MG1655
W3110
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Gene Report : trpE
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion DE(tonB-cysB)206  ,  OCR68,69-1 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  trpE
Related strains
     Strains Search Search strains by gene name:  trpE   Search strains by all related name:  trpE anth b1264 ECK1258 JW1256 tryD tryp-4

General information  (Go to Linear View:)
 Gene Name trpE  
 Alternative name anth,b1264,ECK1258,JW1256,tryD,tryp-4  
 Location, Length 1,319,408 - 1,320,970 (  -  ) ;   28.44 min ; 1563 (bp) ,   520 (aa) Go to Linear View
 Product component I of anthranilate synthase  
 Operon Name trpLEDCBA  
 Note anthranilate synthase component I; GO_process: GO:0000162 - tryptophan biosynthetic process  
 Function enzyme; Amino acid biosynthesis: Tryptophan  
 Gene Ontology GO:0000162 ; tryptophan biosynthetic process ( trpE )
GO:0004049 ; anthranilate synthase activity ( trpE )
GO:0008652 ; amino acid biosynthetic process ( trpE )
GO:0009058 ; biosynthetic process ( trpE )
GO:0009073 ; aromatic amino acid family biosynthetic process ( trpE )
GO:0016829 ; lyase activity ( trpE )
GO:0016833 ; oxo-acid-lyase activity ( trpE )
 PID 1787518  
 EC number
  (KEGG Pathway)
 
4.1.3.27  
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene trpE ( EG11028 )  
    Number of removed 0 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) TRPE_ECOLI ( P00895 ; P78249 )
    -  Protein name Anthranilate synthase component I  
    -  Synonyms EC 4.1.3.27  
    -  Gene name Name=trpE; OrderedLocusNames=b1264;  
    -  Comments
  • CATALYTIC ACTIVITY:Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
  • PATHWAY:Tryptophan biosynthesis; first step.
  • SUBUNIT:Tetramer of two components I and two components II.
  • MISCELLANEOUS:Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
  • SIMILARITY:Belongs to the anthranilate synthase component I family.  
  •   botton Entry name(Acc.no) Q8FHV7 ( Q8FHV7 )
        -  Protein name Anthranilate synthase component I  
        -  Synonyms EC 4.1.3.27  
        -  Gene name Name=trpE; OrderedLocusNames=c1730;  
        -  Comments
  • FUNCTION:The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another (By similarity).
  • CATALYTIC ACTIVITY:ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
  • SIMILARITY:Belongs to the prokaryotic type I/III topoisomerase family.  

  •  Linear View (Whole Mode)
    View Location
       1310.0  –  1335.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP trpE (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Structure Of The Cooperative Allosteric Anthranilate Synthase From Salmonella Typhimurium  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Anthranilate synthase component 1  
             PSI-BLAST Anthranilate synthase component 1
        nr     (database updated : 2007.02.20 )
             BLAST anthranilate synthase component I [Escherichia coli K12]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    GLYCOSAMINOGLYCAN    CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    AMIDATION     

    Other Cross-Reference
        COG COG0147EH 
        EcoCyc trpE 

    MMBR References
    Gene. 1980;9(1-2):69-85.
    Construction of new cloning vehicles with genes of the tryptophan operon of Escherichia coli as genetic markers.
    Enger-Valk BE, Heyneker HL, Oosterbaan RA, Pouwels PH. ( 6247248 )
    J Mol Biol. 1969;44(1):117-27.
    Directed transposition of the arabinose operon: a technique for the isolation of specialized transducing bacteriophages for any Escherichia coli gene.
    Gottesman S, Beckwith JR. ( 4897798 )
    J Bacteriol. 1970;101(1):209-17.
    Mechanism of 3-methylanthranilic acid derepression of the tryptophan operon in Escherichia coli.
    Held WA, Smith OH. ( 4904235 )
    J Mol Biol. 1969;39(1):159-79.
    Operator mutants of the tryptophan operon in Escherichia coli.
    Hiraga S. ( 4938813 )
    J Bacteriol. 1971;107(1):8-15.
    Regulation of tyrosine biosynthesis in Escherichia coli K-12: isolation and characterization of operator mutants.
    Mattern IE, Pittard J. ( 4397929 )
    J Biol Chem. 1960;235:1098-102.
    False feedback inhibition: inhibition of tryptophan biosynthesis by 5-methyltryptophan.
    Moyed HS. ( 14424820 )
    J Mol Biol. 1980;142(4):503-17.
    Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens.
    Nichols BP, Miozzari GF, van Cleemput M, Bennett GN, Yanofsky C. ( 7007652 )
    J Mol Biol. 1981;146(1):45-54.
    Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues.
    Nichols BP, van Cleemput M, Yanofsky C. ( 7021857 )
    Proc Natl Acad Sci U S A. 1979;76:5524-5528
    Attenuation in the Escherichia coli tryptophan operon: role of RNA secondary structure involving the tryptophan codon region.
    Oxender, D. L., G. Zurawski, and C. Yanofsky.
    Nucleic Acids Res. 1981;9:6647-6668
    The complete nucleotide sequence of the tryptophan operon of E. coli.
    Yanofsky, C., T. Platt, I. P. Crawford, B. Nichols, G. E. Christie, H. Horowitz, M. VanCleemput, and A. M. Wu.

