Proofreading thioesterase EntH - Escherichia coli (strain K12)

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P0A8Y8 (ENTH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proofreading thioesterase EntH
EC=3.1.2.-

Alternative name(s):
Enterobactin synthase component H
p15

Gene names

Name:	entH
Synonyms:	ybdB
Ordered Locus Names:	b0597, JW0589

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.7 Ref.8 Ref.9
Pathway	Siderophore biosynthesis; enterobactin biosynthesis. Ref.7
Subunit structure	Homotetramer. Interacts specifically with the aryl carrier protein (ArCP) domain of EntB. Ref.7 Ref.9
Subcellular location	Cytoplasm Ref.7.
Induction	Induced by iron starvation. Ref.7
Sequence similarities	Belongs to the thioesterase PaaI family.
Biophysicochemical properties	Kinetic parameters: K_M=16 µM for 2,3-DHB-EntB Ref.7 Ref.8 Ref.9 K_M=21 µM for 4-HB-CoA K_M=25 µM for 2,4-DHB-EntB K_M=32 µM for lauroyl-EntB K_M=35 µM for 3-HB-CoA K_M=37 µM for 3-HPA-CoA K_M=45 µM for lauroyl-CoA K_M=49 µM for decanoyl-CoA K_M=55 µM for palmitoyl-CoA K_M=161 µM for 2,3-DHB-CoA K_M=176 µM for salicylyl-CoA K_M=212 µM for 3,4-DHB-CoA K_M=219 µM for 2,4-DHB-CoA K_M=256 µM for 3,5-DHB-CoA K_M=272 µM for salicylyl-EntB K_M=350 µM for hexanoyl-CoA K_M=400 µM for propionyl-CoA K_M=475 µM for benzoyl-CoA K_M=800 µM for acetyl-CoA

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 137

137

Proofreading thioesterase EntH HAMAP MF_00907

PRO_0000156676

Sites

Active site

Probable

Experimental info

Mutagenesis

Q → A: Loss of activity. Ref.9

Mutagenesis

Q → N: 290-fold decrease in activity toward salicylyl-CoA. Ref.9

Mutagenesis

H → A: 229-fold decrease in activity toward salicylyl-CoA. Ref.9

Mutagenesis

E → A, D or Q: Loss of activity. Ref.9

Mutagenesis

T → S: 13-fold decrease in activity toward salicylyl-CoA. Ref.9

Mutagenesis

S → A: 140-fold decrease in activity toward salicylyl-CoA. Ref.9

Mutagenesis

S → C: 104-fold decrease in activity toward salicylyl-CoA. Ref.9

Mutagenesis

M → A: 130-fold decrease in activity toward salicylyl-CoA. Ref.9

Secondary structure

137

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A8Y8 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: C8DF8DE63815F206
Show »

FASTA

137

14,970

        10         20         30         40         50         60 
MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA 

        70         80         90        100        110        120 
LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD 

       130 
EQGRRCCTCR LGTAVLG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA." Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A. J. Bacteriol. 171:784-790(1989) [PubMed: 2521621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase." Liu J., Duncan K., Walsh C.T. J. Bacteriol. 171:791-798(1989) [PubMed: 2521622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Enzyme genomics: application of general enzymatic screens to discover new enzymes." Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F. FEMS Microbiol. Rev. 29:263-279(2005) [PubMed: 15808744] [Abstract] Cited for: FUNCTION AS AN ESTERASE.
[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: 17675380] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INTERACTION WITH ENTB, SUBCELLULAR LOCATION, INDUCTION, GENE NAME. Strain: K12.
[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: 19119850] [Abstract] Cited for: FUNCTION AS AN ESTERASE, BIOPHYSICOCHEMICAL PROPERTIES.
[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: 19193103] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68. Strain: K12.
[10]	"Crystal structure of a putative thioesterase." Murshudov G.N., Vagin A.A., Dodson E.J. Submitted (DEC-2003) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-137.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

Q3ECEA. B91904.

RefSeq

NP_415129.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VH9	X-ray	2.15	A/B	2-137	[»]

ProteinModelPortal

P0A8Y8.

SMR

P0A8Y8. Positions 1-137.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A8Y8. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003627; EBESCP00000003627; EBESCG00000002960.
EBESCT00000014793; EBESCP00000014084; EBESCG00000013853.

GeneID

945215.

GenomeReviews

Gene locus JW0589 in contig AP009048_GR.
Gene locus b0597 in contig U00096_GR.

KEGG

ecj:JW0589.
eco:b0597.

PATRIC

32116370. VBIEscCol129921_0625.

Organism-specific databases

EchoBASE

EB1097.

EcoGene

EG11105. entH.

Phylogenomic databases

eggNOG

COG2050.

GeneTree

EBGT00050000011129.

HOGENOM

HBG657960.

OMA

NASHTRS.

PhylomeDB

P0A8Y8.

ProtClustDB

PRK10254.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11105-MONOMER.

BRENDA

3.1.2.2. 2026.

Gene expression databases

Genevestigator

P0A8Y8.

Family and domain databases

HAMAP

MF_00907. Thioesterase_EntH.
[Tree]

InterPro

IPR003736. PAAI.
IPR006683. Thioestr_supf.
[Graphical view]

K01175.

Pfam

PF03061. 4HBT. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00369. Unchar_dom_1. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ENTH_ECOLI

Accession

Primary (citable) accession number: P0A8Y8
Secondary accession number(s): P15050, Q2MBK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents