Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8K9F8 (PHEA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-protein

Including the following 2 domains:

  1. Chorismate mutase
    Short name=CM
    EC=5.4.99.5
  2. Prephenate dehydratase
    Short name=PDT
    EC=4.2.1.51
Gene names
Name:pheA
Ordered Locus Names:BUsg_379
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Catalytic activity

Chorismate = prephenate.

Prephenate = phenylpyruvate + H2O + CO2.

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.

Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.

Subcellular location

Cytoplasm.

Domain

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 similarities

Contains 1 ACT domain.

Contains 1 chorismate mutase domain.

Contains 1 prephenate dehydratase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385P-protein
PRO_0000119183

Regions

Domain1 – 9292Chorismate mutase
Domain105 – 285181Prephenate dehydratase
Domain299 – 37678ACT
Region286 – 385100Regulatory

Sites

Site2781Essential for prephenate dehydratase activity Potential

Sequences

Sequence LengthMass (Da)Tools
Q8K9F8 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E8ED3D4C4B05F48F

FASTA38543,888
        10         20         30         40         50         60 
MPSKNDLLSF RSEINNIDKN IVQLLAKRKK LVLNIAESKI KNNQPIRDIE REKILLEKLT 

        70         80         90        100        110        120 
NLGKKNNLNT NYITRLFQLI IEESVLTQKK LLNKFCNDNN LDLASFSFLG PKGSYSHIAA 

       130        140        150        160        170        180 
SQYAEQNFKT CIENACLSFN EVIQSVENNQ TDYAVLPIEN SCSGFINEIF DILKKTNLFI 

       190        200        210        220        230        240 
IGEINISINH CLLAIKKIEL NKIKAVYSHP QPFQQCSYFI KKFPNWKIQY TNSTADAMKK 

       250        260        270        280        290        300 
IVKYNITTNA ALGSELGSKI YGLKVLYKNL ANKKKNITRF ILLSRKPVSI SSKIPTKTTL 

       310        320        330        340        350        360 
IFNTGQESGA LAEVLLILKK NKLIMKKLTS QNIYKNPWEE MFYIDVQANL SSSLMQETLE 

       370        380 
KIGKITKFIK ILGCYPSENI TPIIP 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67931.1.
RefSeqNP_660720.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9F8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67931; AAM67931; BUsg_379.
GeneID1005778.
KEGGbas:BUsg379.
PATRIC21247576. VBIBucAph100086_0393.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0077.
KOK14170.
OMAIDVQANL.
OrthoDBEOG6WHNT1.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-397-MONOMER.
UniPathwayUPA00120; UER00203.
UPA00121; UER00345.

Family and domain databases

Gene3D1.20.59.10. 1 hit.
InterProIPR002912. 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]
PfamPF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMSSF48600. SSF48600. 1 hit.
TIGRFAMsTIGR01797. CM_P_1. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHEA_BUCAP
AccessionPrimary (citable) accession number: Q8K9F8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names