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Protein

Enterobactin synthase component E

Gene

entE

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. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-trihydroxybenzoate. In the second step, DHB is transferred from 2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB) 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. It can also transfer adenylated salicylate to holo-EntB.10 Publications

Miscellaneous

In the absence of holo-EntB, EntE can transfer the adenylate moiety of the 2,3-dihydroxybenzoyl-AMP intermediate to ATP, generating the stress signaling molecule Ap4A involved in the regulation of cell division during oxidative stress, and releasing 2,3-dihydroxybenzoate. It seems that the expression of EntE during iron starvation produces Ap4A to slow growth until intracellular iron stores can be restored.1 Publication

<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 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 the adenylate analogs, 5'-O-[N-(salicyl)sulfamoyl]adenosine (Sal-AMS) and 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl]adenosine (DHB-AMS). Adenylation of 2,3-dihydroxybenzoate (DHB) is enhanced by a protein-protein interaction between the EntA and EntE.2 Publications

<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 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.9 sec(-1) for S-dihydroxybenzoyltransferase activity with D-pantetheine as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with ATP and DHB as substrates (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 4.4 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 4-aminosalicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 5.94 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 100 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 8.8 and 37 degrees Celsius). Kcat is 140 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate.4 Publications
  1. KM=0.4 µM for holo-EntB (at pH 8.8 and 37 degrees Celsius)1 Publication
  2. KM=0.5 µM for holo-EntB1 Publication
  3. KM=2.5 µM for DHB (at pH 7.8 and 25 degrees Celsius)1 Publication
  4. KM=2.7 µM for DHB1 Publication
  5. KM=2.9 µM for DHB1 Publication
  6. KM=2.9 µM for holo-EntB (at pH 7.8 and 25 degrees Celsius)1 Publication
  7. KM=23.3 µM for holo-EntB (at pH 7.5 and 37 degrees Celsius)1 Publication
  8. KM=70 µM for 3-hydroxybenzoate (at pH 7.8 and 25 degrees Celsius)1 Publication
  9. KM=70 µM for salicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
  10. KM=400 µM for 5,5-diadenosine tetraphosphate1 Publication
  11. KM=430 µM for ATP (at pH 7.8 and 25 degrees Celsius)1 Publication
  12. KM=1200 µM for ATP1 Publication
  13. KM=3100 µM for 4-aminosalicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
  14. KM=34.2 mM for D-pantetheine (at pH 7.8 and 25 degrees Celsius)1 Publication
  1. Vmax=3168.2 pmol/min/mg enzyme1 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 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 sitei235Substrate1 Publication1
Binding sitei240Substrate1 Publication1
Binding sitei309Substrate; via amide nitrogen2 Publications1
Binding sitei331Substrate; via carbonyl oxygen2 Publications1
Binding sitei335Substrate; via amide nitrogen1 Publication1
Binding sitei415Substrate2 Publications1
Binding sitei432Substrate1 Publication1
Binding sitei441Substrate1 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

GO - Biological processi

  • enterobactin biosynthetic process Source: EcoCyc

<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 functionAcyltransferase, Ligase, Transferase
Biological processEnterobactin biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.14 2026

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 E1 Publication (EC:6.3.2.147 Publications)
Alternative name(s):
2,3-dihydroxybenzoate-AMP ligase1 Publication
Short name:
DHB-AMP ligase1 Publication
2,3-dihydroxybenzoate-AMP synthaseCurated (EC:2.7.7.586 Publications)
Dihydroxybenzoic acid-activating enzyme1 Publication
Enterochelin synthase E1 Publication
S-dihydroxybenzoyltransferase1 Publication (EC:2.5.1.-6 Publications)
<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:entE1 Publication
Ordered Locus Names:b0594, JW0586
<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
EG10263 entE

<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

Membrane

<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_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>Mutagenesisi437R → D: Catalyzes the adenylation reaction with 10% reduction of activity compared to the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-473. 1 Publication1
Mutagenesisi473K → D: Catalyzes the adenylation reaction with same activity as the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-437. 1 Publication1
Mutagenesisi494R → D: Catalyzes the adenylation reaction with same activity as the wild-type. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4856

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001930751 – 536Enterobactin synthase component EAdd BLAST536

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P10378

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

More...
PaxDbi
P10378

PRoteomics IDEntifications database

More...
PRIDEi
P10378

<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.2 Publications

<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. Monomer. EntA and EntE interact together.5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259905, 320 interactors

Database of interacting proteins

More...
DIPi
DIP-9515N

Protein interaction database and analysis system

More...
IntActi
P10378, 13 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0662

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P10378

<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

1536
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P10378

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

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SMRi
P10378

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

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>Regioni438 – 439Phosphopantetheine binding2 Publications2

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108IQC Bacteria
COG1021 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230011

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P10378

KEGG Orthology (KO)

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KOi
K02363

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10378

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR011963 DHB_AMP_lig

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02275 DHB_AMP_lig, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 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.

P10378-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS
60 70 80 90 100
YRELNQAADN LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP
110 120 130 140 150
VLALFSHQRS ELNAYASQIE PALLIADRQH ALFSGDDFLN TFVTEHSSIR
160 170 180 190 200
VVQLLNDSGE HNLQDAINHP AEDFTATPSP ADEVAYFQLS GGTTGTPKLI
210 220 230 240 250
PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS PGSLGVFLAG
260 270 280 290 300
GTVVLAADPS ATLCFPLIEK HQVNVTALVP PAVSLWLQAL IEGESRAQLA
310 320 330 340 350
SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK
360 370 380 390 400
IIHTQGYPMC PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH
410 420 430 440 450
NASAFDANGF YCSGDLISID PEGYITVQGR EKDQINRGGE KIAAEEIENL
460 470 480 490 500
LLRHPAVIYA ALVSMEDELM GEKSCAYLVV KEPLRAVQVR RFLREQGIAE
510 520 530
FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
Length:536
Mass (Da):59,112
Last modified:November 1, 1997 - v3
<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:iF818942DFDD8DC99
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti369 – 378DAEGNPLPQG → ECRRKSTAAR in CAA33158 (PubMed:2525505).Curated10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X15058 Genomic DNA Translation: CAA33158.1
U82598 Genomic DNA Translation: AAB40794.1
U00096 Genomic DNA Translation: AAC73695.1
AP009048 Genomic DNA Translation: BAE76349.1
M24148 Unassigned DNA Translation: AAA16101.1
M36700 Genomic DNA Translation: AAA18492.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H64792 SYECEB

NCBI Reference Sequences

More...
RefSeqi
NP_415126.1, NC_000913.3
WP_000026812.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73695; AAC73695; b0594
BAE76349; BAE76349; BAE76349

Database of genes from NCBI RefSeq genomes

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GeneIDi
947426

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0586
eco:b0594

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1675

<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
X15058 Genomic DNA Translation: CAA33158.1
U82598 Genomic DNA Translation: AAB40794.1
U00096 Genomic DNA Translation: AAC73695.1
AP009048 Genomic DNA Translation: BAE76349.1
M24148 Unassigned DNA Translation: AAA16101.1
M36700 Genomic DNA Translation: AAA18492.1
PIRiH64792 SYECEB
RefSeqiNP_415126.1, NC_000913.3
WP_000026812.1, NZ_LN832404.1

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
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J1-536[»]
4IZ6X-ray2.40A/B1-536[»]
ProteinModelPortaliP10378
SMRiP10378
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259905, 320 interactors
DIPiDIP-9515N
IntActiP10378, 13 interactors
STRINGi316385.ECDH10B_0662

Chemistry databases

BindingDBiP10378
ChEMBLiCHEMBL4856

Proteomic databases

EPDiP10378
PaxDbiP10378
PRIDEiP10378

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73695; AAC73695; b0594
BAE76349; BAE76349; BAE76349
GeneIDi947426
KEGGiecj:JW0586
eco:b0594
PATRICifig|1411691.4.peg.1675

Organism-specific databases

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

More...
EchoBASEi
EB0259
EcoGeneiEG10263 entE

Phylogenomic databases

eggNOGiENOG4108IQC Bacteria
COG1021 LUCA
HOGENOMiHOG000230011
InParanoidiP10378
KOiK02363
PhylomeDBiP10378

Enzyme and pathway databases

UniPathwayi
UPA00017

BioCyciEcoCyc:ENTE-MONOMER
MetaCyc:ENTE-MONOMER
BRENDAi6.3.2.14 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P10378

Family and domain databases

InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR011963 DHB_AMP_lig
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR02275 DHB_AMP_lig, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiENTE_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: P10378
Secondary accession number(s): P15049, P77773, Q2MBK7
<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: July 1, 1989
Last sequence update: November 1, 1997
Last modified: December 5, 2018
This is version 159 of the entry and version 3 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, 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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