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Protein

Enterobactin synthase component B

Gene

entB

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

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron2+ atoms. EntB is a bifunctional protein that serves as an isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-dihydroxybenzoate (DHB). In the enterobactin assembly, EntB functions as an aryl carrier protein phosphopantetheinylated near the C terminus by EntD to yield holo-EntB, which is then acylated by EntE with 2,3-dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine.8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the ‘Function’ 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

Inhibited by 3-[(carboxyethenyl)oxy]-6-hydroxy-1-benzoic acid and 3-[(carboxyethenyl)oxy]benzoic acid.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 600 min(-1) for isochorismatase activity with isochorismate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 540 min(-1) for isochorismatase activity with 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 310 min(-1) for isochorismatase activity with 4,5-dihydroisochorismate as substrate (at pH 7 and 37 degrees Celsius).1 Publication
  1. KM=14.7 µM for isochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  2. KM=23 µM for 4,5-dihydroisochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  3. KM=86 µM for 3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  4. KM=120 µM for 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate (at pH 7 and 37 degrees Celsius)1 Publication
  5. KM=280 µM for cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  1. Vmax=18.5 µmol/min/mg enzyme (at pH 7 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 6.5 and 7.5. At pH 5.5, EntB retains 50% of isochorismatase activity.1 Publication

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

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi227Magnesium1 Publication1
Metal bindingi242Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi244Magnesium1 Publication1

<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

  • 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • isochorismatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphopantetheine binding Source: UniProtKB
  • transferase activity, transferring alkyl or aryl (other than methyl) groups Source: EcoliWiki

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 functionHydrolase, Ligase, Multifunctional enzyme
Biological processEnterobactin biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ENTB-MONOMER
MetaCyc:ENTB-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.3.2.1 2026
6.3.2.14 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0ADI4

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

More...
UniPathwayi
UPA00017

<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_and_taxonomy_section">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:
Enterobactin synthase component B1 Publication (EC:6.3.2.144 Publications)
Alternative name(s):
Enterobactin biosynthesis bifunctional protein EntB1 Publication
Enterochelin synthase B1 Publication
Including the following 2 domains:
Isochorismatase1 Publication (EC:3.3.2.14 Publications)
Alternative name(s):
2,3-dihydro-2,3-dihydroxybenzoate synthase1 Publication
Isochorismate lyase1 Publication
Aryl carrier protein1 Publication
Short name:
ArCP1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:entB1 Publication
Synonyms:entG1 Publication
Ordered Locus Names:b0595, JW0587
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10260 entB

<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

GO - Cellular componenti

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are hypersensitive to the antimicrobial peptide wrwycr.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi240D → R: The catalytic efficiency slightly increases, but a 8-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication1
Mutagenesisi242G → A: Not efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi244D → A: Efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi244D → R: Not efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi249M → A: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication1
Mutagenesisi263D → R: The catalytic efficiency is the same as the wild-type, but a 3-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication1
Mutagenesisi264F → E: The affinity for EntE and catalytic efficiency of the S-dihydroxybenzoyltransferase EntE are below that of the wild-type. 2 Publications1
Mutagenesisi268A → Q: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication1
Mutagenesisi269K → A: Behaves similarly to the wild-type. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002018222 – 285Enterobactin synthase component BAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei245O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-dihydroxybenzoate in a reaction catalyzed by EntE.1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0ADI4

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

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PaxDbi
P0ADI4

PRoteomics IDEntifications database

More...
PRIDEi
P0ADI4

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P0ADI4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Under conditions of iron deficiency and by the fur protein.1 Publication

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Dimer.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4260905, 201 interactors

Database of interacting proteins

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DIPi
DIP-9512N

Protein interaction database and analysis system

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IntActi
P0ADI4, 29 interactors

STRING: functional protein association networks

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STRINGi
316385.ECDH10B_0663

<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

1285
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0ADI4

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

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SMRi
P0ADI4

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P0ADI4

<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_and_domains_section">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>Domaini209 – 284CarrierPROSITE-ProRule annotationAdd BLAST76

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>Regioni2 – 213Isochorismatase1 PublicationAdd BLAST212

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the isochorismatase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105WQI Bacteria
COG1535 LUCA
COG3433 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000078667

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0ADI4

KEGG Orthology (KO)

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KOi
K01252

Database for complete collections of gene phylogenies

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PhylomeDBi
P0ADI4

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1200.10, 1 hit
3.40.50.850, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036736 ACP-like_sf
IPR016291 Isochorismatase
IPR000868 Isochorismatase-like
IPR036380 Isochorismatase-like_sf
IPR009081 PP-bd_ACP

