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Protein

Isochorismate synthase EntC

Gene

entC

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 (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate.6 Publications

Catalytic activityi

Chorismate = isochorismate.3 Publications

Cofactori

Mg2+1 Publication

Kineticsi

Kcat is 290 min(-1) for mutase activity with chorismate. Kcat is 173 min(-1) for mutase activity with chorismate (at pH 7.8 and 37 degrees Celsius). Kcat is 108 min(-1) for mutase activity with isochorismate (at pH 7.8 and 37 degrees Celsius). Kcat is 37 min(-1) for mutase activity with chorismate.3 Publications

  1. KM=5 µM for isochorismate (at pH 7.8 and 37 degrees Celsius)1 Publication
  2. KM=7 µM for chorismate1 Publication
  3. KM=14 µM for chorismate (at pH 7.8 and 37 degrees Celsius)1 Publication
  4. KM=41 µM for chorismate1 Publication

    Pathwayi: enterobactin biosynthesis

    This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.Curated
    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 bindingi140 – 1401Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi142 – 1421Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi145 – 1451Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi146 – 1461Magnesium1 Publication
    Active sitei147 – 1471Proton acceptor1 Publication
    Active sitei197 – 1971Proton donor1 Publication
    Metal bindingi241 – 2411Magnesium1 Publication
    Binding sitei241 – 2411Substrate1 Publication
    Binding sitei303 – 3031Substrate; via carbonyl oxygen1 Publication
    Binding sitei347 – 3471Substrate1 Publication
    Binding sitei361 – 3611Substrate; via amide nitrogen1 Publication
    Metal bindingi376 – 3761Magnesium1 Publication

    GO - Molecular functioni

    • isochorismate synthase activity Source: EcoCyc
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Enterobactin biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ENTC-MONOMER.
    ECOL316407:JW0585-MONOMER.
    MetaCyc:ENTC-MONOMER.
    BRENDAi5.4.4.2. 2026.
    SABIO-RKP0AEJ2.
    UniPathwayiUPA00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isochorismate synthase EntC1 Publication (EC:5.4.4.23 Publications)
    Alternative name(s):
    Isochorismate mutaseCurated
    Gene namesi
    Name:entC1 Publication
    Ordered Locus Names:b0593, JW0585
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10261. entC.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to produce enterobactin and are hypersensitive to the antimicrobial peptide wrwycr.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi303 – 3031A → T: Loss of mutase activity. 1 Publication
    Mutagenesisi304 – 3041L → A: Loss of mutase activity. 1 Publication
    Mutagenesisi327 – 3271F → Y: Loss of mutase activity. 1 Publication
    Mutagenesisi346 – 3461I → L: Loss of mutase activity. 1 Publication
    Mutagenesisi359 – 3591F → Q: Loss of mutase activity. 1 Publication

    Chemistry

    ChEMBLiCHEMBL1075176.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Isochorismate synthase EntCPRO_0000154144Add
    BLAST

    Proteomic databases

    PaxDbiP0AEJ2.
    PRIDEiP0AEJ2.

    Expressioni

    Inductioni

    Under conditions of iron deficiency and by the fur protein.2 Publications

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi4260986. 156 interactions.
    DIPiDIP-47970N.
    IntActiP0AEJ2. 9 interactions.
    MINTiMINT-1300552.
    STRINGi511145.b0593.

    Chemistry

    BindingDBiP0AEJ2.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243Combined sources
    Beta strandi30 – 345Combined sources
    Beta strandi36 – 394Combined sources
    Helixi52 – 6615Combined sources
    Beta strandi73 – 786Combined sources
    Beta strandi87 – 904Combined sources
    Beta strandi92 – 965Combined sources
    Helixi99 – 10810Combined sources
    Beta strandi117 – 1248Combined sources
    Helixi126 – 14116Combined sources
    Beta strandi142 – 1443Combined sources
    Beta strandi146 – 16015Combined sources
    Helixi164 – 17411Combined sources
    Beta strandi176 – 1849Combined sources
    Beta strandi186 – 1883Combined sources
    Beta strandi190 – 1956Combined sources
    Beta strandi198 – 2036Combined sources
    Beta strandi206 – 2105Combined sources
    Beta strandi212 – 2176Combined sources
    Turni222 – 2276Combined sources
    Helixi228 – 2347Combined sources
    Helixi236 – 25318Combined sources
    Turni254 – 2563Combined sources
    Beta strandi257 – 2615Combined sources
    Beta strandi267 – 2704Combined sources
    Beta strandi272 – 2787Combined sources
    Beta strandi281 – 2855Combined sources
    Helixi291 – 2988Combined sources
    Turni302 – 3043Combined sources
    Beta strandi305 – 3084Combined sources
    Helixi309 – 31911Combined sources
    Turni325 – 3284Combined sources
    Beta strandi329 – 3357Combined sources
    Beta strandi340 – 3445Combined sources
    Beta strandi347 – 3526Combined sources
    Beta strandi355 – 36410Combined sources
    Helixi370 – 38819Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HWOX-ray2.30A/B1-391[»]
    ProteinModelPortaliP0AEJ2.
    SMRiP0AEJ2. Positions 13-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEJ2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni214 – 2152Substrate1 Publication

    Sequence similaritiesi

    Belongs to the isochorismate synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105E4F. Bacteria.
    COG1169. LUCA.
    HOGENOMiHOG000028185.
    InParanoidiP0AEJ2.
    KOiK02361.
    OMAiMWHLSSR.
    OrthoDBiEOG6PGK1Z.
    PhylomeDBiP0AEJ2.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR015890. Chorismate_C.
    IPR004561. IsoChor_synthase.
    [Graphical view]
    PfamiPF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00543. isochor_syn. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AEJ2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDTSLAEEVQ QTMATLAPNR FFFMSPYRSF TTSGCFARFD EPAVNGDSPD
    60 70 80 90 100
    SPFQQKLAAL FADAKAQGIK NPVMVGAIPF DPRQPSSLYI PESWQSFSRQ
    110 120 130 140 150
    EKQASARRFT RSQSLNVVER QAIPEQTTFE QMVARAAALT ATPQVDKVVL
    160 170 180 190 200
    SRLIDITTDA AIDSGVLLER LIAQNPVSYN FHVPLADGGV LLGASPELLL
    210 220 230 240 250
    RKDGERFSSI PLAGSARRQP DEVLDREAGN RLLASEKDRH EHELVTQAMK
    260 270 280 290 300
    EVLRERSSEL HVPSSPQLIT TPTLWHLATP FEGKANSQEN ALTLACLLHP
    310 320 330 340 350
    TPALSGFPHQ AATQVIAELE PFDRELFGGI VGWCDSEGNG EWVVTIRCAK
    360 370 380 390
    LRENQVRLFA GAGIVPASSP LGEWRETGVK LSTMLNVFGL H
    Length:391
    Mass (Da):42,932
    Last modified:December 20, 2005 - v1
    Checksum:i62882569DFC41AC4
    GO

    Sequence cautioni

    The sequence AAB40793.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3062SG → TA in AAA18491 (PubMed:2110093).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M36700 Genomic DNA. Translation: AAA18491.1.
    M24142 Unassigned DNA. Translation: AAA16100.1.
    U82598 Genomic DNA. Translation: AAB40793.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73694.1.
    AP009048 Genomic DNA. Translation: BAE76348.1.
    X53274 Genomic DNA. Translation: CAA37371.1.
    PIRiJT0497. SYECIK.
    RefSeqiNP_415125.1. NC_000913.3.
    WP_000381303.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73694; AAC73694; b0593.
    BAE76348; BAE76348; BAE76348.
    GeneIDi945511.
    KEGGiecj:JW0585.
    eco:b0593.
    PATRICi32116362. VBIEscCol129921_0621.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M36700 Genomic DNA. Translation: AAA18491.1.
    M24142 Unassigned DNA. Translation: AAA16100.1.
    U82598 Genomic DNA. Translation: AAB40793.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73694.1.
    AP009048 Genomic DNA. Translation: BAE76348.1.
    X53274 Genomic DNA. Translation: CAA37371.1.
    PIRiJT0497. SYECIK.
    RefSeqiNP_415125.1. NC_000913.3.
    WP_000381303.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HWOX-ray2.30A/B1-391[»]
    ProteinModelPortaliP0AEJ2.
    SMRiP0AEJ2. Positions 13-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260986. 156 interactions.
    DIPiDIP-47970N.
    IntActiP0AEJ2. 9 interactions.
    MINTiMINT-1300552.
    STRINGi511145.b0593.

