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Protein

Proofreading thioesterase EntH

Gene

entH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  1. KM=16 µM for 2,3-DHB-EntB1 Publication
  2. KM=116 µM for 2,3-DHB-EntB1 Publication
  3. KM=21 µM for 4-hydroxybenzoyl-CoA1 Publication
  4. KM=190 µM for 4-hydroxybenzoyl-CoA1 Publication
  5. KM=25 µM for 2,4-DHB-EntB1 Publication
  6. KM=32 µM for lauroyl-EntB1 Publication
  7. KM=35 µM for 3-hydroxybenzoyl-CoA1 Publication
  8. KM=265 µM for 3-hydroxybenzoyl-CoA1 Publication
  9. KM=37 µM for 3-HPA-CoA1 Publication
  10. KM=45 µM for lauroyl-CoA1 Publication
  11. KM=49 µM for decanoyl-CoA1 Publication
  12. KM=55 µM for palmitoyl-CoA1 Publication
  13. KM=4.25 µM for palmitoyl-CoA1 Publication
  14. KM=161 µM for 2,3-dihydroxybenzoyl-CoA1 Publication
  15. KM=176 µM for salicylyl-CoA1 Publication
  16. KM=212 µM for 3,4-dihydroxybenzoyl-CoA1 Publication
  17. KM=219 µM for 2,4-dihydroxybenzoyl-CoA1 Publication
  18. KM=256 µM for 3,5-dihydroxybenzoyl-CoA1 Publication
  19. KM=272 µM for salicylyl-EntB1 Publication
  20. KM=350 µM for hexanoyl-CoA1 Publication
  21. KM=400 µM for propionyl-CoA1 Publication
  22. KM=475 µM for benzoyl-CoA1 Publication
  23. KM=800 µM for acetyl-CoA1 Publication

    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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei48 – 481Substrate1 Publication
    Active sitei63 – 631Nucleophile or proton acceptor1 PublicationUniRule annotation1 Publication
    Binding sitei82 – 821Substrate; via carbonyl oxygen1 Publication

    GO - Molecular functioni

    • 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
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11105-MONOMER.
    ECOL316407:JW0589-MONOMER.
    MetaCyc:EG11105-MONOMER.
    BRENDAi3.1.2.2. 2026.
    UniPathwayiUPA00017.

    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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11105. entH.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481Q → A: Loss of activity. 2 Publications
    Mutagenesisi48 – 481Q → N: 290-fold decrease in activity toward salicylyl-CoA. 1 Publication
    Mutagenesisi54 – 541H → A: 229-fold decrease in activity toward salicylyl-CoA. Loss of activity toward benzoyl-CoA. 2 Publications
    Mutagenesisi63 – 631E → A, D or Q: Loss of activity. 2 Publications
    Mutagenesisi64 – 641T → S: 13-fold decrease in activity toward salicylyl-CoA. 1 Publication
    Mutagenesisi67 – 671S → A: 140-fold decrease in activity toward salicylyl-CoA. 1 Publication
    Mutagenesisi67 – 671S → C: 104-fold decrease in activity toward salicylyl-CoA. 1 Publication
    Mutagenesisi68 – 681M → A: 130-fold decrease in activity toward salicylyl-CoA. 1 Publication
    Mutagenesisi68 – 681M → 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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137Proofreading thioesterase EntHPRO_0000156676Add
    BLAST

    Proteomic databases

    EPDiP0A8Y8.
    PaxDbiP0A8Y8.
    PRIDEiP0A8Y8.

    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

    WithEntry#Exp.IntActNotes
    entBP0ADI43EBI-1118982,EBI-547993

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260982. 15 interactions.
    DIPiDIP-11343N.
    IntActiP0A8Y8. 2 interactions.
    STRINGi511145.b0597.

