UniProtKB - P0A8Y8 (ENTH_ECOLI)
Protein
Proofreading thioesterase EntH
Gene
entH
Organism
Escherichia coli (strain K12)
Status
Functioni
Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs.5 Publications
Kineticsi
- KM=16 µM for 2,3-DHB-EntB1 Publication
- KM=116 µM for 2,3-DHB-EntB1 Publication
- KM=21 µM for 4-hydroxybenzoyl-CoA1 Publication
- KM=190 µM for 4-hydroxybenzoyl-CoA1 Publication
- KM=25 µM for 2,4-DHB-EntB1 Publication
- KM=32 µM for lauroyl-EntB1 Publication
- KM=35 µM for 3-hydroxybenzoyl-CoA1 Publication
- KM=265 µM for 3-hydroxybenzoyl-CoA1 Publication
- KM=37 µM for 3-HPA-CoA1 Publication
- KM=45 µM for lauroyl-CoA1 Publication
- KM=49 µM for decanoyl-CoA1 Publication
- KM=55 µM for palmitoyl-CoA1 Publication
- KM=4.25 µM for palmitoyl-CoA1 Publication
- KM=161 µM for 2,3-dihydroxybenzoyl-CoA1 Publication
- KM=176 µM for salicylyl-CoA1 Publication
- KM=212 µM for 3,4-dihydroxybenzoyl-CoA1 Publication
- KM=219 µM for 2,4-dihydroxybenzoyl-CoA1 Publication
- KM=256 µM for 3,5-dihydroxybenzoyl-CoA1 Publication
- KM=272 µM for salicylyl-EntB1 Publication
- KM=350 µM for hexanoyl-CoA1 Publication
- KM=400 µM for propionyl-CoA1 Publication
- KM=475 µM for benzoyl-CoA1 Publication
- KM=800 µM for acetyl-CoA1 Publication
: enterobactin biosynthesis Pathwayi
This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.UniRule annotation1 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 | 48 | Substrate1 Publication | 1 | |
Active sitei | 63 | Nucleophile or proton acceptor1 PublicationUniRule annotation1 Publication | 1 | |
Binding sitei | 82 | Substrate; via carbonyl oxygen1 Publication | 1 |
GO - Molecular functioni
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity Source: GO_Central
- CoA hydrolase activity Source: EcoCyc
- hydrolase activity, acting on ester bonds Source: EcoCyc
- identical protein binding Source: EcoCyc
- thiolester hydrolase activity Source: EcoCyc
GO - Biological processi
- enterobactin biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Hydrolase |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11105-MONOMER MetaCyc:EG11105-MONOMER |
BRENDAi | 3.1.2.2, 2026 |
SABIO-RKi | P0A8Y8 |
UniPathwayi | UPA00017 |
Names & Taxonomyi
Protein namesi | Recommended name: Proofreading thioesterase EntHUniRule annotation (EC:3.1.2.-UniRule annotation)Alternative name(s): Enterobactin synthase component HUniRule annotation p15 |
Gene namesi | Name:entH1 PublicationUniRule annotation Synonyms:ybdB Ordered Locus Names:b0597, JW0589 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 48 | Q → A: Loss of activity. 2 Publications | 1 | |
Mutagenesisi | 48 | Q → N: 290-fold decrease in activity toward salicylyl-CoA. 1 Publication | 1 | |
Mutagenesisi | 54 | H → A: 229-fold decrease in activity toward salicylyl-CoA. Loss of activity toward benzoyl-CoA. 2 Publications | 1 | |
Mutagenesisi | 63 | E → A, D or Q: Loss of activity. 2 Publications | 1 | |
Mutagenesisi | 64 | T → S: 13-fold decrease in activity toward salicylyl-CoA. 1 Publication | 1 | |
Mutagenesisi | 67 | S → A: 140-fold decrease in activity toward salicylyl-CoA. 1 Publication | 1 | |
Mutagenesisi | 67 | S → C: 104-fold decrease in activity toward salicylyl-CoA. 1 Publication | 1 | |
Mutagenesisi | 68 | M → A: 130-fold decrease in activity toward salicylyl-CoA. 1 Publication | 1 | |
Mutagenesisi | 68 | M → V: 47-fold increase in catalytic efficiency toward 1,4-dihydroxy-2-naphthoyl-CoA and 10-fold increase in catalytic efficiency toward lauroyl-CoA. Does not affect catalytic efficiency toward benzoyl-CoA. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000156676 | 1 – 137 | Proofreading thioesterase EntHAdd BLAST | 137 |
Proteomic databases
PaxDbi | P0A8Y8 |
PRIDEi | P0A8Y8 |
Expressioni
Inductioni
Induced by iron starvation.1 Publication
Interactioni
Subunit structurei
Homotetramer. Dimer of dimers.
Interacts specifically with the aryl carrier protein (ArCP) domain of EntB.
