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Protein

Anthranilate synthase component 1

Gene

trpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.3 Publications

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

Cooperatively feedback inhibited by tryptophan.3 Publications

Kineticsi

  1. KM=1.2 µM for chorismate (at pH 7.5)3 Publications
  2. KM=15 mM for ammonia (at 37 degrees Celsius and at pH 7.6)3 Publications

    pH dependencei

    Optimum pH is between 7.2 and 7.8.3 Publications

    Pathwayi: L-tryptophan biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-tryptophan from chorismate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
    2. Bifunctional protein TrpGD (trpGD)
    3. Tryptophan biosynthesis protein TrpCF (trpC)
    4. Tryptophan biosynthesis protein TrpCF (trpC)
    5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
    This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401TryptophanBy similarity
    Metal bindingi361 – 3611MagnesiumBy similarity
    Binding sitei449 – 4491ChorismateBy similarity
    Binding sitei469 – 4691ChorismateBy similarity
    Binding sitei485 – 4851Chorismate; via amide nitrogenBy similarity
    Metal bindingi498 – 4981MagnesiumBy similarity

    GO - Molecular functioni

    • anthranilate synthase activity Source: EcoCyc
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ANTHRANSYNCOMPI-MONOMER.
    ECOL316407:JW1256-MONOMER.
    MetaCyc:ANTHRANSYNCOMPI-MONOMER.
    UniPathwayiUPA00035; UER00040.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate synthase component 1 (EC:4.1.3.27)
    Short name:
    AS
    Short name:
    ASI
    Gene namesi
    Name:trpE
    Ordered Locus Names:b1264, JW1256
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11028. trpE.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Anthranilate synthase component 1PRO_0000154092Add
    BLAST

    Proteomic databases

    PaxDbiP00895.
    PRIDEiP00895.

    Interactioni

    Subunit structurei

    Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large lpha subunit (TrpE).By similarity

    Protein-protein interaction databases

    BioGridi4260124. 12 interactions.
    IntActiP00895. 25 interactions.
    STRINGi511145.b1264.

    Structurei

    3D structure databases

    ProteinModelPortaliP00895.
    SMRiP00895. Positions 5-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni291 – 2933Tryptophan bindingBy similarity
    Regioni328 – 3292Chorismate bindingBy similarity
    Regioni483 – 4853Chorismate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CRQ. Bacteria.
    COG0147. LUCA.
    HOGENOMiHOG000025144.
    InParanoidiP00895.
    KOiK01657.
    OMAiMQDQDFT.
    OrthoDBiEOG6D5G6B.
    PhylomeDBiP00895.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR019999. Anth_synth_I-like.
    IPR006805. Anth_synth_I_N.
    IPR005257. Anth_synth_I_TrpE.
    IPR015890. Chorismate_C.
    [Graphical view]
    PfamiPF04715. Anth_synt_I_N. 1 hit.
    PF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001373. TrpE. 1 hit.
    PRINTSiPR00095. ANTSNTHASEI.
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00565. trpE_proteo. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P00895-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQTQKPTLEL LTCEGAYRDN PTALFHQLCG DRPATLLLES ADIDSKDDLK
    60 70 80 90 100
    SLLLVDSALR ITALGDTVTI QALSGNGEAL LALLDNALPA GVESEQSPNC
    110 120 130 140 150
    RVLRFPPVSP LLDEDARLCS LSVFDAFRLL QNLLNVPKEE REAMFFGGLF
    160 170 180 190 200
    SYDLVAGFED LPQLSAENNC PDFCFYLAET LMVIDHQKKS TRIQASLFAP
    210 220 230 240 250
    NEEEKQRLTA RLNELRQQLT EAAPPLPVVS VPHMRCECNQ SDEEFGGVVR
    260 270 280 290 300
    LLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND
    310 320 330 340 350
    FTLFGASPES SLKYDATSRQ IEIYPIAGTR PRGRRADGSL DRDLDSRIEL
    360 370 380 390 400
    EMRTDHKELS EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV
    410 420 430 440 450
    SRVVGELRHD LDALHAYRAC MNMGTLSGAP KVRAMQLIAE AEGRRRGSYG
    460 470 480 490 500
    GAVGYFTAHG DLDTCIVIRS ALVENGIATV QAGAGVVLDS VPQSEADETR
    510 520
    NKARAVLRAI ATAHHAQETF
    Length:520
    Mass (Da):57,494
    Last modified:November 1, 1997 - v2
    Checksum:i87696C0538CF66EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471G → S in CAA23666 (PubMed:7038627).Curated
    Sequence conflicti147 – 1471G → S in CAA23671 (PubMed:7021857).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131C → S in strain: TRPA2/COLVB.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00368 Genomic DNA. Translation: CAA23666.1.
    V00372 Genomic DNA. Translation: CAA23671.1.
    J01714 Genomic DNA. Translation: AAA57297.1.
    U00096 Genomic DNA. Translation: AAC74346.1.
    AP009048 Genomic DNA. Translation: BAA14799.1.
    M24959 Genomic DNA. Translation: AAA24692.1.
    PIRiC64874. NNEC1.
    RefSeqiNP_415780.1. NC_000913.3.
    WP_001194582.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74346; AAC74346; b1264.
    BAA14799; BAA14799; BAA14799.
    GeneIDi945846.
    KEGGiecj:JW1256.
    eco:b1264.
    PATRICi32117788. VBIEscCol129921_1314.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00368 Genomic DNA. Translation: CAA23666.1.
    V00372 Genomic DNA. Translation: CAA23671.1.
    J01714 Genomic DNA. Translation: AAA57297.1.
    U00096 Genomic DNA. Translation: AAC74346.1.
    AP009048 Genomic DNA. Translation: BAA14799.1.
    M24959 Genomic DNA. Translation: AAA24692.1.
    PIRiC64874. NNEC1.
    RefSeqiNP_415780.1. NC_000913.3.
    WP_001194582.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP00895.
    SMRiP00895. Positions 5-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260124. 12 interactions.
    IntActiP00895. 25 interactions.
    STRINGi511145.b1264.

