Reviewed, UniProtKB/Swiss-Prot P00898 (TRPE_SALTY)

Names and origin

Protein names

Recommended name:
    Anthranilate synthase component 1
    EC=4.1.3.27
Alternative name(s):
    Anthranilate synthase component I

Gene names

Name:	trpE
Ordered Locus Names:	STM1723

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
Enzyme regulation	Feedback inhibited by tryptophan. Ref.6
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subunit structure	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.
Sequence similarities	Belongs to the anthranilate synthase component I family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	anthranilate synthase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpD	P00905	1	EBI-1030716,EBI-1030724

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

Anthranilate synthase component 1

PRO_0000154110

Experimental info

Mutagenesis

39

1

E → K: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. Ref.6

Mutagenesis

40

1

S → F: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. Ref.6

Mutagenesis

41

1

A → V: Decrease in feedback control by tryptophan. Ref.6

Mutagenesis

128

1

R → H: Almost no change in feedback control by tryptophan. Ref.6

Mutagenesis

174

1

C → Y: Almost no change in feedback control by tryptophan. Ref.6

Mutagenesis

288

1

N → D: Decrease in feedback control by tryptophan. Ref.6

Mutagenesis

289

1

P → L: Decrease in feedback control by tryptophan. Ref.6

Mutagenesis

293

1

M → T: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. Ref.6

Mutagenesis

294

1

F → L: Decrease in feedback control by tryptophan. Ref.6

Mutagenesis

305

1

G → S: Decrease in feedback control by tryptophan. Ref.6

Mutagenesis

402

1

R → W: Almost no change in feedback control by tryptophan. Ref.6

Mutagenesis

460

1

G → D: Almost no change in feedback control by tryptophan. Ref.6

Mutagenesis

465

1

C → Y: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. Ref.6

Mutagenesis

515

1

H → Y: Almost no change in feedback control by tryptophan. Ref.6

Sequence conflict

61

1

I → F in CAA24668. Ref.1

Sequence conflict

70

1

I → S in CAA24668. Ref.1

Sequence conflict

164

1

L → H in CAA24668. Ref.1

Sequence conflict

179

1

E → G in CAA24668. Ref.1

Sequence conflict

187

1

Q → R in CAA24668. Ref.1

Sequence conflict

348

1

I → T in CAA24668. Ref.1

Sequence conflict

359 – 360

2

LS → PC in CAA24668. Ref.1

Sequence conflict

368

1

L → P in CAA24668. Ref.1

Sequence conflict

395

1

Y → C Ref.1

Sequence conflict

397

1

M → I Ref.1

Sequence conflict

481

1

Q → R in CAA24668. Ref.1

Secondary structure

1

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520

Helix Strand Turn

Details...