    Sequences
    Amino acid
    FASTA format
    0001 MQTQKPTLEL LTCEGAYRDN PTALFHQLCG DRPATLLLES ADIDSKDDLK SLLLVDSALR ITALGDTVTI 
    0071 QALSGNGEAL LALLDNALPA GVESEQSPNC RVLRFPPVSP LLDEDARLCS LSVFDAFRLL QNLLNVPKEE 
    0141 REAMFFGGLF SYDLVAGFED LPQLSAENNC PDFCFYLAET LMVIDHQKKS TRIQASLFAP NEEEKQRLTA 
    0211 RLNELRQQLT EAAPPLPVVS VPHMRCECNQ SDEEFGGVVR LLQKAIRAGE IFQVVPSRRF SLPCPSPLAA 
    0281 YYVLKKSNPS PYMFFMQDND FTLFGASPES SLKYDATSRQ IEIYPIAGTR PRGRRADGSL DRDLDSRIEL 
    0351 EMRTDHKELS EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV SRVVGELRHD LDALHAYRAC 
    0421 MNMGTLSGAP KVRAMQLIAE AEGRRRGSYG GAVGYFTAHG DLDTCIVIRS ALVENGIATV QAGAGVVLDS 
    0491 VPQSEADETR NKARAVLRAI ATAHHAQETF 
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             acttcctgaa acgggcagtg tattcaccat 
    -070 gcgtaaagca atcagatacc cagcccgcct aatgagcggg cttttttttg aacaaaatta gagaataaca 
    0001 atgcaaacac aaaaaccgac tctcgaactg ctaacctgcg aaggcgctta tcgcgacaat cccaccgcgc 
    0071 tttttcacca gttgtgtggg gatcgtccgg caacgctgct gctggaatcc gcagatatcg acagcaaaga 
    0141 tgatttaaaa agcctgctgc tggtagacag tgcgctgcgc attacagctt taggtgacac tgtcacaatc 
    0211 caggcacttt ccggcaacgg cgaagccctc ctggcactac tggataacgc cctgcctgcg ggtgtggaaa 
    0281 gtgaacaatc accaaactgc cgtgtgctgc gcttcccccc tgtcagtcca ctgctggatg aagacgcccg 
    0351 cttatgctcc ctttcggttt ttgacgcttt ccgtttattg cagaatctgt tgaatgtacc gaaggaagaa 
    0421 cgagaagcca tgttcttcgg cggcctgttc tcttatgacc ttgtggcggg atttgaagat ttaccgcaac 
    0491 tgtcagcgga aaataactgc cctgatttct gtttttatct cgctgaaacg ctgatggtga ttgaccatca 
    0561 gaaaaaaagc acccgtattc aggccagcct gtttgctccg aatgaagaag aaaaacaacg tctcactgct 
    0631 cgcctgaacg aactacgtca gcaactgacc gaagccgcgc cgccgctgcc agtggtttcc gtgccgcata 
    0701 tgcgttgtga atgtaatcag agcgatgaag agttcggtgg cgtagtgcgt ttgttgcaaa aagcgattcg 
    0771 cgctggagaa attttccagg tggtgccatc tcgccgtttc tctctgccct gcccgtcacc gctggcggcc 
    0841 tattacgtgc tgaaaaagag taatcccagc ccgtacatgt tttttatgca ggataatgat ttcaccctat 
    0911 ttggcgcgtc gccggaaagc tcgctcaagt atgatgccac cagccgccag attgagatct acccgattgc 
    0981 cggaacacgc ccacgcggtc gtcgcgccga tggttcactg gacagagatc tcgacagccg tattgaactg 
    1051 gaaatgcgta ccgatcataa agagctgtct gaacatctga tgctggttga tctcgcccgt aatgatctgg 
    1121 cacgcatttg cacccccggc agccgctacg tcgccgatct caccaaagtt gaccgttatt cctatgtgat 
    1191 gcacctcgtc tctcgcgtag tcggcgaact gcgtcacgat cttgacgccc tgcacgctta tcgcgcctgt 
    1261 atgaatatgg ggacgttaag cggtgcgccg aaagtacgcg ctatgcagtt aattgccgag gcggaaggtc 
    1331 gtcgccgcgg cagctacggc ggcgcggtag gttatttcac cgcgcatggc gatctcgaca cctgcattgt 
    1401 gatccgctcg gcgctggtgg aaaacggtat cgccaccgtg caagcgggtg ctggtgtagt ccttgattct 
    1471 gttccgcagt cggaagccga cgaaacccgt aacaaagccc gcgctgtact gcgcgctatt gccaccgcgc 
    1541 atcatgcaca ggagactttc tgatggctga cattctgctg ctcgataata tcgactcttt tacgtacaac 
    1611 ctggcagatc agttgcgcag caatgggcat aacgtggtga tttaccgcaa cca