
- tyrosine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Isomerase, Lyase, Multifunctional enzyme |
Biological process | Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER |
BRENDAi | 5.4.99.5, 2026 |
SABIO-RKi | P0A9J8 |
UniPathwayi | UPA00120;UER00203 UPA00121;UER00345 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional chorismate mutase/prephenate dehydrataseCuratedAlternative name(s): Chorismate mutase-prephenate dehydratase1 Publication P-protein1 Publication Including the following 2 domains: |
Gene namesi | Name:pheA1 Publication Ordered Locus Names:b2599, JW2580 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm Curated
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 11 | R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication | 1 | |
Mutagenesisi | 28 | R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication | 1 | |
Mutagenesisi | 39 | K → A, Q or R: Important decrease in catalytic efficiency and affinity. 1 Publication | 1 | |
Mutagenesisi | 52 | E → A, D or Q: Important decrease in catalytic efficiency and affinity. 1 Publication | 1 | |
Mutagenesisi | 88 | Q → A, E or K: Important decrease in catalytic efficiency and affinity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3341586 |
DrugBanki | DB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000119185 | 1 – 386 | Bifunctional chorismate mutase/prephenate dehydrataseAdd BLAST | 386 |
Proteomic databases
jPOSTi | P0A9J8 |
PaxDbi | P0A9J8 |
PRIDEi | P0A9J8 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4263461, 19 interactors |
DIPi | DIP-36017N |
IntActi | P0A9J8, 17 interactors |
STRINGi | 511145.b2599 |
Chemistry databases
BindingDBi | P0A9J8 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A9J8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A9J8 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 92 | Chorismate mutasePROSITE-ProRule annotationAdd BLAST | 92 | |
Domaini | 105 – 285 | Prephenate dehydratasePROSITE-ProRule annotationAdd BLAST | 181 | |
Domaini | 299 – 376 | ACTPROSITE-ProRule annotationAdd BLAST | 78 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 286 – 386 | Regulatory (Phe-binding)1 PublicationAdd BLAST | 101 |
Phylogenomic databases
eggNOGi | COG0077, Bacteria COG1605, Bacteria |
HOGENOMi | CLU_035008_1_0_6 |
InParanoidi | P0A9J8 |
PhylomeDBi | P0A9J8 |
Family and domain databases
Gene3Di | 1.20.59.10, 1 hit |
InterProi | View protein in InterPro IPR045865, ACT-like_dom_sf IPR002912, ACT_dom IPR008242, Chor_mutase/pphenate_deHydtase IPR036263, Chorismate_II_sf IPR036979, CM_dom_sf IPR002701, CM_II_prokaryot IPR010952, CM_P_1 IPR001086, Preph_deHydtase IPR018528, Preph_deHydtase_CS |
Pfami | View protein in Pfam PF01817, CM_2, 1 hit PF00800, PDT, 1 hit |
PIRSFi | PIRSF001500, Chor_mut_pdt_Ppr, 1 hit |
SMARTi | View protein in SMART SM00830, CM_2, 1 hit |
SUPFAMi | SSF48600, SSF48600, 1 hit SSF55021, SSF55021, 1 hit |
TIGRFAMsi | TIGR01797, CM_P_1, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS51168, CHORISMATE_MUT_2, 1 hit PS00857, PREPHENATE_DEHYDR_1, 1 hit PS00858, PREPHENATE_DEHYDR_2, 1 hit PS51171, PREPHENATE_DEHYDR_3, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A9J8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID
60 70 80 90 100
RERDLLERLI TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN
110 120 130 140 150
PHSARIAFLG PKGSYSHLAA RQYAARHFEQ FIESGCAKFA DIFNQVETGQ
160 170 180 190 200
ADYAVVPIEN TSSGAINDVY DLLQHTSLSI VGEMTLTIDH CLLVSGTTDL