    Proteomic databases

    PaxDbiP00895.
    PRIDEiP00895.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74346; AAC74346; b1264.
    BAA14799; BAA14799; BAA14799.
    GeneIDi945846.
    KEGGiecj:JW1256.
    eco:b1264.
    PATRICi32117788. VBIEscCol129921_1314.

    Organism-specific databases

    EchoBASEiEB1021.
    EcoGeneiEG11028. trpE.

    Phylogenomic databases

    eggNOGiENOG4105CRQ. Bacteria.
    COG0147. LUCA.
    HOGENOMiHOG000025144.
    InParanoidiP00895.
    KOiK01657.
    OMAiMQDQDFT.
    OrthoDBiEOG6D5G6B.
    PhylomeDBiP00895.

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00040.
    BioCyciEcoCyc:ANTHRANSYNCOMPI-MONOMER.
    ECOL316407:JW1256-MONOMER.
    MetaCyc:ANTHRANSYNCOMPI-MONOMER.

    Miscellaneous databases

    PROiP00895.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR019999. Anth_synth_I-like.
    IPR006805. Anth_synth_I_N.
    IPR005257. Anth_synth_I_TrpE.
    IPR015890. Chorismate_C.
    [Graphical view]
    PfamiPF04715. Anth_synt_I_N. 1 hit.
    PF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001373. TrpE. 1 hit.
    PRINTSiPR00095. ANTSNTHASEI.
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00565. trpE_proteo. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
      Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
      Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues."
      Nichols B.P., van Cleemput M., Yanofsky C.
      J. Mol. Biol. 146:45-54(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "Comparison of the nucleotide sequences of the initial transcribed regions of the tryptophan operons of Escherichia coli and Salmonella typhimurium."
      Lee F., Bertrand K., Bennett G.N., Yanofsky C.
      J. Mol. Biol. 121:193-217(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    7. "Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation."
      Li S.-L., Hanlon J., Yanofsky C.
      Biochemistry 13:1736-1744(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25.
      Strain: TRPA2/COLVB.
    8. "Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli."
      Baker T.I., Crawford I.P.
      J. Biol. Chem. 241:5577-5584(1966) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    9. "Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: purification and characterization of component I."
      Ito J., Cox E.C., Yanofsky C.
      J. Bacteriol. 97:725-733(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    10. "Feedback regulation in the anthranilate aggregate from wild type and mutant strains of Escherichia coli."
      Pabst M.J., Kuhn J.C., Somerville R.L.
      J. Biol. Chem. 248:901-914(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.

    Entry informationi

    Entry nameiTRPE_ECOLI
    AccessioniPrimary (citable) accession number: P00895
    Secondary accession number(s): P78249
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1997
    Last modified: May 11, 2016
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, 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. 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.