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UniProtKB - Q8K9F8 (CMPDT_BUCAP)
Protein
Bifunctional chorismate mutase/prephenate dehydratase
Gene
pheA
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Functioni
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
By similarityCatalytic activityi
: L-phenylalanine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.By similarity 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.By similarity 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 | SubstrateBy similarity | 1 | |
Binding sitei | 28 | SubstrateBy similarity | 1 | |
Binding sitei | 39 | SubstrateBy similarity | 1 | |
Binding sitei | 48 | SubstrateBy similarity | 1 | |
Binding sitei | 52 | SubstrateBy similarity | 1 | |
Binding sitei | 84 | SubstrateBy similarity | 1 | |
Binding sitei | 88 | SubstrateBy similarity | 1 | |
Sitei | 278 | Essential for prephenate dehydratase activitySequence analysis | 1 |
GO - Molecular functioni
- chorismate mutase activity Source: UniProtKB-EC
- prephenate dehydratase activity Source: UniProtKB-EC
GO - Biological processi
- chorismate metabolic process Source: InterPro
- L-phenylalanine biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Allosteric enzyme, Isomerase, Lyase, Multifunctional enzyme |
Biological process | Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis |
Enzyme and pathway databases
BioCyci | BAPH198804:G1FZU-398-MONOMER |
UniPathwayi | UPA00120;UER00203 UPA00121;UER00345 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional chorismate mutase/prephenate dehydrataseBy similarityAlternative name(s): Chorismate mutase-prephenate dehydrataseBy similarity P-proteinBy similarity Including the following 2 domains: |
Gene namesi | Name:pheA Ordered Locus Names:BUsg_379 |
Organismi | Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) |
Taxonomic identifieri | 198804 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Erwiniaceae › Buchnera › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000119183 | 1 – 385 | Bifunctional chorismate mutase/prephenate dehydrataseAdd BLAST | 385 |
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 – 385 | RegulatoryAdd BLAST | 100 |
Domaini
The regulatory domain shows changes in the ESRP sequence, which is involved in the allosteric binding of phenylalanine. These changes suggest the desensitization of the enzyme to inhibition by phenylalanine and would permit the overproduction of phenylalanine.By similarity
Phylogenomic databases
eggNOGi | COG0077, Bacteria COG1605, Bacteria |
HOGENOMi | CLU_035008_1_0_6 |
OMAi | PLMIYRE |
OrthoDBi | 1280729at2 |
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 PS51171, PREPHENATE_DEHYDR_3, 1 hit |
i Sequence
Sequence statusi: Complete.
Q8K9F8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPSKNDLLSF RSEINNIDKN IVQLLAKRKK LVLNIAESKI KNNQPIRDIE
60 70 80 90 100
REKILLEKLT NLGKKNNLNT NYITRLFQLI IEESVLTQKK LLNKFCNDNN
110 120 130 140 150
LDLASFSFLG PKGSYSHIAA SQYAEQNFKT CIENACLSFN EVIQSVENNQ
160 170 180 190 200
TDYAVLPIEN SCSGFINEIF DILKKTNLFI IGEINISINH CLLAIKKIEL
210 220 230 240 250
NKIKAVYSHP QPFQQCSYFI KKFPNWKIQY TNSTADAMKK IVKYNITTNA
260 270 280 290 300
ALGSELGSKI YGLKVLYKNL ANKKKNITRF ILLSRKPVSI SSKIPTKTTL
310 320 330 340 350
IFNTGQESGA LAEVLLILKK NKLIMKKLTS QNIYKNPWEE MFYIDVQANL
360 370 380
SSSLMQETLE KIGKITKFIK ILGCYPSENI TPIIP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE013218 Genomic DNA Translation: AAM67931.1 |
RefSeqi | WP_011053898.1, NC_004061.1 |
Genome annotation databases
EnsemblBacteriai | AAM67931; AAM67931; BUsg_379 |
KEGGi | bas:BUsg_379 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE013218 Genomic DNA Translation: AAM67931.1 |
RefSeqi | WP_011053898.1, NC_004061.1 |
3D structure databases
SMRi | Q8K9F8 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 198804.BUsg_379 |
Genome annotation databases
EnsemblBacteriai | AAM67931; AAM67931; BUsg_379 |
KEGGi | bas:BUsg_379 |
Phylogenomic databases
eggNOGi | COG0077, Bacteria COG1605, Bacteria |
HOGENOMi | CLU_035008_1_0_6 |
OMAi | PLMIYRE |
OrthoDBi | 1280729at2 |
Enzyme and pathway databases
UniPathwayi | UPA00120;UER00203 UPA00121;UER00345 |
BioCyci | BAPH198804:G1FZU-398-MONOMER |
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 PS51171, PREPHENATE_DEHYDR_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CMPDT_BUCAP | |
Accessioni | Q8K9F8Primary (citable) accession number: Q8K9F8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 15, 2002 |
Last sequence update: | October 1, 2002 | |
Last modified: | February 23, 2022 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |