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Anthranilate synthase component 1 (AS) (ASI) (EC 4.1.3.27)

 TRPE_SALTY              Reviewed;         520 AA.
P00898;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 3.
25-OCT-2017, entry version 144.
RecName: Full=Anthranilate synthase component 1;
Short=AS;
Short=ASI;
EC=4.1.3.27;
Name=trpE; OrderedLocusNames=STM1723;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7042989; DOI=10.1016/0022-2836(82)90003-1;
Yanofsky C., van Cleemput M.;
"Nucleotide sequence of trpE of Salmonella typhimurium and its
homology with the corresponding sequence of Escherichia coli.";
J. Mol. Biol. 155:235-246(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[3]
PROTEIN SEQUENCE OF 1-25.
STRAIN=ST-13;
PubMed=4598537; DOI=10.1021/bi00705a028;
Li S.-L., Hanlon J., Yanofsky C.;
"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.";
Biochemistry 13:1736-1744(1974).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
PubMed=351195; DOI=10.1016/S0022-2836(78)80005-9;
Lee F., Bertrand K., Bennett G.N., Yanofsky C.;
"Comparison of the nucleotide sequences of the initial transcribed
regions of the tryptophan operons of Escherichia coli and Salmonella
typhimurium.";
J. Mol. Biol. 121:193-217(1978).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 495-520.
STRAIN=LT2;
PubMed=7007652; DOI=10.1016/0022-2836(80)90260-0;
Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N.,
Yanofsky C.;
"Nucleotide sequences of the trpG regions of Escherichia coli,
Shigella dysenteriae, Salmonella typhimurium and Serratia
marcescens.";
J. Mol. Biol. 142:503-517(1980).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
SUBUNIT.
PubMed=4358945; DOI=10.1021/bi00699a024;
Grieshaber M., Bauerle R.;
"Monomeric and dimeric forms of component II of the anthranilate
synthetase--anthranilate 5-phosphoribosylpyrophosphate
phosphoribosyltransferase complex of Salmonella typhimurium.
Implications concerning the mode of assembly of the complex.";
Biochemistry 13:373-383(1974).
[7]
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
GLU-39; SER-40; ALA-41; ARG-128; CYS-174; ASN-288; PRO-289; MET-293;
PHE-294; GLY-305; ARG-402; GLY-460; CYS-465 AND HIS-515.
PubMed=2022650;
Caligiuri M.G., Bauerle R.;
"Identification of amino acid residues involved in feedback regulation
of the anthranilate synthase complex from Salmonella typhimurium.
Evidence for an amino-terminal regulatory site.";
J. Biol. Chem. 266:8328-8335(1991).
[8]
CRYSTALLIZATION, COFACTOR, AND SUBUNIT.
PubMed=10089433; DOI=10.1107/S0907444998010233;
Tolbert W.D., Chatterji S., Bauerle R., Kretsinger R.;
"Crystallization and preliminary crystallographic studies of the
anthranilate synthase partial complex from Salmonella typhimurium.";
Acta Crystallogr. D 55:305-306(1999).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-192 IN COMPLEX WITH
TRYPTOPHAN, ENZYME REGULATION, AND SUBUNIT.
PubMed=11224570; DOI=10.1038/84988;
Morollo A.A., Eck M.J.;
"Structure of the cooperative allosteric anthranilate synthase from
Salmonella typhimurium.";
Nat. Struct. Biol. 8:243-247(2001).
-!- FUNCTION: 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. {ECO:0000269|PubMed:4358945}.
-!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
pyruvate + L-glutamate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10089433};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:10089433};
-!- ENZYME REGULATION: Cooperatively feedback inhibited by tryptophan.
{ECO:0000269|PubMed:11224570, ECO:0000269|PubMed:2022650,
ECO:0000269|PubMed:4358945}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.3 uM for chorismate (PubMed:2022650)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
KM=4 uM for anthranilate (with the dimeric form and for the
phosphoribosyltransferase activity at pH 7.5)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
KM=6 uM for anthranilate (with the monomeric form and for the
phosphoribosyltransferase activity at pH 7.5)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
KM=10 uM for phosphoribosylpyrophosphate (with the monomeric and
dimeric forms and for the phosphoribosyltransferase activity at
pH 7.5) {ECO:0000269|PubMed:2022650,
ECO:0000269|PubMed:4358945};
KM=30 uM for magnesium ion (with the monomeric and dimeric forms
and for the phosphoribosyltransferase activity at pH 7.5)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
Vmax=5800 nmol/min/mg enzyme (with the dimeric form and for the
phosphoribosyltransferase activity at pH 7.5)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
Vmax=4700 nmol/min/mg enzyme (for the monomeric form at pH 7.5)
{ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945};
Note=Kcat is 12 (sec-1) for chorismate.