210 220 230 240 250
STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK VAQAKSPHVA
260 270 280 290 300
ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL
310 320 330 340 350
LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL
360 370 380
ESAEMQKALK ELGEITRSMK VLGCYPSENV VPVDPT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M10431 Genomic DNA Translation: AAA24330.1 U00096 Genomic DNA Translation: AAC75648.1 AP009048 Genomic DNA Translation: BAA16484.1 M58024 Genomic DNA Translation: AAA62784.1 V00314 Genomic DNA Translation: CAA23601.1 |
PIRi | A30261, KMECPW |
RefSeqi | NP_417090.1, NC_000913.3 WP_000200120.1, NZ_SSUR01000056.1 |
Genome annotation databases
EnsemblBacteriai | AAC75648; AAC75648; b2599 BAA16484; BAA16484; BAA16484 |
GeneIDi | 58463063 947081 |
KEGGi | ecj:JW2580 eco:b2599 |
PATRICi | fig|1411691.4.peg.4140 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M10431 Genomic DNA Translation: AAA24330.1 U00096 Genomic DNA Translation: AAC75648.1 AP009048 Genomic DNA Translation: BAA16484.1 M58024 Genomic DNA Translation: AAA62784.1 V00314 Genomic DNA Translation: CAA23601.1 |
PIRi | A30261, KMECPW |
RefSeqi | NP_417090.1, NC_000913.3 WP_000200120.1, NZ_SSUR01000056.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ECM | X-ray | 2.20 | A/B | 1-109 | [»] | |
5VHT | X-ray | 2.00 | A/B | 1-92 | [»] | |
SMRi | P0A9J8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263461, 19 interactors |
DIPi | DIP-36017N |
IntActi | P0A9J8, 17 interactors |
STRINGi | 511145.b2599 |
Chemistry databases
BindingDBi | P0A9J8 |
ChEMBLi | CHEMBL3341586 |
DrugBanki | DB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid |
Proteomic databases
jPOSTi | P0A9J8 |
PaxDbi | P0A9J8 |
PRIDEi | P0A9J8 |
Genome annotation databases
EnsemblBacteriai | AAC75648; AAC75648; b2599 BAA16484; BAA16484; BAA16484 |
GeneIDi | 58463063 947081 |
KEGGi | ecj:JW2580 eco:b2599 |
PATRICi | fig|1411691.4.peg.4140 |
Organism-specific databases
EchoBASEi | EB0701 |
Phylogenomic databases
eggNOGi | COG0077, Bacteria COG1605, Bacteria |
HOGENOMi | CLU_035008_1_0_6 |
InParanoidi | P0A9J8 |
PhylomeDBi | P0A9J8 |
Enzyme and pathway databases
UniPathwayi | UPA00120;UER00203 UPA00121;UER00345 |
BioCyci | EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER |
BRENDAi | 5.4.99.5, 2026 |
SABIO-RKi | P0A9J8 |
Miscellaneous databases
EvolutionaryTracei | P0A9J8 |
PROi | PR:P0A9J8 |
Family and domain databases
Gene3Di | 1.20.59.10, 1 hit |
InterProi | View protein in InterPro IPR045865, ACT-like_dom_sf IPR002912, ACT_dom IPR008242, Chor_mutase/pphenate_deHydtase IPR036263, Chorismate_II_sf IPR036979, CM_dom_sf IPR002701, CM_II_prokaryot IPR010952, CM_P_1 IPR001086, Preph_deHydtase IPR018528, Preph_deHydtase_CS |
Pfami | View protein in Pfam PF01817, CM_2, 1 hit PF00800, PDT, 1 hit |
PIRSFi | PIRSF001500, Chor_mut_pdt_Ppr, 1 hit |
SMARTi | View protein in SMART SM00830, CM_2, 1 hit |
SUPFAMi | SSF48600, SSF48600, 1 hit SSF55021, SSF55021, 1 hit |
TIGRFAMsi | TIGR01797, CM_P_1, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS51168, CHORISMATE_MUT_2, 1 hit PS00857, PREPHENATE_DEHYDR_1, 1 hit PS00858, PREPHENATE_DEHYDR_2, 1 hit PS51171, PREPHENATE_DEHYDR_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CMPDT_ECOLI | |
Accessioni | P0A9J8Primary (citable) accession number: P0A9J8 Secondary accession number(s): P07022, P78204 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | April 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references