UniRule annotation3 PublicationsBinary interactionsi
P0A8Y8
With | #Exp. | IntAct |
---|---|---|
entB [P0ADI4] | 3 | EBI-1118982,EBI-547993 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4260982, 15 interactors |
DIPi | DIP-11343N |
IntActi | P0A8Y8, 2 interactors |
STRINGi | 511145.b0597 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A8Y8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A8Y8 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 54 – 55 | Substrate binding1 Publication | 2 | |
Regioni | 89 – 92 | Substrate binding1 Publication | 4 |
Sequence similaritiesi
Belongs to the thioesterase PaaI family.UniRule annotation
Phylogenomic databases
eggNOGi | COG2050, Bacteria |
HOGENOMi | CLU_089876_13_1_6 |
InParanoidi | P0A8Y8 |
PhylomeDBi | P0A8Y8 |
Family and domain databases
HAMAPi | MF_00907, Thioesterase_EntH, 1 hit |
InterProi | View protein in InterPro IPR029069, HotDog_dom_sf IPR003736, PAAI_dom IPR026576, Thioesterase_EntH IPR006683, Thioestr_dom |
Pfami | View protein in Pfam PF03061, 4HBT, 1 hit |
SUPFAMi | SSF54637, SSF54637, 1 hit |
TIGRFAMsi | TIGR00369, unchar_dom_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A8Y8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF
60 70 80 90 100
GLLHGGASAA LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG
110 120 130
VCQPLHLGRQ NQSWEIVVFD EQGRRCCTCR LGTAVLG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M24148 Unassigned DNA Translation: AAA16104.1 M24143 Genomic DNA Translation: AAA76837.1 U82598 Genomic DNA Translation: AAB40797.1 U00096 Genomic DNA Translation: AAC73698.1 AP009048 Genomic DNA Translation: BAE76352.1 |
PIRi | B91904, Q3ECEA |
RefSeqi | NP_415129.1, NC_000913.3 WP_000637953.1, NZ_STEB01000047.1 |
Genome annotation databases
EnsemblBacteriai | AAC73698; AAC73698; b0597 BAE76352; BAE76352; BAE76352 |
GeneIDi | 58390977 945215 |
KEGGi | ecj:JW0589 eco:b0597 |
PATRICi | fig|1411691.4.peg.1672 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M24148 Unassigned DNA Translation: AAA16104.1 M24143 Genomic DNA Translation: AAA76837.1 U82598 Genomic DNA Translation: AAB40797.1 U00096 Genomic DNA Translation: AAC73698.1 AP009048 Genomic DNA Translation: BAE76352.1 |
PIRi | B91904, Q3ECEA |
RefSeqi | NP_415129.1, NC_000913.3 WP_000637953.1, NZ_STEB01000047.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1VH9 | X-ray | 2.15 | A/B | 2-137 | [»] | |
4K4C | X-ray | 1.85 | A/B/C/D | 1-137 | [»] | |
4K4D | X-ray | 2.17 | A/B | 1-137 | [»] | |
SMRi | P0A8Y8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260982, 15 interactors |
DIPi | DIP-11343N |
IntActi | P0A8Y8, 2 interactors |
STRINGi | 511145.b0597 |
Proteomic databases
PaxDbi | P0A8Y8 |
PRIDEi | P0A8Y8 |
Genome annotation databases
EnsemblBacteriai | AAC73698; AAC73698; b0597 BAE76352; BAE76352; BAE76352 |
GeneIDi | 58390977 945215 |
KEGGi | ecj:JW0589 eco:b0597 |
PATRICi | fig|1411691.4.peg.1672 |
Organism-specific databases
EchoBASEi | EB1097 |
Phylogenomic databases
eggNOGi | COG2050, Bacteria |
HOGENOMi | CLU_089876_13_1_6 |
InParanoidi | P0A8Y8 |
PhylomeDBi | P0A8Y8 |
Enzyme and pathway databases
UniPathwayi | UPA00017 |
BioCyci | EcoCyc:EG11105-MONOMER MetaCyc:EG11105-MONOMER |
BRENDAi | 3.1.2.2, 2026 |
SABIO-RKi | P0A8Y8 |
Miscellaneous databases
EvolutionaryTracei | P0A8Y8 |
PROi | PR:P0A8Y8 |
Family and domain databases
HAMAPi | MF_00907, Thioesterase_EntH, 1 hit |
InterProi | View protein in InterPro IPR029069, HotDog_dom_sf IPR003736, PAAI_dom IPR026576, Thioesterase_EntH IPR006683, Thioestr_dom |
Pfami | View protein in Pfam PF03061, 4HBT, 1 hit |
SUPFAMi | SSF54637, SSF54637, 1 hit |
TIGRFAMsi | TIGR00369, unchar_dom_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ENTH_ECOLI | |
Accessioni | P0A8Y8Primary (citable) accession number: P0A8Y8 Secondary accession number(s): P15050, Q2MBK4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 21, 2005 |
Last sequence update: | June 21, 2005 | |
Last modified: | April 7, 2021 | |
This is version 115 of the entry and version 1 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