TRPE_SALTY
ID TRPE_SALTY Reviewed; 520 AA.
AC P00898;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=STM1723;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7042989; DOI=10.1016/0022-2836(82)90003-1;
RA Yanofsky C., van Cleemput M.;
RT "Nucleotide sequence of trpE of Salmonella typhimurium and its homology
RT with the corresponding sequence of Escherichia coli.";
RL J. Mol. Biol. 155:235-246(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-25.
RC STRAIN=ST-13;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 495-520.
RC STRAIN=LT2;
RX PubMed=7007652; DOI=10.1016/0022-2836(80)90260-0;
RA Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.;
RT "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella
RT dysenteriae, Salmonella typhimurium and Serratia marcescens.";
RL J. Mol. Biol. 142:503-517(1980).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=4358945; DOI=10.1021/bi00699a024;
RA Grieshaber M., Bauerle R.;
RT "Monomeric and dimeric forms of component II of the anthranilate
RT synthetase--anthranilate 5-phosphoribosylpyrophosphate
RT phosphoribosyltransferase complex of Salmonella typhimurium. Implications
RT concerning the mode of assembly of the complex.";
RL Biochemistry 13:373-383(1974).
RN [7]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP GLU-39; SER-40; ALA-41; ARG-128; CYS-174; ASN-288; PRO-289; MET-293;
RP PHE-294; GLY-305; ARG-402; GLY-460; CYS-465 AND HIS-515.
RX PubMed=2022650; DOI=10.1016/s0021-9258(18)92979-0;
RA Caligiuri M.G., Bauerle R.;
RT "Identification of amino acid residues involved in feedback regulation of
RT the anthranilate synthase complex from Salmonella typhimurium. Evidence for
RT an amino-terminal regulatory site.";
RL J. Biol. Chem. 266:8328-8335(1991).
RN [8]
RP CRYSTALLIZATION, COFACTOR, AND SUBUNIT.
RX PubMed=10089433; DOI=10.1107/s0907444998010233;
RA Tolbert W.D., Chatterji S., Bauerle R., Kretsinger R.;
RT "Crystallization and preliminary crystallographic studies of the
RT anthranilate synthase partial complex from Salmonella typhimurium.";
RL Acta Crystallogr. D 55:305-306(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-192 IN COMPLEX WITH TRYPTOPHAN,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=11224570; DOI=10.1038/84988;
RA Morollo A.A., Eck M.J.;
RT "Structure of the cooperative allosteric anthranilate synthase from
RT Salmonella typhimurium.";
RL Nat. Struct. Biol. 8:243-247(2001).
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:4358945}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10089433};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10089433};
CC -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan.
CC {ECO:0000269|PubMed:11224570, ECO:0000269|PubMed:2022650,
CC ECO:0000269|PubMed:4358945}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for chorismate {ECO:0000269|PubMed:2022650};
CC KM=4 uM for anthranilate (with the dimeric form and for the
CC phosphoribosyltransferase activity at pH 7.5)
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC KM=6 uM for anthranilate (with the monomeric form and for the
CC phosphoribosyltransferase activity at pH 7.5)
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC KM=10 uM for phosphoribosylpyrophosphate (with the monomeric and
CC dimeric forms and for the phosphoribosyltransferase activity at pH
CC 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC KM=30 uM for magnesium ion (with the monomeric and dimeric forms and
CC for the phosphoribosyltransferase activity at pH 7.5)
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC Vmax=5800 nmol/min/mg enzyme (with the dimeric form and for the
CC phosphoribosyltransferase activity at pH 7.5)
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC Vmax=4700 nmol/min/mg enzyme (for the monomeric form at pH 7.5)
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
CC Note=kcat is 12 sec(-1) for chorismate. {ECO:0000269|PubMed:2022650};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Homodimer. In fact, exists in a monomer-dimer equilibrium in
CC solution, shifted spontaneously in favor of the dimer; the monomer has
CC a reduced activity compared with the dimer. Heterotetramer consisting
CC of two non-identical subunits: a beta subunit (TrpG) and a large alpha
CC subunit (TrpE) (Potential). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; V01378; CAA24668.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20641.1; -; Genomic_DNA.