    Structurei

    Secondary structure

    1
    137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 146Combined sources
    Turni15 – 184Combined sources
    Helixi20 – 234Combined sources
    Beta strandi27 – 315Combined sources
    Beta strandi36 – 416Combined sources
    Turni44 – 463Combined sources
    Beta strandi51 – 533Combined sources
    Helixi55 – 7117Combined sources
    Beta strandi79 – 8911Combined sources
    Beta strandi95 – 10713Combined sources
    Beta strandi109 – 11911Combined sources
    Beta strandi125 – 13612Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VH9X-ray2.15A/B2-137[»]
    4K4CX-ray1.85A/B/C/D1-137[»]
    4K4DX-ray2.17A/B1-137[»]
    ProteinModelPortaliP0A8Y8.
    SMRiP0A8Y8. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 552Substrate binding1 Publication
    Regioni89 – 924Substrate binding1 Publication

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108TZA. Bacteria.
    COG2050. LUCA.
    HOGENOMiHOG000066991.
    InParanoidiP0A8Y8.
    OMAiEVRGICQ.
    OrthoDBiEOG6PGKBS.
    PhylomeDBiP0A8Y8.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    HAMAPiMF_00907. Thioesterase_EntH.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR026576. Thioesterase_EntH.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A8Y8-1 [UniParc]FASTAAdd 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.
    PIRiB91904. Q3ECEA.
    RefSeqiNP_415129.1. NC_000913.3.
    WP_000637953.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73698; AAC73698; b0597.
    BAE76352; BAE76352; BAE76352.
    GeneIDi945215.
    KEGGiecj:JW0589.
    eco:b0597.
    PATRICi32116370. VBIEscCol129921_0625.

    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.
    PIRiB91904. Q3ECEA.
    RefSeqiNP_415129.1. NC_000913.3.
    WP_000637953.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VH9X-ray2.15A/B2-137[»]
    4K4CX-ray1.85A/B/C/D1-137[»]
    4K4DX-ray2.17A/B1-137[»]
    ProteinModelPortaliP0A8Y8.
    SMRiP0A8Y8. Positions 1-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260982. 15 interactions.
    DIPiDIP-11343N.
    IntActiP0A8Y8. 2 interactions.
    STRINGi511145.b0597.

    Proteomic databases

    EPDiP0A8Y8.
    PaxDbiP0A8Y8.
    PRIDEiP0A8Y8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73698; AAC73698; b0597.
    BAE76352; BAE76352; BAE76352.
    GeneIDi945215.
    KEGGiecj:JW0589.
    eco:b0597.
    PATRICi32116370. VBIEscCol129921_0625.

    Organism-specific databases

    EchoBASEiEB1097.
    EcoGeneiEG11105. entH.

    Phylogenomic databases

    eggNOGiENOG4108TZA. Bacteria.
    COG2050. LUCA.
    HOGENOMiHOG000066991.
    InParanoidiP0A8Y8.
    OMAiEVRGICQ.
    OrthoDBiEOG6PGKBS.
    PhylomeDBiP0A8Y8.

    Enzyme and pathway databases

    UniPathwayiUPA00017.
    BioCyciEcoCyc:EG11105-MONOMER.
    ECOL316407:JW0589-MONOMER.
    MetaCyc:EG11105-MONOMER.
    BRENDAi3.1.2.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y8.
    PROiP0A8Y8.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    HAMAPiMF_00907. Thioesterase_EntH.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR026576. Thioesterase_EntH.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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] [Europe PMC] [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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [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.
      Strain: K12.
    10. "Divergence of substrate specificity and function in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB."
      Latham J.A., Chen D., Allen K.N., Dunaway-Mariano D.
      Biochemistry 53:4775-4787(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF MET-68.
    11. "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.
    12. "Structure and catalysis in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB."
      Wu R., Latham J.A., Chen D., Farelli J., Zhao H., Matthews K., Allen K.N., Dunaway-Mariano D.
      Biochemistry 53:4788-4805(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, SUBUNIT, MUTAGENESIS OF GLN-48; HIS-54; GLU-63 AND MET-68, ACTIVE SITE.

    Entry informationi

    Entry nameiENTH_ECOLI
    AccessioniPrimary (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: March 16, 2016
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.