{ECO:0000269|PubMed:2022650};
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 1/5.
-!- SUBUNIT: Homodimer. In fact, exists in a monomer-dimer equilibrium
in solution, shifted spontaneously in favor of the dimer; the
monomer has a reduced activity compared with the dimer.
Heterotetramer consisting of two non-identical subunits: a beta
subunit (TrpG) and a large alpha subunit (TrpE) (Potential).
{ECO:0000305}.
-!- SIMILARITY: Belongs to the anthranilate synthase component I
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V01378; CAA24668.1; -; Genomic_DNA.
EMBL; AE006468; AAL20641.1; -; Genomic_DNA.
EMBL; M24960; AAA27238.1; -; Genomic_DNA.
EMBL; J01811; AAA57311.1; -; Genomic_DNA.
PIR; A92878; NNEB1T.
RefSeq; NP_460682.1; NC_003197.2.
RefSeq; WP_001194371.1; NC_003197.2.
PDB; 1I1Q; X-ray; 1.90 A; A=1-520.
PDBsum; 1I1Q; -.
ProteinModelPortal; P00898; -.
SMR; P00898; -.
IntAct; P00898; 1.
MINT; MINT-189120; -.
STRING; 99287.STM1723; -.
BindingDB; P00898; -.
ChEMBL; CHEMBL1075109; -.
PaxDb; P00898; -.
PRIDE; P00898; -.
EnsemblBacteria; AAL20641; AAL20641; STM1723.
GeneID; 1253242; -.
KEGG; stm:STM1723; -.
PATRIC; fig|99287.12.peg.1819; -.
eggNOG; ENOG4105CRQ; Bacteria.
eggNOG; COG0147; LUCA.
HOGENOM; HOG000025144; -.
KO; K01657; -.
OMA; AYRSFMN; -.
PhylomeDB; P00898; -.
UniPathway; UPA00035; UER00040.
EvolutionaryTrace; P00898; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0005950; C:anthranilate synthase complex; IBA:GO_Central.
GO; GO:0004049; F:anthranilate synthase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
Gene3D; 3.60.120.10; -; 1.
InterPro; IPR005801; ADC_synthase.
InterPro; IPR019999; Anth_synth_I-like.
InterPro; IPR006805; Anth_synth_I_N.
InterPro; IPR005257; Anth_synth_I_TrpE.
InterPro; IPR015890; Chorismate_C.
PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
Pfam; PF04715; Anth_synt_I_N; 1.
Pfam; PF00425; Chorismate_bind; 1.
PIRSF; PIRSF001373; TrpE; 1.
PRINTS; PR00095; ANTSNTHASEI.
SUPFAM; SSF56322; SSF56322; 1.
TIGRFAMs; TIGR00565; trpE_proteo; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
Aromatic amino acid biosynthesis; Complete proteome;
Direct protein sequencing; Lyase; Magnesium; Metal-binding;
Reference proteome; Tryptophan biosynthesis.
CHAIN 1 520 Anthranilate synthase component 1.
/FTId=PRO_0000154110.
REGION 291 293 Tryptophan binding.
REGION 328 329 Chorismate binding.
{ECO:0000250|UniProtKB:P00897}.
REGION 483 485 Chorismate binding.
{ECO:0000250|UniProtKB:P00897}.
METAL 361 361 Magnesium.
{ECO:0000250|UniProtKB:P00897}.
METAL 498 498 Magnesium.
{ECO:0000250|UniProtKB:P00897}.
BINDING 40 40 Tryptophan.
{ECO:0000269|PubMed:11224570}.
BINDING 50 50 Tryptophan.
{ECO:0000269|PubMed:11224570}.
BINDING 449 449 Chorismate.
{ECO:0000250|UniProtKB:P00897}.
BINDING 469 469 Chorismate.
{ECO:0000250|UniProtKB:P00897}.
BINDING 485 485 Chorismate; via amide nitrogen.
{ECO:0000250|UniProtKB:P00897}.
MUTAGEN 39 39 E->K: Complete loss of feedback control
by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 40 40 S->F: Complete loss of feedback control
by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 41 41 A->V: Decrease in feedback control by
tryptophan. {ECO:0000269|PubMed:2022650}.
MUTAGEN 128 128 R->H: Almost no change in feedback
control by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 174 174 C->Y: Almost no change in feedback
control by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 288 288 N->D: Decrease in feedback control by
tryptophan. {ECO:0000269|PubMed:2022650}.
MUTAGEN 289 289 P->L: Decrease in feedback control by
tryptophan. {ECO:0000269|PubMed:2022650}.
MUTAGEN 293 293 M->T: Complete loss of feedback control
by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 294 294 F->L: Decrease in feedback control by
tryptophan. {ECO:0000269|PubMed:2022650}.
MUTAGEN 305 305 G->S: Decrease in feedback control by
tryptophan. {ECO:0000269|PubMed:2022650}.
MUTAGEN 402 402 R->W: Almost no change in feedback
control by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 460 460 G->D: Almost no change in feedback
control by tryptophan.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 465 465 C->Y: Complete loss of feedback control
by tryptophan. 4-fold decrease of
affinity binding for chorismate.
{ECO:0000269|PubMed:2022650}.
MUTAGEN 515 515 H->Y: Almost no change in feedback
control by tryptophan.
{ECO:0000269|PubMed:2022650}.
CONFLICT 61 61 I -> F (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 70 70 I -> S (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 164 164 L -> H (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 179 179 E -> G (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 187 187 Q -> R (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 348 348 I -> T (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 359 360 LS -> PC (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 368 368 L -> P (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 395 395 Y -> C (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 397 397 M -> I (in Ref. 1; CAA24668).
{ECO:0000305}.
CONFLICT 481 481 Q -> R (in Ref. 1; CAA24668).
{ECO:0000305}.
STRAND 9 15 {ECO:0000244|PDB:1I1Q}.
HELIX 21 29 {ECO:0000244|PDB:1I1Q}.
STRAND 33 39 {ECO:0000244|PDB:1I1Q}.
HELIX 43 45 {ECO:0000244|PDB:1I1Q}.
STRAND 50 64 {ECO:0000244|PDB:1I1Q}.
STRAND 67 74 {ECO:0000244|PDB:1I1Q}.
HELIX 75 78 {ECO:0000244|PDB:1I1Q}.
HELIX 80 85 {ECO:0000244|PDB:1I1Q}.
STRAND 93 97 {ECO:0000244|PDB:1I1Q}.
STRAND 100 104 {ECO:0000244|PDB:1I1Q}.
HELIX 114 118 {ECO:0000244|PDB:1I1Q}.
HELIX 125 132 {ECO:0000244|PDB:1I1Q}.
STRAND 143 150 {ECO:0000244|PDB:1I1Q}.
HELIX 152 157 {ECO:0000244|PDB:1I1Q}.
STRAND 167 169 {ECO:0000244|PDB:1I1Q}.
STRAND 172 185 {ECO:0000244|PDB:1I1Q}.
TURN 186 189 {ECO:0000244|PDB:1I1Q}.
STRAND 190 197 {ECO:0000244|PDB:1I1Q}.
HELIX 202 220 {ECO:0000244|PDB:1I1Q}.
STRAND 237 240 {ECO:0000244|PDB:1I1Q}.
HELIX 242 257 {ECO:0000244|PDB:1I1Q}.
STRAND 262 264 {ECO:0000244|PDB:1I1Q}.
STRAND 267 273 {ECO:0000244|PDB:1I1Q}.
HELIX 277 287 {ECO:0000244|PDB:1I1Q}.
STRAND 291 297 {ECO:0000244|PDB:1I1Q}.
STRAND 302 309 {ECO:0000244|PDB:1I1Q}.
STRAND 311 315 {ECO:0000244|PDB:1I1Q}.
TURN 316 319 {ECO:0000244|PDB:1I1Q}.
STRAND 320 323 {ECO:0000244|PDB:1I1Q}.
STRAND 326 331 {ECO:0000244|PDB:1I1Q}.
HELIX 342 354 {ECO:0000244|PDB:1I1Q}.
HELIX 356 376 {ECO:0000244|PDB:1I1Q}.
STRAND 383 392 {ECO:0000244|PDB:1I1Q}.
STRAND 394 407 {ECO:0000244|PDB:1I1Q}.
HELIX 413 420 {ECO:0000244|PDB:1I1Q}.
HELIX 424 426 {ECO:0000244|PDB:1I1Q}.
STRAND 427 430 {ECO:0000244|PDB:1I1Q}.
HELIX 431 442 {ECO:0000244|PDB:1I1Q}.
TURN 447 450 {ECO:0000244|PDB:1I1Q}.
STRAND 451 457 {ECO:0000244|PDB:1I1Q}.
STRAND 462 466 {ECO:0000244|PDB:1I1Q}.
STRAND 469 474 {ECO:0000244|PDB:1I1Q}.
STRAND 477 483 {ECO:0000244|PDB:1I1Q}.
HELIX 492 513 {ECO:0000244|PDB:1I1Q}.
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


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