DR EMBL; M24960; AAA27238.1; -; Genomic_DNA.
DR EMBL; J01811; AAA57311.1; -; Genomic_DNA.
DR PIR; A92878; NNEB1T.
DR RefSeq; NP_460682.1; NC_003197.2.
DR RefSeq; WP_001194371.1; NC_003197.2.
DR PDB; 1I1Q; X-ray; 1.90 A; A=1-520.
DR PDBsum; 1I1Q; -.
DR AlphaFoldDB; P00898; -.
DR SMR; P00898; -.
DR IntAct; P00898; 1.
DR MINT; P00898; -.
DR STRING; 99287.STM1723; -.
DR BindingDB; P00898; -.
DR ChEMBL; CHEMBL1075109; -.
DR PaxDb; P00898; -.
DR PRIDE; P00898; -.
DR EnsemblBacteria; AAL20641; AAL20641; STM1723.
DR GeneID; 1253242; -.
DR KEGG; stm:STM1723; -.
DR PATRIC; fig|99287.12.peg.1819; -.
DR HOGENOM; CLU_006493_9_4_6; -.
DR PhylomeDB; P00898; -.
DR BioCyc; SENT99287:STM1723-MON; -.
DR SABIO-RK; P00898; -.
DR UniPathway; UPA00035; UER00040.
DR EvolutionaryTrace; P00898; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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 3D-structure; 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_0000154110"
FT BINDING 40
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:11224570"
FT BINDING 50
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:11224570"
FT BINDING 291..293
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
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 MUTAGEN 39
FT /note="E->K: Complete loss of feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 40
FT /note="S->F: Complete loss of feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 41
FT /note="A->V: Decrease in feedback control by tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 128
FT /note="R->H: Almost no change in feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 174
FT /note="C->Y: Almost no change in feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 288
FT /note="N->D: Decrease in feedback control by tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 289
FT /note="P->L: Decrease in feedback control by tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 293
FT /note="M->T: Complete loss of feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 294
FT /note="F->L: Decrease in feedback control by tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 305
FT /note="G->S: Decrease in feedback control by tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 402
FT /note="R->W: Almost no change in feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 460
FT /note="G->D: Almost no change in feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 465
FT /note="C->Y: Complete loss of feedback control by
FT tryptophan. 4-fold decrease of affinity binding for
FT chorismate."
FT /evidence="ECO:0000269|PubMed:2022650"
FT MUTAGEN 515
FT /note="H->Y: Almost no change in feedback control by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:2022650"
FT CONFLICT 61
FT /note="I -> F (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="I -> S (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="L -> H (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> G (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="Q -> R (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="I -> T (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="LS -> PC (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="L -> P (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="Y -> C (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="M -> I (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="Q -> R (in Ref. 1; CAA24668)"
FT /evidence="ECO:0000305"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 50..64
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:1I1Q"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 202..220
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1I1Q"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 356..376
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 394..407
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:1I1Q"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 492..513
FT /evidence="ECO:0007829|PDB:1I1Q"
SQ SEQUENCE 520 AA; 57088 MW; B120E903DB7F8329 CRC64;
MQTPKPTLEL LTCDAAYREN PTALFHQVCG DRPATLLLES ADIDSKDDLK SLLLVDSALR
ITALGDTVTI QALSDNGASL LPLLDTALPA GVENDVLPAG RVLRFPPVSP LLDEDARLCS
LSVFDAFRLL QGVVNIPTQE REAMFFGGLF AYDLVAGFEA LPHLEAGNNC PDYCFYLAET
LMVIDHQKKS TRIQASLFTA SDREKQRLNA RLAYLSQQLT QPAPPLPVTP VPDMRCECNQ
SDDAFGAVVR QLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND
FTLFGASPES SLKYDAASRQ IEIYPIAGTR PRGRRADGTL DRDLDSRIEL DMRTDHKELS
EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV SRVVGELRHD LDALHAYRAC
MNMGTLSGAP KVRAMQLIAD AEGQRRGSYG GAVGYFTAHG DLDTCIVIRS ALVENGIATV
QAGAGIVLDS VPQSEADETR NKARAVLRAI ATAHHAQETF
