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Protein

Enterobactin synthase component D

Gene

entD

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

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. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.3 Publications

Catalytic activityi

CoA + apo-EntB/F = adenosine 3',5'-bisphosphate + holo-EntB/F.2 Publications

Cofactori

Mg2+By similarity

Kineticsi

Kcat is 5.1 min(-1) for transferase activity with EntB as substrate (at pH 7.5 and 37 degrees Celsius).1 Publication

  1. KM=6.5 µM for EntB (at pH 7.5 and 37 degrees Celsius)1 Publication

    Pathwayi: enterobactin biosynthesis

    This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 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
    Metal bindingi107 – 1071MagnesiumBy similarity
    Metal bindingi109 – 1091MagnesiumBy similarity
    Metal bindingi152 – 1521MagnesiumBy similarity

    GO - Molecular functioni

    • holo-[acyl-carrier-protein] synthase activity Source: EcoCyc
    • magnesium ion binding Source: InterPro

    GO - Biological processi

    • enterobactin biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Enterobactin biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ENTD-MONOMER.
    ECOL316407:JW5085-MONOMER.
    MetaCyc:ENTD-MONOMER.
    UniPathwayiUPA00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enterobactin synthase component D1 Publication
    Alternative name(s):
    4'-phosphopantetheinyl transferase EntD1 Publication (EC:2.7.8.-2 Publications)
    Enterochelin synthase D1 Publication
    Gene namesi
    Name:entD1 Publication
    Ordered Locus Names:b0583, JW5085
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10262. entD.

    Subcellular locationi

    GO - Cellular componenti

    • enterobactin synthetase complex Source: EcoCyc
    • integral component of plasma membrane Source: EcoliWiki
    • intrinsic component of plasma membrane Source: EcoliWiki
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206Enterobactin synthase component DPRO_0000206069Add
    BLAST

    Proteomic databases

    PaxDbiP19925.

    Interactioni

    Subunit structurei

    EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase.1 Publication

    Protein-protein interaction databases

    BioGridi4260709. 77 interactions.
    IntActiP19925. 1 interaction.
    STRINGi511145.b0583.

    Structurei

    3D structure databases

    ProteinModelPortaliP19925.
    SMRiP19925. Positions 45-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4108TSE. Bacteria.
    COG2977. LUCA.
    HOGENOMiHOG000276815.
    InParanoidiP19925.
    KOiK02362.

    Family and domain databases

    Gene3Di3.90.470.20. 1 hit.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR003542. Enbac_synth_compD-like.
    [Graphical view]
    PfamiPF01648. ACPS. 1 hit.
    [Graphical view]
    PRINTSiPR01399. ENTSNTHTASED.
    SUPFAMiSSF56214. SSF56214. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P19925-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTTHTSLPF AGHTLHFVEF DPANFCEQDL LWLPHYAQLQ HAGRKRKTEH
    60 70 80 90 100
    LAGRIAAVYA LREYGYKCVP AIGELRQPVW PAEVYGSISH CGTTALAVVS
    110 120 130 140 150
    RQPIGIDIEE IFSVQTAREL TDNIITPAEH ERLADCGLAF SLALTLAFSA
    160 170 180 190 200
    KESAFKASEI QTDAGFLDYQ IISWNKQQVI IHRENEMFAV HWQIKEKIVI

    TLCQHD
    Length:206
    Mass (Da):23,259
    Last modified:November 16, 2011 - v3
    Checksum:iF2ED3F858A0C5DDF
    GO

    Sequence cautioni

    The sequence AAB40782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA35224.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence CAB57861.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 752EL → DV in CAB57861 (PubMed:2526281).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X17426 Genomic DNA. Translation: CAB57861.1. Different initiation.
    U82598 Genomic DNA. Translation: AAB40782.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73684.2.
    AP009048 Genomic DNA. Translation: BAA35224.2. Different initiation.
    PIRiE64791.
    RefSeqiNP_415115.2. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73684; AAC73684; b0583.
    BAA35224; BAA35224; BAA35224.
    GeneIDi945194.
    KEGGiecj:JW5085.
    eco:b0583.
    PATRICi32116336. VBIEscCol129921_0608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X17426 Genomic DNA. Translation: CAB57861.1. Different initiation.
    U82598 Genomic DNA. Translation: AAB40782.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73684.2.
    AP009048 Genomic DNA. Translation: BAA35224.2. Different initiation.
    PIRiE64791.
    RefSeqiNP_415115.2. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP19925.
    SMRiP19925. Positions 45-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260709. 77 interactions.
    IntActiP19925. 1 interaction.
    STRINGi511145.b0583.

    Proteomic databases

    PaxDbiP19925.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73684; AAC73684; b0583.
    BAA35224; BAA35224; BAA35224.
    GeneIDi945194.
    KEGGiecj:JW5085.
    eco:b0583.
    PATRICi32116336. VBIEscCol129921_0608.

    Organism-specific databases

    EchoBASEiEB0258.
    EcoGeneiEG10262. entD.

    Phylogenomic databases

    eggNOGiENOG4108TSE. Bacteria.
    COG2977. LUCA.
    HOGENOMiHOG000276815.
    InParanoidiP19925.
    KOiK02362.

    Enzyme and pathway databases

    UniPathwayiUPA00017.
    BioCyciEcoCyc:ENTD-MONOMER.
    ECOL316407:JW5085-MONOMER.
    MetaCyc:ENTD-MONOMER.

    Miscellaneous databases

    PROiP19925.

    Family and domain databases

    Gene3Di3.90.470.20. 1 hit.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR003542. Enbac_synth_compD-like.
    [Graphical view]
    PfamiPF01648. ACPS. 1 hit.
    [Graphical view]
    PRINTSiPR01399. ENTSNTHTASED.
    SUPFAMiSSF56214. SSF56214. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The entD gene of the Escherichia coli K12 enterobactin gene cluster."
      Coderre P.E., Earhart C.F.
      J. Gen. Microbiol. 135:3043-3055(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Erratum
      Coderre P.E., Earhart C.F.
      J. Gen. Microbiol. 136:1667-1667(1990)
    3. "The Escherichia coli enterobactin biosynthesis gene, entD: nucleotide sequence and membrane localization of its protein product."
      Armstrong S.K., Pettis G.S., Forrester L.J., McIntosh M.A.
      Mol. Microbiol. 3:757-766(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "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.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "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.
    8. Cited for: FUNCTION.
    9. "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate."
      Gehring A.M., Bradley K.A., Walsh C.T.
      Biochemistry 36:8495-8503(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: BL21-DE3.
    10. "Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF."
      Gehring A.M., Mori I., Walsh C.T.
      Biochemistry 37:2648-2659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiENTD_ECOLI
    AccessioniPrimary (citable) accession number: P19925
    Secondary accession number(s): P77092
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 16, 2011
    Last modified: January 20, 2016
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Deletion of the C-terminal 25 residues of EntB results in very strong decrease of the catalytic efficiency of EntD.1 Publication

    Keywords - Technical termi

    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. 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.