P00897 (TRPE_SERMA) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Serratia marcescens

Taxonomic identifier

615 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
Cofactor	Binds 1 magnesium ion per subunit.
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
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	anthranilate synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpG	P00900	2	EBI-1031345,EBI-1031352

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 519

519

Anthranilate synthase component 1

PRO_0000154111

Sites

Metal binding

360

1

Magnesium

Metal binding

497

1

Magnesium

Experimental info

Sequence conflict

502 – 504

3

ARA → PVP Ref.4

Secondary structure

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519

Helix Strand Turn

Details...

Beta strand

8 – 14

7

Helix

20 – 28

9

Beta strand

32 – 40

9

Turn

42 – 44

3

Beta strand

47 – 63

17

Beta strand

66 – 71

6

Helix

76 – 78

3

Helix

79 – 86

8

Beta strand

91 – 96

6

Beta strand

99 – 103

5

Beta strand

109 – 111

3

Helix

113 – 117

5

Helix

123 – 130

8

Beta strand

132 – 134

3

Beta strand

142 – 149

8

Helix

151 – 156

6

Beta strand

171 – 184

14

Turn

185 – 188

4

Beta strand

189 – 196

8

Helix

201 – 218

18

Beta strand

236 – 239

4

Helix

241 – 256

16

Beta strand

261 – 263

3

Beta strand

266 – 272

7

Helix

277 – 286

10

Beta strand

290 – 296

7

Beta strand

301 – 307

7

Beta strand

309 – 314

6

Turn

315 – 318

4

Beta strand

319 – 322

4

Beta strand

325 – 329

5

Helix

341 – 353

13

Helix

355 – 375

21

Turn

378 – 380

3

Beta strand

382 – 391

10

Beta strand

396 – 406

11

Helix

412 – 419

8

Helix

423 – 425

3

Beta strand

426 – 429

4

Helix

430 – 441

12

Turn

446 – 449

4

Beta strand

450 – 456

7

Beta strand

461 – 465

5

Beta strand

468 – 473

6

Beta strand

476 – 482

7

Helix

491 – 512

22

Sequences

	Sequence		Length	Mass (Da)
	P00897 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: D3B59D47619FB0C1	FASTA	519	57,658
	10 20 30 40 50 60 MNTKPQLTLL KVQASYRGDP TTLFHQLCGA RPATLLLESA EINDKQNLQS LLVIDSALPI 70 80 90 100 110 120 TALGHTVSVQ ALTANGPALL PVLDEALPPE VRNQARPNGR ELTFPAIDAV QDEDARLRSL 130 140 150 160 170 180 SVFDALRTLL TLVDSPADER EAVMLGGLFA YDLVAGFENL PAVRQDQRCP DFCFYLAETL 190 200 210 220 230 240 LVLDHQRGSA RLQASVFSEQ ASEAQRLQHR LEQLQAELQQ PPQPIPHQKL ENMQLSCNQS 250 260 270 280 290 300 DEEYGAVVSE LQEAIRQGEI FQVVPSRRFS LPCPAPLGPY QTLKDNNPSP YMFFMQDDDF 310 320 330 340 350 360 TLFGASPESA LKYDAGNRQI EIYPIAGTRP RGRRADGSLD LDLDSRIELE MRTDHKELAE 370 380 390 400 410 420 HLMLVDLARN DLARICQAGS RYVADLTKVD RYSFVMHLVS RVVGTLRADL DVLHAYQACM 430 440 450 460 470 480 NMGTLSGAPK VRAMQLIAAL RSTRRGSYGG RVGYFTAHRH LDTCIVIRSA YVEDGHRTVQ 490 500 510 AGAGVVQDSI RRREADETRN KARAVLRAIA TAHHAKEVF

References

[1]	"The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan." Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., Mills S.E. Proc. Natl. Acad. Sci. U.S.A. 98:6021-6026(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[2]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25. Strain: SM6.
[3]	"The regulatory region of the trp operon of Serratia marcescens." Miozzari G.F., Yanofsky C. Nature 276:684-689(1978) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-519. Strain: SM6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY027546 Genomic DNA. Translation: AAA57308.2.

PIR

A01117.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I7Q	X-ray	1.95	A/C	1-519	[»]
1I7S	X-ray	2.40	A/C	1-519	[»]

ProteinModelPortal

P00897.

SMR

P00897. Positions 3-519.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00897. 1 interaction.

Proteomic databases

PRIDE

P00897.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00035; UER00040.

Family and domain databases

Gene3D

3.60.120.10. 1 hit.

InterPro

IPR005801. ADC_synthase.
IPR019999. Anth_synth_I.
IPR006805. Anth_synth_I_N.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate-bd_C.
[Graphical view]

Pfam

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

PIRSF

PIRSF001373. TrpE. 1 hit.

PRINTS

PR00095. ANTSNTHASEI.

SUPFAM

SSF56322. TRPE_1_chor_bd. 1 hit.

TIGRFAMs

TIGR00565. trpE_proteo. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00897.

Entry information

Entry name

TRPE_SERMA

Accession

Primary (citable) accession number: P00897

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 14, 2001
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program