Domains within Campylobacter jejuni protein A0A1E7P9U9_CAMJU (A0A1E7P9U9)

Chorismate mutase

Alternative representations: 1 /

Protein length357 aa
Source databaseUniProt
Identifiers A0A0B6TWB9_CAMJU, A0A0B6TWB9, Q0PBJ3_CAMJE, Q0PBJ3, A0A059HY67_CAMJU, A0A059HY67, A0A0E1ZNC3_CAMJU, A0A0E1ZNC3, A0A1E7P9U9_CAMJU, A0A1E7P9U9

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

A0A1E7P9U9_CAMJU is shown as pheA in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for pheA

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 192222.Cj0316 in eggNOG.

OGTaxonomic classDescription
LCOG0077All organisms (root)prephenate dehydratase [EC:4.2.1.51],chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],arogenate/prephenate dehydratase [EC:4.2.1.91 4.2.1.51]
LCOG1605All organisms (root)chorismate mutase [EC:5.4.99.5],chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],isochorismate pyruvate lyase [EC:4.2.99.21]
COG1605Bacteria (superkingdom)chorismate mutase [EC:5.4.99.5],chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],isochorismate pyruvate lyase [EC:4.2.99.21]
COG0077Bacteria (superkingdom)prephenate dehydratase [EC:4.2.1.51],chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],chorismate mutase [EC:5.4.99.5]
61GN7Proteobacteria (phylum)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],3-deoxy-7-phosphoheptulonate synthase [EC:2.5.1.54],chorismate mutase [EC:5.4.99.5]
A27D8delta/epsilon subdivisions (subphylum)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],chorismate mutase [EC:5.4.99.5]
83X3CEpsilonproteobacteria (class)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],chorismate mutase [EC:5.4.99.5]
DX0A8Campylobacterales (order)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51],chorismate mutase [EC:5.4.99.5]
FCBUQCampylobacteraceae (family)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51]
9NHVHCampylobacter (genus)chorismate mutase / prephenate dehydratase [EC:5.4.99.5 4.2.1.51]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: