TRPE_ECOLI
ID TRPE_ECOLI Reviewed; 520 AA.
AC P00895; P78249;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=b1264, JW1256;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7038627; DOI=10.1093/nar/9.24.6647;
RA Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E.,
RA Horowitz H., van Cleemput M., Wu A.M.;
RT "The complete nucleotide sequence of the tryptophan operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 9:6647-6668(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7021857; DOI=10.1016/0022-2836(81)90365-x;
RA Nichols B.P., van Cleemput M., Yanofsky C.;
RT "Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase
RT component I contains no tryptophan residues.";
RL J. Mol. Biol. 146:45-54(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=351195; DOI=10.1016/s0022-2836(78)80005-9;
RA Lee F., Bertrand K., Bennett G.N., Yanofsky C.;
RT "Comparison of the nucleotide sequences of the initial transcribed regions
RT of the tryptophan operons of Escherichia coli and Salmonella typhimurium.";
RL J. Mol. Biol. 121:193-217(1978).
RN [7]
RP PROTEIN SEQUENCE OF 1-25.
RC STRAIN=TRPA2/COLVB;
RX PubMed=4598537; DOI=10.1021/bi00705a028;
RA Li S.-L., Hanlon J., Yanofsky C.;
RT "Separation of anthranilate synthetase components I and II of Escherichia
RT coli, Salmonella typhimurium, and Serratia marcescens and determination of
RT their amino-terminal sequences by automatic Edman degradation.";
RL Biochemistry 13:1736-1744(1974).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=5333199; DOI=10.1016/s0021-9258(18)96383-0;
RA Baker T.I., Crawford I.P.;
RT "Anthranilate synthetase. Partial purification and some kinetic studies on
RT the enzyme from Escherichia coli.";
RL J. Biol. Chem. 241:5577-5584(1966).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=4886289; DOI=10.1128/jb.97.2.725-733.1969;
RA Ito J., Cox E.C., Yanofsky C.;
RT "Anthranilate synthetase, an enzyme specified by the tryptophan operon of
RT Escherichia coli: purification and characterization of component I.";
RL J. Bacteriol. 97:725-733(1969).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=4567790; DOI=10.1016/s0021-9258(19)44352-4;
RA Pabst M.J., Kuhn J.C., Somerville R.L.;
RT "Feedback regulation in the anthranilate aggregate from wild type and
RT mutant strains of Escherichia coli.";
RL J. Biol. Chem. 248:901-914(1973).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia.
CC {ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:4886289,
CC ECO:0000269|PubMed:5333199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000269|PubMed:4886289};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan.
CC {ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:4886289,
CC ECO:0000269|PubMed:5333199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for chorismate (at pH 7.5) {ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:4886289, ECO:0000269|PubMed:5333199};
CC KM=15 mM for ammonia (at 37 degrees Celsius and at pH 7.6)
CC {ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:4886289,
CC ECO:0000269|PubMed:5333199};
CC pH dependence:
CC Optimum pH is between 7.2 and 7.8. {ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:4886289, ECO:0000269|PubMed:5333199};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large lpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; V00368; CAA23666.1; -; Genomic_DNA.
DR EMBL; V00372; CAA23671.1; -; Genomic_DNA.
DR EMBL; J01714; AAA57297.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74346.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14799.1; -; Genomic_DNA.
DR EMBL; M24959; AAA24692.1; -; Genomic_DNA.
DR PIR; C64874; NNEC1.
DR RefSeq; NP_415780.1; NC_000913.3.
DR RefSeq; WP_001194582.1; NZ_SSZK01000031.1.
DR AlphaFoldDB; P00895; -.
DR SMR; P00895; -.
DR BioGRID; 4260124; 12.
DR BioGRID; 850213; 4.
DR ComplexPortal; CPX-4783; Anthranilate synthase complex.
DR IntAct; P00895; 25.
DR STRING; 511145.b1264; -.
DR jPOST; P00895; -.
DR PaxDb; P00895; -.
DR PRIDE; P00895; -.
DR EnsemblBacteria; AAC74346; AAC74346; b1264.
DR EnsemblBacteria; BAA14799; BAA14799; BAA14799.
DR GeneID; 945846; -.
DR KEGG; ecj:JW1256; -.
DR KEGG; eco:b1264; -.
DR PATRIC; fig|1411691.4.peg.1019; -.
DR EchoBASE; EB1021; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_4_6; -.
DR InParanoid; P00895; -.
DR OMA; AYRSFMN; -.
DR PhylomeDB; P00895; -.
DR BioCyc; EcoCyc:ANTHRANSYNCOMPI-MON; -.
DR BioCyc; MetaCyc:ANTHRANSYNCOMPI-MON; -.
DR SABIO-RK; P00895; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:P00895; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005950; C:anthranilate synthase complex; IC:ComplexPortal.
DR GO; GO:0004049; F:anthranilate synthase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:EcoCyc.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00565; trpE_proteo; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Direct protein sequencing; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..520
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154092"
FT BINDING 40
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 291..293
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 328..329
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 469
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 483..485
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 485
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT VARIANT 13
FT /note="C -> S (in strain: TRPA2/COLVB)"
FT CONFLICT 147
FT /note="G -> S (in Ref. 1; CAA23666 and 2; CAA23671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 57494 MW; 87696C0538CF66EA CRC64;
MQTQKPTLEL LTCEGAYRDN PTALFHQLCG DRPATLLLES ADIDSKDDLK SLLLVDSALR
ITALGDTVTI QALSGNGEAL LALLDNALPA GVESEQSPNC RVLRFPPVSP LLDEDARLCS
LSVFDAFRLL QNLLNVPKEE REAMFFGGLF SYDLVAGFED LPQLSAENNC PDFCFYLAET
LMVIDHQKKS TRIQASLFAP NEEEKQRLTA RLNELRQQLT EAAPPLPVVS VPHMRCECNQ
SDEEFGGVVR LLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND
FTLFGASPES SLKYDATSRQ IEIYPIAGTR PRGRRADGSL DRDLDSRIEL EMRTDHKELS
EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV SRVVGELRHD LDALHAYRAC
MNMGTLSGAP KVRAMQLIAE AEGRRRGSYG GAVGYFTAHG DLDTCIVIRS ALVENGIATV
QAGAGVVLDS VPQSEADETR NKARAVLRAI ATAHHAQETF
