UniProtKB - P10378 (ENTE_ECOLI)
Protein
Enterobactin synthase component E
Gene
entE
Organism
Escherichia coli (strain K12)
Status
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
Catalytic activityi
- 3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6 diphosphate + enterobactin + 4 H+7 PublicationsEC:6.3.2.147 Publications
- EC:2.7.7.586 Publications
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
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
- KM=0.4 µM for holo-EntB (at pH 8.8 and 37 degrees Celsius)1 Publication
- KM=0.5 µM for holo-EntB1 Publication
- KM=2.5 µM for DHB (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=2.7 µM for DHB1 Publication
- KM=2.9 µM for DHB1 Publication
- KM=2.9 µM for holo-EntB (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=23.3 µM for holo-EntB (at pH 7.5 and 37 degrees Celsius)1 Publication
- KM=70 µM for 3-hydroxybenzoate (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=70 µM for salicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=400 µM for 5,5-diadenosine tetraphosphate1 Publication
- KM=430 µM for ATP (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=1200 µM for ATP1 Publication
- KM=3100 µM for 4-aminosalicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
- KM=34.2 mM for D-pantetheine (at pH 7.8 and 25 degrees Celsius)1 Publication
- Vmax=3168.2 pmol/min/mg enzyme1 Publication
: enterobactin biosynthesis Pathwayi
This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 235 | Substrate1 Publication | 1 | |
Binding sitei | 240 | Substrate1 Publication | 1 | |
Binding sitei | 309 | Substrate; via amide nitrogen2 Publications | 1 | |
Binding sitei | 331 | Substrate; via carbonyl oxygen2 Publications | 1 | |
Binding sitei | 335 | Substrate; via amide nitrogen1 Publication | 1 | |
Binding sitei | 415 | Substrate2 Publications | 1 | |
Binding sitei | 432 | Substrate1 Publication | 1 | |
Binding sitei | 441 | Substrate1 Publication | 1 |
GO - Molecular functioni
- (2,3-dihydroxybenzoyl)adenylate synthase activity Source: EcoCyc
- 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- transferase activity, transferring acyl groups Source: UniProtKB-KW
GO - Biological processi
- enterobactin biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Acyltransferase, Ligase, Transferase |
Biological process | Enterobactin biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:ENTE-MONOMER MetaCyc:ENTE-MONOMER |
BRENDAi | 6.3.2.14, 2026 |
UniPathwayi | UPA00017 |
Names & Taxonomyi
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) |
Gene namesi | Name:entE1 Publication Ordered Locus Names:b0594, JW0586 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Membrane 1 Publication
GO - Cellular componenti
Keywords - Cellular componenti
MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 437 | R → 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 Publication | 1 | |
Mutagenesisi | 473 | K → 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 Publication | 1 | |
Mutagenesisi | 494 | R → D: Catalyzes the adenylation reaction with same activity as the wild-type. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4856 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000193075 | 1 – 536 | Enterobactin synthase component EAdd BLAST | 536 |
Proteomic databases
jPOSTi | P10378 |
PaxDbi | P10378 |
PRIDEi | P10378 |
Expressioni
Inductioni
Under conditions of iron deficiency and by the fur protein.2 Publications
Interactioni
Subunit structurei
Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Monomer. EntA and EntE interact together.
5 PublicationsBinary interactionsi
P10378
With | #Exp. | IntAct |
---|---|---|
entB [P0ADI4] | 2 | EBI-550322,EBI-547993 |
Protein-protein interaction databases
BioGRIDi | 4259905, 320 interactors 851747, 5 interactors |
ComplexPortali | CPX-5747, entAE 2,3-dihydroxybenzoate-AMP ligase complex CPX-5748, entBE aryl carrier complex |
DIPi | DIP-9515N |
IntActi | P10378, 13 interactors |
STRINGi | 511145.b0594 |
Chemistry databases
BindingDBi | P10378 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P10378 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 438 – 439 | Phosphopantetheine binding2 Publications | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1021, Bacteria |
HOGENOMi | CLU_000022_59_7_6 |
InParanoidi | P10378 |
PhylomeDBi | P10378 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR025110, AMP-bd_C IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, AMP-dep_Synthh-like_sf IPR011963, DHB_AMP_lig |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF13193, AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR02275, DHB_AMP_lig, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
P10378-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 369 – 378 | DAEGNPLPQG → ECRRKSTAAR in CAA33158 (PubMed:2525505).Curated | 10 |
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 |
PIRi | H64792, SYECEB |
RefSeqi | NP_415126.1, NC_000913.3 WP_000026812.1, NZ_SSZK01000032.1 |
Genome annotation databases
EnsemblBacteriai | AAC73695; AAC73695; b0594 BAE76349; BAE76349; BAE76349 |
GeneIDi | 947426 |
KEGGi | ecj:JW0586 eco:b0594 |
PATRICi | fig|1411691.4.peg.1675 |
Similar proteinsi
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 |
PIRi | H64792, SYECEB |
RefSeqi | NP_415126.1, NC_000913.3 WP_000026812.1, NZ_SSZK01000032.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3RG2 | X-ray | 3.10 | A/B/C/D/E/F/G/H/I/J | 1-536 | [»] | |
4IZ6 | X-ray | 2.40 | A/B | 1-536 | [»] | |
6IYK | X-ray | 2.45 | A/B | 1-536 | [»] | |
6IYL | X-ray | 2.56 | A/B | 1-536 | [»] | |
SMRi | P10378 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259905, 320 interactors 851747, 5 interactors |
ComplexPortali | CPX-5747, entAE 2,3-dihydroxybenzoate-AMP ligase complex CPX-5748, entBE aryl carrier complex |
DIPi | DIP-9515N |
IntActi | P10378, 13 interactors |
STRINGi | 511145.b0594 |
Chemistry databases
BindingDBi | P10378 |
ChEMBLi | CHEMBL4856 |
Proteomic databases
jPOSTi | P10378 |
PaxDbi | P10378 |
PRIDEi | P10378 |
Genome annotation databases
EnsemblBacteriai | AAC73695; AAC73695; b0594 BAE76349; BAE76349; BAE76349 |
GeneIDi | 947426 |
KEGGi | ecj:JW0586 eco:b0594 |
PATRICi | fig|1411691.4.peg.1675 |
Organism-specific databases
EchoBASEi | EB0259 |
Phylogenomic databases
eggNOGi | COG1021, Bacteria |
HOGENOMi | CLU_000022_59_7_6 |
InParanoidi | P10378 |
PhylomeDBi | P10378 |
Enzyme and pathway databases
UniPathwayi | UPA00017 |
BioCyci | EcoCyc:ENTE-MONOMER MetaCyc:ENTE-MONOMER |
BRENDAi | 6.3.2.14, 2026 |
Miscellaneous databases
PROi | PR:P10378 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR025110, AMP-bd_C IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, AMP-dep_Synthh-like_sf IPR011963, DHB_AMP_lig |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF13193, AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR02275, DHB_AMP_lig, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ENTE_ECOLI | |
Accessioni | P10378Primary (citable) accession number: P10378 Secondary accession number(s): P15049, P77773, Q2MBK7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | November 1, 1997 | |
Last modified: | December 2, 2020 | |
This is version 173 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families