Beta strand

9 – 15

7

Helix

21 – 29

9

Beta strand

33 – 39

7

Helix

43 – 45

3

Beta strand

50 – 64

15

Beta strand

67 – 74

8

Helix

75 – 78

4

Helix

80 – 85

6

Beta strand

93 – 97

5

Beta strand

100 – 104

5

Helix

114 – 118

5

Helix

125 – 132

8

Beta strand

143 – 150

8

Helix

152 – 157

6

Beta strand

167 – 169

3

Beta strand

172 – 185

14

Turn

186 – 189

4

Beta strand

190 – 197

8

Helix

202 – 220

19

Beta strand

237 – 240

4

Helix

242 – 257

16

Beta strand

262 – 264

3

Beta strand

267 – 273

7

Helix

277 – 287

11

Beta strand

291 – 297

7

Beta strand

302 – 309

8

Beta strand

311 – 315

5

Turn

316 – 319

4

Beta strand

320 – 323

4

Beta strand

326 – 331

6

Helix

342 – 354

13

Helix

356 – 376

21

Beta strand

383 – 392

10

Beta strand

394 – 407

14

Helix

413 – 420

8

Helix

424 – 426

3

Beta strand

427 – 430

4

Helix

431 – 442

12

Turn

447 – 450

4

Beta strand

451 – 457

7

Beta strand

462 – 466

5

Beta strand

469 – 474

6

Beta strand

477 – 483

7

Helix

492 – 513

22

Sequences

	Sequence		Length	Mass (Da)
	P00898-1 [UniParc]. Last modified January 23, 2002. Version 3. Checksum: B120E903DB7F8329	FASTA	520	57,088
	10 20 30 40 50 60 MQTPKPTLEL LTCDAAYREN PTALFHQVCG DRPATLLLES ADIDSKDDLK SLLLVDSALR 70 80 90 100 110 120 ITALGDTVTI QALSDNGASL LPLLDTALPA GVENDVLPAG RVLRFPPVSP LLDEDARLCS 130 140 150 160 170 180 LSVFDAFRLL QGVVNIPTQE REAMFFGGLF AYDLVAGFEA LPHLEAGNNC PDYCFYLAET 190 200 210 220 230 240 LMVIDHQKKS TRIQASLFTA SDREKQRLNA RLAYLSQQLT QPAPPLPVTP VPDMRCECNQ 250 260 270 280 290 300 SDDAFGAVVR QLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND 310 320 330 340 350 360 FTLFGASPES SLKYDAASRQ IEIYPIAGTR PRGRRADGTL DRDLDSRIEL DMRTDHKELS 370 380 390 400 410 420 EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV SRVVGELRHD LDALHAYRAC 430 440 450 460 470 480 MNMGTLSGAP KVRAMQLIAD AEGQRRGSYG GAVGYFTAHG DLDTCIVIRS ALVENGIATV 490 500 510 520 QAGAGIVLDS VPQSEADETR NKARAVLRAI ATAHHAQETF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of trpE of Salmonella typhimurium and its homology with the corresponding sequence of Escherichia coli." Yanofsky C., van Cleemput M. J. Mol. Biol. 155:235-246(1982) [PubMed: 7042989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." 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. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"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: 4598537] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25. Strain: ST-13.
[4]	"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: 351195] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[5]	"Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens." Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C. J. Mol. Biol. 142:503-517(1980) [PubMed: 7007652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 495-520. Strain: LT2.
[6]	"Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site." Caligiuri M.G., Bauerle R. J. Biol. Chem. 266:8328-8335(1991) [PubMed: 2022650] [Abstract] Cited for: ENZYME REGULATION, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V01378 Genomic DNA. Translation: CAA24668.1.
AE008776 Genomic DNA. Translation: AAL20641.1.
M24960 Genomic DNA. Translation: AAA27238.1.
J01811 Genomic DNA. Translation: AAA57311.1.

PIR

NNEB1T. A92878.

RefSeq

NP_460682.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I1Q	X-ray	1.90	A	1-520	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00898. 1 interaction.

Genome annotation databases

GeneID

1253242.

GenomeReviews

Gene locus STM1723 in contig AE006468_GR.

KEGG

stm:STM1723.

NMPDR

fig|99287.1.peg.1669.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P00898.

OMA

P00898. HKELAEH.

Enzyme and pathway databases

BioCyc

STYP99287:STM1723-MON.

BRENDA

4.1.3.27. 2.

Family and domain databases

InterPro

IPR005801. ADC_synthase.
IPR006805. Anth_synth_I_N.
IPR019999. Anthranilate_synth_I_C.
IPR015890. Chorismate-bd_C.
IPR005257. TrpE_synth.
[Graphical view]

Gene3D

G3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.

PANTHER

PTHR11236. TRPE_1_chor_bd. 1 hit.

Pfam

PF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]

PRINTS

PR00095. ANTSNTHASEI.

ProDom

PD000779. Anth_synth_chor. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00565. trpE_proteo. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TRPE_SALTY

Accession

Primary (citable) accession number: P00898

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2002
Last modified:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)