    Chemistry

    BindingDBiP0AEJ2.
    ChEMBLiCHEMBL1075176.

    Proteomic databases

    PaxDbiP0AEJ2.
    PRIDEiP0AEJ2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73694; AAC73694; b0593.
    BAE76348; BAE76348; BAE76348.
    GeneIDi945511.
    KEGGiecj:JW0585.
    eco:b0593.
    PATRICi32116362. VBIEscCol129921_0621.

    Organism-specific databases

    EchoBASEiEB0257.
    EcoGeneiEG10261. entC.

    Phylogenomic databases

    eggNOGiENOG4105E4F. Bacteria.
    COG1169. LUCA.
    HOGENOMiHOG000028185.
    InParanoidiP0AEJ2.
    KOiK02361.
    OMAiMWHLSSR.
    OrthoDBiEOG6PGK1Z.
    PhylomeDBiP0AEJ2.

    Enzyme and pathway databases

    UniPathwayiUPA00017.
    BioCyciEcoCyc:ENTC-MONOMER.
    ECOL316407:JW0585-MONOMER.
    MetaCyc:ENTC-MONOMER.
    BRENDAi5.4.4.2. 2026.
    SABIO-RKP0AEJ2.

    Miscellaneous databases

    EvolutionaryTraceiP0AEJ2.
    PROiP0AEJ2.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR015890. Chorismate_C.
    IPR004561. IsoChor_synthase.
    [Graphical view]
    PfamiPF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00543. isochor_syn. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Opacity factor from group A streptococci is an apoproteinase."
      Elkins M.F., Earhart C.F.
      FEMS Microbiol. Lett. 56:35-39(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC and evolutionary relationship of isochorismate synthetase and other chorismate-utilizing enzymes."
      Ozenberger B.A., Brickman T.J., McIntosh M.A.
      J. Bacteriol. 171:775-783(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: K12.
    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. "Regulation of divergent transcription from the iron-responsive fepB-entC promoter-operator regions in Escherichia coli."
      Brickman T.J., Ozenberger B.A., McIntosh M.A.
      J. Mol. Biol. 212:669-682(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    7. "Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate."
      Liu J., Quinn N., Berchtold G.A., Walsh C.T.
      Biochemistry 29:1417-1425(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    8. "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: INDUCTION.
    9. "Anaerobic biosynthesis of enterobactin Escherichia coli: regulation of entC gene expression and evidence against its involvement in menaquinone (vitamin K2) biosynthesis."
      Kwon O., Hudspeth M.E., Meganathan R.
      J. Bacteriol. 178:3252-3259(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    10. "The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli."
      Dahm C., Muller R., Schulte G., Schmidt K., Leistner E.
      Biochim. Biophys. Acta 1425:377-386(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    11. "Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase."
      Jiang M., Guo Z.
      J. Am. Chem. Soc. 129:730-731(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution."
      Orchard S.S., Rostron J.E., Segall A.M.
      Microbiology 158:547-559(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Crystal structure of Escherichia coli enterobactin-specific isochorismate synthase (EntC) bound to its reaction product isochorismate: implications for the enzyme mechanism and differential activity of chorismate-utilizing enzymes."
      Sridharan S., Howard N., Kerbarh O., Blaszczyk M., Abell C., Blundell T.L.
      J. Mol. Biol. 397:290-300(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-303; PHE-327; ILE-346 AND PHE-359, COFACTOR, SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiENTC_ECOLI
    AccessioniPrimary (citable) accession number: P0AEJ2
    Secondary accession number(s): P10377, P77099, Q2MBK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: January 20, 2016
    This is version 86 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, Direct protein sequencing, 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.