entH

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

K_M=
16 µM for 2,3-DHB-EntB
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
116 µM for 2,3-DHB-EntB
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
21 µM for 4-hydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
190 µM for 4-hydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
25 µM for 2,4-DHB-EntB
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
32 µM for lauroyl-EntB
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
35 µM for 3-hydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
265 µM for 3-hydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
37 µM for 3-HPA-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
45 µM for lauroyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
49 µM for decanoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
55 µM for palmitoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
4.25 µM for palmitoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
161 µM for 2,3-dihydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
176 µM for salicylyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
212 µM for 3,4-dihydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
219 µM for 2,4-dihydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
256 µM for 3,5-dihydroxybenzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
272 µM for salicylyl-EntB
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
350 µM for hexanoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
400 µM for propionyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
475 µM for benzoyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
K_M=
800 µM for acetyl-CoA
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH."
  Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.
  Biochemistry 48:511-513(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.

Pathwayⁱ: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.UniRule annotation1 Publication
View 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	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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

enterobactin biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- Ref.7
  "The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal enterobactin biosynthesis by interacting with the ArCP domain of EntB."
  Leduc D., Battesti A., Bouveret E.
  J. Bacteriol. 189:7112-7126(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INTERACTION WITH ENTB, SUBCELLULAR LOCATION, INDUCTION, GENE NAME.

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase

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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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 Publications

Binary interactionsⁱ

P0A8Y8

With	#Exp.	IntAct
entB [P0ADI4]	3	EBI-1118982,EBI-547993

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- Ref.9
  "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues."
  Guo Z.F., Sun Y., Zheng S., Guo Z.
  Biochemistry 48:1712-1722(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	4260982, 15 interactors
Database of interacting proteins More...DIPⁱ	DIP-11343N
IntActⁱ	P0A8Y8, 2 interactors
STRINGⁱ	511145.b0597

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	9 – 14	Combined sources	6
Turnⁱ	15 – 18	Combined sources	4
Helixⁱ	20 – 23	Combined sources	4
Beta strandⁱ	27 – 31	Combined sources	5
Beta strandⁱ	36 – 41	Combined sources	6
Turnⁱ	44 – 46	Combined sources	3
Beta strandⁱ	51 – 53	Combined sources	3
Helixⁱ	55 – 71	Combined sources	17
Beta strandⁱ	79 – 89	Combined sources	11
Beta strandⁱ	95 – 107	Combined sources	13
Beta strandⁱ	109 – 119	Combined sources	11
Beta strandⁱ	125 – 136	Combined sources	12

Show more details

3D 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03061, 4HBT, 1 hit
SUPFAMⁱ	SSF54637, SSF54637, 1 hit
TIGRFAMsⁱ	TIGR00369, unchar_dom_1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A8Y8-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:137

Mass (Da):14,970

Last modified:June 21, 2005 - v1

Checksum:ⁱC8DF8DE63815F206

GO

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
NCBI Reference Sequences More...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

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0A8Y8	Proofreading thioesterase EntH		ECOL6		137	UniRef100_P0A8Y9
Proofreading thioesterase EntH		SHIDS		137
Thioesterase		PSEAI		137
Proofreading thioesterase EntH		Escherichia coli D6-113.11		137
Proofreading thioesterase EntH		Enterobacteriaceae bacterium 8376wD9		137
+147

Protein	Similar proteins		Species	Score	Length	Source
P0A8Y8	Proofreading thioesterase EntH		SALTY		137	UniRef90_Q8ZR29
Proofreading thioesterase EntH		CITRI		138
Proofreading thioesterase EntH		SHISS		137
Proofreading thioesterase EntH		SALSV		137
Proofreading thioesterase EntH		ECOLU		137
+951

Protein	Similar proteins		Species	Score	Length	Source
P0A8Y8	Proofreading thioesterase EntH		SALTY		137	UniRef50_Q8ZR29
Proofreading thioesterase EntH		CITRI		138
Proofreading thioesterase EntH		SHISS		137
Proofreading thioesterase EntH		SALEP		137
Proofreading thioesterase EntH		ECOL6		137
+1640

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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

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
Protein Ontology More...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

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UniParc

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Annotation systems

Supporting data

UniProtKB - P0A8Y8 (ENTH_ECOLI)

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Proofreading thioesterase EntH

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<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

<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

<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: enterobactin biosynthesis

Sites

<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

Enzyme and pathway databases

<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 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

Cytoplasm and Cytosol

Cytosol

Keywords - Cellular componenti

<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

<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

Proteomic databases

<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 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

P0A8Y8

GO - Molecular functioni

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Family and domain databases

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: enterobactin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