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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Metal bindingi140Magnesium; via carbonyl oxygen1 Publication1
    Metal bindingi142Magnesium; via carbonyl oxygen1 Publication1
    Metal bindingi145Magnesium; via carbonyl oxygen1 Publication1
    Metal bindingi146Magnesium1 Publication1
    Active sitei147Proton acceptor1 Publication1
    Active sitei197Proton donor1 Publication1
    Metal bindingi241Magnesium1 Publication1
    Binding sitei241Substrate1 Publication1
    Binding sitei303Substrate; via carbonyl oxygen1 Publication1
    Binding sitei347Substrate1 Publication1
    Binding sitei361Substrate; via amide nitrogen1 Publication1
    Metal bindingi376Magnesium1 Publication1

    GO - Molecular functioni

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

    GO - Biological processi

    • enterobactin biosynthetic process Source: EcoCyc
    • salicylic acid biosynthetic process Source: GO_Central
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10261. entC.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi303A → T: Loss of mutase activity. 1 Publication1
    Mutagenesisi304L → A: Loss of mutase activity. 1 Publication1
    Mutagenesisi327F → Y: Loss of mutase activity. 1 Publication1
    Mutagenesisi346I → L: Loss of mutase activity. 1 Publication1
    Mutagenesisi359F → Q: Loss of mutase activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL1075176.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001541441 – 391Isochorismate synthase EntCAdd BLAST391

    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 interactors.
    DIPiDIP-47970N.
    IntActiP0AEJ2. 9 interactors.
    MINTiMINT-1300552.
    STRINGi511145.b0593.

    Chemistry databases

    BindingDBiP0AEJ2.

    Structurei

    Secondary structure

    1391
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi22 – 24Combined sources3
    Beta strandi30 – 34Combined sources5
    Beta strandi36 – 39Combined sources4
    Turni44 – 47Combined sources4
    Helixi52 – 66Combined sources15
    Beta strandi73 – 78Combined sources6
    Beta strandi87 – 90Combined sources4
    Beta strandi92 – 96Combined sources5
    Helixi99 – 108Combined sources10
    Beta strandi117 – 124Combined sources8
    Helixi126 – 141Combined sources16
    Beta strandi142 – 144Combined sources3
    Beta strandi146 – 160Combined sources15
    Helixi164 – 174Combined sources11
    Beta strandi176 – 184Combined sources9
    Beta strandi186 – 188Combined sources3
    Beta strandi190 – 195Combined sources6
    Beta strandi198 – 203Combined sources6
    Beta strandi206 – 210Combined sources5
    Beta strandi212 – 217Combined sources6
    Turni222 – 227Combined sources6
    Helixi228 – 234Combined sources7
    Helixi236 – 253Combined sources18
    Turni254 – 256Combined sources3
    Beta strandi257 – 261Combined sources5
    Beta strandi267 – 270Combined sources4
    Beta strandi272 – 278Combined sources7
    Beta strandi281 – 285Combined sources5
    Helixi291 – 298Combined sources8
    Turni302 – 304Combined sources3
    Beta strandi305 – 308Combined sources4
    Helixi309 – 319Combined sources11
    Turni325 – 328Combined sources4
    Beta strandi329 – 335Combined sources7
    Beta strandi340 – 344Combined sources5
    Beta strandi347 – 352Combined sources6
    Beta strandi355 – 364Combined sources10
    Helixi370 – 388Combined sources19

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3HWOX-ray2.30A/B1-391[»]
    5JXZX-ray1.88A/B1-391[»]
    5JY4X-ray2.11A/B1-391[»]
    5JY8X-ray2.94A/B1-391[»]
    5JZDX-ray2.30A/B1-391[»]
    ProteinModelPortaliP0AEJ2.
    SMRiP0AEJ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEJ2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni214 – 215Substrate1 Publication2

    Sequence similaritiesi

    Belongs to the isochorismate synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105E4F. Bacteria.
    COG1169. LUCA.
    HOGENOMiHOG000028185.
    InParanoidiP0AEJ2.
    KOiK02361.
    OMAiMWHLSSR.
    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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti305 – 306SG → TA in AAA18491 (PubMed:2110093).Curated2

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3HWOX-ray2.30A/B1-391[»]
    5JXZX-ray1.88A/B1-391[»]
    5JY4X-ray2.11A/B1-391[»]
    5JY8X-ray2.94A/B1-391[»]
    5JZDX-ray2.30A/B1-391[»]
    ProteinModelPortaliP0AEJ2.
    SMRiP0AEJ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry databases

    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.
    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...

    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: November 2, 2016
    This is version 89 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.