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Entry version 132 (23 Feb 2022)
Sequence version 1 (01 Apr 1988)
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Protein

Bifunctional chorismate mutase/prephenate dehydratase

Gene

pheA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Both activities are inhibited by L-phenylalanine.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.1 Publication
  1. KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius)1 Publication
  2. KM=1.0 mM for prephenate (at pH 7.8 and at 37 degrees Celsius)1 Publication
  3. KM=147 µM for chorismate (at pH 4.9)1 Publication
  4. KM=296 µM for chorismate (at pH 7.5)1 Publication

pH dependencei

Optimum pH is 7.3 for chorismate mutase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.Curated 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.Curated 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei11Substrate1 Publication1
Binding sitei28Substrate1 Publication1
Binding sitei39Substrate1 Publication1
Binding sitei48Substrate1 Publication1
Binding sitei52Substrate1 Publication1
Binding sitei84Substrate1 Publication1
Binding sitei88Substrate1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei278Essential for prephenate dehydratase activitySequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.4.99.5, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A9J8

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00120;UER00203
UPA00121;UER00345

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional chorismate mutase/prephenate dehydrataseCurated
Alternative name(s):
Chorismate mutase-prephenate dehydratase1 Publication
P-protein1 Publication
Including the following 2 domains:
Chorismate mutase1 Publication (EC:5.4.99.51 Publication)
Short name:
CMCurated
Prephenate dehydratase1 Publication (EC:4.2.1.511 Publication)
Short name:
PDTCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pheA1 Publication
Ordered Locus Names:b2599, JW2580
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi11R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication1
Mutagenesisi28R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication1
Mutagenesisi39K → A, Q or R: Important decrease in catalytic efficiency and affinity. 1 Publication1
Mutagenesisi52E → A, D or Q: Important decrease in catalytic efficiency and affinity. 1 Publication1
Mutagenesisi88Q → A, E or K: Important decrease in catalytic efficiency and affinity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3341586

Drug and drug target database

More...
DrugBanki
DB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001191851 – 386Bifunctional chorismate mutase/prephenate dehydrataseAdd BLAST386

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9J8

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A9J8

PRoteomics IDEntifications database

More...
PRIDEi
P0A9J8

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263461, 19 interactors

Database of interacting proteins

More...
DIPi
DIP-36017N

Protein interaction database and analysis system

More...
IntActi
P0A9J8, 17 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2599

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A9J8

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A9J8

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A9J8

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 92Chorismate mutasePROSITE-ProRule annotationAdd BLAST92
Domaini105 – 285Prephenate dehydratasePROSITE-ProRule annotationAdd BLAST181
Domaini299 – 376ACTPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni286 – 386Regulatory (Phe-binding)1 PublicationAdd BLAST101

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0077, Bacteria
COG1605, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_035008_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9J8

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9J8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.59.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01817, CM_2, 1 hit
PF00800, PDT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001500, Chor_mut_pdt_Ppr, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00830, CM_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48600, SSF48600, 1 hit
SSF55021, SSF55021, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01797, CM_P_1, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51671, ACT, 1 hit
PS51168, CHORISMATE_MUT_2, 1 hit
PS00857, PREPHENATE_DEHYDR_1, 1 hit
PS00858, PREPHENATE_DEHYDR_2, 1 hit
PS51171, PREPHENATE_DEHYDR_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A9J8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID
60 70 80 90 100
RERDLLERLI TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN
110 120 130 140 150
PHSARIAFLG PKGSYSHLAA RQYAARHFEQ FIESGCAKFA DIFNQVETGQ
160 170 180 190 200
ADYAVVPIEN TSSGAINDVY DLLQHTSLSI VGEMTLTIDH CLLVSGTTDL
210 220 230 240 250
STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK VAQAKSPHVA
260 270 280 290 300
ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL
310 320 330 340 350
LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL
360 370 380
ESAEMQKALK ELGEITRSMK VLGCYPSENV VPVDPT
Length:386
Mass (Da):43,111
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4B0960854C75A4F1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M10431 Genomic DNA Translation: AAA24330.1
U00096 Genomic DNA Translation: AAC75648.1
AP009048 Genomic DNA Translation: BAA16484.1
M58024 Genomic DNA Translation: AAA62784.1
V00314 Genomic DNA Translation: CAA23601.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A30261, KMECPW

NCBI Reference Sequences

More...
RefSeqi
NP_417090.1, NC_000913.3
WP_000200120.1, NZ_SSUR01000056.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75648; AAC75648; b2599
BAA16484; BAA16484; BAA16484

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58463063
947081

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2580
eco:b2599

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4140

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10431 Genomic DNA Translation: AAA24330.1
U00096 Genomic DNA Translation: AAC75648.1
AP009048 Genomic DNA Translation: BAA16484.1
M58024 Genomic DNA Translation: AAA62784.1
V00314 Genomic DNA Translation: CAA23601.1
PIRiA30261, KMECPW
RefSeqiNP_417090.1, NC_000913.3
WP_000200120.1, NZ_SSUR01000056.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ECMX-ray2.20A/B1-109[»]
5VHTX-ray2.00A/B1-92[»]
SMRiP0A9J8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263461, 19 interactors
DIPiDIP-36017N
IntActiP0A9J8, 17 interactors
STRINGi511145.b2599

Chemistry databases

BindingDBiP0A9J8
ChEMBLiCHEMBL3341586
DrugBankiDB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid

Proteomic databases

jPOSTiP0A9J8
PaxDbiP0A9J8
PRIDEiP0A9J8

Genome annotation databases

EnsemblBacteriaiAAC75648; AAC75648; b2599
BAA16484; BAA16484; BAA16484
GeneIDi58463063
947081
KEGGiecj:JW2580
eco:b2599
PATRICifig|1411691.4.peg.4140

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0701

Phylogenomic databases

eggNOGiCOG0077, Bacteria
COG1605, Bacteria
HOGENOMiCLU_035008_1_0_6
InParanoidiP0A9J8
PhylomeDBiP0A9J8

Enzyme and pathway databases

UniPathwayiUPA00120;UER00203
UPA00121;UER00345
BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER
BRENDAi5.4.99.5, 2026
SABIO-RKiP0A9J8

Miscellaneous databases

EvolutionaryTraceiP0A9J8

Protein Ontology

More...
PROi
PR:P0A9J8

Family and domain databases

Gene3Di1.20.59.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF01817, CM_2, 1 hit
PF00800, PDT, 1 hit
PIRSFiPIRSF001500, Chor_mut_pdt_Ppr, 1 hit
SMARTiView protein in SMART
SM00830, CM_2, 1 hit
SUPFAMiSSF48600, SSF48600, 1 hit
SSF55021, SSF55021, 1 hit
TIGRFAMsiTIGR01797, CM_P_1, 1 hit
PROSITEiView protein in PROSITE
PS51671, ACT, 1 hit
PS51168, CHORISMATE_MUT_2, 1 hit
PS00857, PREPHENATE_DEHYDR_1, 1 hit
PS00858, PREPHENATE_DEHYDR_2, 1 hit
PS51171, PREPHENATE_DEHYDR_3, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCMPDT_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9J8
Secondary accession number(s): P07022, P78204
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: February 23, 2022
This is version 132 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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