SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8K9F8

- PHEA_BUCAP

UniProt

Q8K9F8 - PHEA_BUCAP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
P-protein
Gene
pheA, BUsg_379
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5 - Protein predictedi

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei278 – 2781Essential for prephenate dehydratase activity Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. L-phenylalanine biosynthetic process Source: UniProtKB-UniPathway
  2. chorismate metabolic process Source: InterPro
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-protein
PRO_0000119183Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi198804.BUsg379.

Structurei

3D structure databases

ProteinModelPortaliQ8K9F8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292Chorismate mutase
Add
BLAST
Domaini105 – 285181Prephenate dehydratase
Add
BLAST
Domaini299 – 37678ACT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 385100Regulatory
Add
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.

Phylogenomic databases

eggNOGiCOG0077.
KOiK14170.
OMAiIDVQANL.
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

MPSKNDLLSF RSEINNIDKN IVQLLAKRKK LVLNIAESKI KNNQPIRDIE    50
REKILLEKLT NLGKKNNLNT NYITRLFQLI IEESVLTQKK LLNKFCNDNN 100
LDLASFSFLG PKGSYSHIAA SQYAEQNFKT CIENACLSFN EVIQSVENNQ 150
TDYAVLPIEN SCSGFINEIF DILKKTNLFI IGEINISINH CLLAIKKIEL 200
NKIKAVYSHP QPFQQCSYFI KKFPNWKIQY TNSTADAMKK IVKYNITTNA 250
ALGSELGSKI YGLKVLYKNL ANKKKNITRF ILLSRKPVSI SSKIPTKTTL 300
IFNTGQESGA LAEVLLILKK NKLIMKKLTS QNIYKNPWEE MFYIDVQANL 350
SSSLMQETLE KIGKITKFIK ILGCYPSENI TPIIP 385
Length:385
Mass (Da):43,888
Last modified:October 1, 2002 - v1
Checksum:iE8ED3D4C4B05F48F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67931.1 .
RefSeqi NP_660720.1. NC_004061.1.
WP_011053898.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q8K9F8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 198804.BUsg379.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67931 ; AAM67931 ; BUsg_379 .
GeneIDi 1005778.
KEGGi bas:BUsg379.
PATRICi 21247576. VBIBucAph100086_0393.

Phylogenomic databases

eggNOGi COG0077.
KOi K14170.
OMAi IDVQANL.
OrthoDBi EOG6WHNT1.

Enzyme and pathway databases

UniPathwayi UPA00120 ; UER00203 .
UPA00121 ; UER00345 .
BioCyci BAPH198804:GHMG-397-MONOMER.

Family and domain databases

Gene3Di 1.20.59.10. 1 hit.
InterProi IPR002912. 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 ]
Pfami PF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view ]
PIRSFi PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTi SM00830. CM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF48600. SSF48600. 1 hit.
TIGRFAMsi TIGR01797. CM_P_1. 1 hit.
PROSITEi PS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 85 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