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Protein

P-protein

Gene

pheA

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Chorismate = prephenate.
Prephenate = phenylpyruvate + H2O + CO2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei278 – 2781Essential for prephenate dehydratase activitySequence Analysis

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. chorismate mutase activity Source: UniProtKB-EC
  3. prephenate dehydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. chorismate metabolic process Source: InterPro
  2. L-phenylalanine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-397-MONOMER.
UniPathwayiUPA00120; UER00203.
UPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
P-protein
Including the following 2 domains:
Chorismate mutase (EC:5.4.99.5)
Short name:
CM
Prephenate dehydratase (EC:4.2.1.51)
Short name:
PDT
Gene namesi
Name:pheA
Ordered Locus Names:BUsg_379
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385P-proteinPRO_0000119183Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi198804.BUsg379.

Structurei

3D structure databases

ProteinModelPortaliQ8K9F8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292Chorismate mutasePROSITE-ProRule annotationAdd
BLAST
Domaini105 – 285181Prephenate dehydratasePROSITE-ProRule annotationAdd
BLAST
Domaini299 – 37678ACTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 385100RegulatoryAdd
BLAST

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.

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 chorismate mutase domain.PROSITE-ProRule annotation
Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0077.
KOiK14170.
OMAiAGTFSEQ.
OrthoDBiEOG6WHNT1.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR010952. CM_P_1.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01797. CM_P_1. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9F8-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:385
Mass (Da):43,888
Last modified:October 1, 2002 - v1
Checksum:iE8ED3D4C4B05F48F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67931.1.
RefSeqiNP_660720.1. NC_004061.1.
WP_011053898.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67931; AAM67931; BUsg_379.
GeneIDi1005778.
KEGGibas:BUsg379.
PATRICi21247576. VBIBucAph100086_0393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67931.1.
RefSeqiNP_660720.1. NC_004061.1.
WP_011053898.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ8K9F8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67931; AAM67931; BUsg_379.
GeneIDi1005778.
KEGGibas:BUsg379.
PATRICi21247576. VBIBucAph100086_0393.

Phylogenomic databases

eggNOGiCOG0077.
KOiK14170.
OMAiAGTFSEQ.
OrthoDBiEOG6WHNT1.

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.
UPA00121; UER00345.
BioCyciBAPH198804:GHMG-397-MONOMER.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR010952. CM_P_1.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01797. CM_P_1. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiPHEA_BUCAP
AccessioniPrimary (citable) accession number: Q8K9F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: March 4, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Multifunctional enzyme

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.