The PANTHER Classification System

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PANTHERi
PTHR43540:SF3 PTHR43540:SF3, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00857 Isochorismatase, 1 hit
PF00550 PP-binding, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001111 Isochorismatase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01398 ISCHRISMTASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47336 SSF47336, 1 hit
SSF52499 SSF52499, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50075 CARRIER, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADI4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC
60 70 80 90 100
PMMEQVIANI AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT
110 120 130 140 150
RSPEQQKVVD RLTPDADDTV LVKWRYSAFH RSPLEQMLKE SGRNQLIITG
160 170 180 190 200
VYAHIGCMTT ATDAFMRDIK PFMVADALAD FSRDEHLMSL KYVAGRSGRV
210 220 230 240 250
VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID YGLDSVRMMA
260 270 280
LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
Length:285
Mass (Da):32,554
Last modified:December 6, 2005 - 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:iE98C62D5ED23BAB1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M24148 Unassigned DNA Translation: AAA16102.1
M24143 Genomic DNA Translation: AAA76835.1
U82598 Genomic DNA Translation: AAB40795.1
U00096 Genomic DNA Translation: AAC73696.1
AP009048 Genomic DNA Translation: BAE76350.1

Protein sequence database of the Protein Information Resource

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PIRi
C91904 YXECIC

NCBI Reference Sequences

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RefSeqi
NP_415127.1, NC_000913.3
WP_001007138.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC73696; AAC73696; b0595
BAE76350; BAE76350; BAE76350

Database of genes from NCBI RefSeq genomes

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GeneIDi
946178

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW0587
eco:b0595

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.1674

<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
M24148 Unassigned DNA Translation: AAA16102.1
M24143 Genomic DNA Translation: AAA76835.1
U82598 Genomic DNA Translation: AAB40795.1
U00096 Genomic DNA Translation: AAC73696.1
AP009048 Genomic DNA Translation: BAE76350.1
PIRiC91904 YXECIC
RefSeqiNP_415127.1, NC_000913.3
WP_001007138.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FQ1X-ray2.30A/B1-285[»]
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J209-285[»]
4IZ6X-ray2.40A/B211-285[»]
ProteinModelPortaliP0ADI4
SMRiP0ADI4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260905, 201 interactors
DIPiDIP-9512N
IntActiP0ADI4, 29 interactors
STRINGi316385.ECDH10B_0663

2D gel databases

SWISS-2DPAGEiP0ADI4

Proteomic databases

EPDiP0ADI4
PaxDbiP0ADI4
PRIDEiP0ADI4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73696; AAC73696; b0595
BAE76350; BAE76350; BAE76350
GeneIDi946178
KEGGiecj:JW0587
eco:b0595
PATRICifig|1411691.4.peg.1674

Organism-specific databases

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

More...
EchoBASEi
EB0256
EcoGeneiEG10260 entB

Phylogenomic databases

eggNOGiENOG4105WQI Bacteria
COG1535 LUCA
COG3433 LUCA
HOGENOMiHOG000078667
InParanoidiP0ADI4
KOiK01252
PhylomeDBiP0ADI4

Enzyme and pathway databases

UniPathwayi
UPA00017

BioCyciEcoCyc:ENTB-MONOMER
MetaCyc:ENTB-MONOMER
BRENDAi3.3.2.1 2026
6.3.2.14 2026
SABIO-RKiP0ADI4

Miscellaneous databases

EvolutionaryTraceiP0ADI4

Protein Ontology

More...
PROi
PR:P0ADI4

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.40.50.850, 1 hit
InterProiView protein in InterPro
IPR036736 ACP-like_sf
IPR016291 Isochorismatase
IPR000868 Isochorismatase-like
IPR036380 Isochorismatase-like_sf
IPR009081 PP-bd_ACP
PANTHERiPTHR43540:SF3 PTHR43540:SF3, 1 hit
PfamiView protein in Pfam
PF00857 Isochorismatase, 1 hit
PF00550 PP-binding, 1 hit
PIRSFiPIRSF001111 Isochorismatase, 1 hit
PRINTSiPR01398 ISCHRISMTASE
SUPFAMiSSF47336 SSF47336, 1 hit
SSF52499 SSF52499, 1 hit
PROSITEiView protein in PROSITE
PS50075 CARRIER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiENTB_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: P0ADI4
Secondary accession number(s): P15048, Q2MBK6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: December 5, 2018
This is version 112 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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