P0A6D3 (AROA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferase
EC=2.5.1.19

Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase
Short name=EPSP synthase
Short name=EPSPS

Gene names

Name:	aroA
Ordered Locus Names:	b0908, JW0891

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. HAMAP-Rule MF_00210
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. HAMAP-Rule MF_00210
Subunit structure	Monomer.
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_00210.
Sequence similarities	Belongs to the EPSP synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP chorismate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

3-phosphoshikimate 1-carboxyvinyltransferase HAMAP-Rule MF_00210

PRO_0000088253

Sites

Site

408

1

Modified by bromopyruvate

Site

411

1

Modified by bromopyruvate

Natural variations

Natural variant

96

1

G → A Confers glyphosate inhibition.

Experimental info

Sequence conflict

23

1

S → T in CAA25223. Ref.1

Sequence conflict

330

1

T → R in CAA25223. Ref.1

Secondary structure

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427

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

11 – 17

7

Helix

22 – 34

13

Beta strand

35 – 43

9

Helix

48 – 59

12

Beta strand

63 – 66

4

Beta strand

68 – 70

3

Beta strand

73 – 76

4

Beta strand

79 – 81

3

Beta strand

88 – 91

4

Helix

96 – 105

10

Beta strand

108 – 116

9

Helix

119 – 123

5

Helix

127 – 135

9

Beta strand

140 – 145

6

Beta strand

151 – 155

5

Beta strand

160 – 168

9

Helix

171 – 179

9

Helix

180 – 182

3

Beta strand

183 – 185

3

Beta strand

187 – 195

9

Helix

199 – 210

12

Beta strand

216 – 218

3

Turn

219 – 221

3

Beta strand

222 – 225

4

Beta strand

235 – 238

4

Helix

243 – 256

14

Beta strand

257 – 264

8

Helix

272 – 275

4

Helix

276 – 283

8

Beta strand

286 – 289

4

Beta strand

291 – 297

7

Beta strand

305 – 307

3

Turn

312 – 314

3

Helix

315 – 321

7

Helix

322 – 324

3

Beta strand

325 – 327

3

Beta strand

329 – 333

5

Helix

335 – 339

5

Beta strand

340 – 342

3

Helix

344 – 354

11

Beta strand

358 – 361

4

Beta strand

363 – 369

7

Helix

385 – 392

8

Helix

393 – 395

3

Beta strand

396 – 399

4

Beta strand

401 – 405

5

Helix

406 – 411

6

Helix

416 – 423

8

Sequences

	Sequence		Length	Mass (Da)
	P0A6D3 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: B1F55469EB4D9F97	FASTA	427	46,096
	10 20 30 40 50 60 MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV RHMLNALTAL 70 80 90 100 110 120 GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR 130 140 150 160 170 180 MKERPIGHLV DALRLGGAKI TYLEQENYPP LRLQGGFTGG NVDVDGSVSS QFLTALLMTA 190 200 210 220 230 240 PLAPEDTVIR IKGDLVSKPY IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE 250 260 270 280 290 300 GDASSASYFL AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE 310 320 330 340 350 360 LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE 370 380 390 400 410 420 EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFEQL ARISQAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence of Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase." Duncan K., Lewendon A., Coggins J.R. FEBS Lett. 170:59-63(1984) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Palma C.A., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M., Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Kim K., Komp C., Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-427. Strain: K12 / MG1655 / ATCC 47076.
[6]	"5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli --the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411." Huynh Q.K. Arch. Biochem. Biophys. 284:407-412(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INHIBITION BY BROMOPYRUVATE.
[7]	"Photo-oxidation of 5-enolpyruvoylshikimate-3-phosphate synthase from Escherichia coli: evidence for a reactive imidazole group (His385) at the herbicide glyphosate-binding site." Huynh Q.K. Biochem. J. 290:525-530(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOTO-OXIDATION AT HIS-385.
[8]	"Structure and topological symmetry of the glyphosate target 5-enol-pyruvylshikimate-3-phosphate synthase: a distinctive protein fold." Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.-S., Dayringer H.E., Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A., Padgette S.R., Kishore G.M. Proc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00557 Genomic DNA. Translation: CAA25223.1.
U00096 Genomic DNA. Translation: AAC73994.1.
AP009048 Genomic DNA. Translation: BAA35643.1.
U31523 Genomic DNA. Translation: AAA81514.1.

PIR

XUECVS. C64830.

RefSeq

NP_415428.1. NC_000913.2.
YP_489180.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EPS	X-ray	3.00	A	1-427	[»]
1G6S	X-ray	1.50	A	1-427	[»]
1G6T	X-ray	1.60	A	1-427	[»]
1MI4	X-ray	1.70	A	1-427	[»]
1P88	NMR	-	A	25-240	[»]
1P89	NMR	-	A	25-240	[»]
1Q0I	model	-	A	1-427	[»]
1Q0J	model	-	A	1-427	[»]
1Q36	X-ray	1.60	A	1-427	[»]
1X8R	X-ray	1.50	A	1-427	[»]
1X8T	X-ray	1.90	A	1-427	[»]
2AA9	X-ray	1.50	A	1-427	[»]
2AAY	X-ray	1.55	A	1-427	[»]
2PQ9	X-ray	1.60	A	1-427	[»]
2QFQ	X-ray	1.50	A	1-427	[»]
2QFS	X-ray	1.55	A	1-427	[»]
2QFT	X-ray	1.55	A	1-427	[»]
2QFU	X-ray	1.60	A	1-427	[»]
3FJX	X-ray	1.75	A	1-427	[»]
3FJZ	X-ray	1.70	A	1-427	[»]
3FK0	X-ray	1.70	A	1-427	[»]
3FK1	X-ray	1.70	A	1-427	[»]

ProteinModelPortal

P0A6D3.

SMR

P0A6D3. Positions 1-427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48256N.

IntAct

P0A6D3. 3 interactions.

STRING

511145.b0908.

2D gel databases

SWISS-2DPAGE

P0A6D3.

Proteomic databases

PaxDb

P0A6D3.

PRIDE

P0A6D3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.

GeneID

12931017.
945528.

KEGG

ecj:Y75_p0880.
eco:b0908.

PATRIC

32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASE

EB0071.

EcoGene

EG10073. aroA.

Phylogenomic databases

eggNOG

COG0128.

HOGENOM

HOG000247372.

KO

K00800.

OMA

GADIEWG.

ProtClustDB

PRK02427.

Enzyme and pathway databases

BioCyc

EcoCyc:AROA-MONOMER.
ECOL316407:JW0891-MONOMER.
MetaCyc:AROA-MONOMER.

SABIO-RK

P0A6D3.

UniPathway

UPA00053; UER00089.

Gene expression databases

Genevestigator

P0A6D3.

Family and domain databases

Gene3D

3.65.10.10. 2 hits.

HAMAP

MF_00210. EPSP_synth.

InterPro

IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]

Pfam

PF00275. EPSP_synthase. 1 hit.
[Graphical view]

PIRSF

PIRSF000505. EPSPS. 1 hit.

SUPFAM

SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.

TIGRFAMs

TIGR01356. aroA. 1 hit.

PROSITE

PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A6D3.

ChEMBL

CHEMBL5033.

EvolutionaryTrace

P0A6D3.

Entry information

Entry name

AROA_ECOLI

Accession

Primary (citable) accession number: P0A6D3
Secondary accession number(s): P07638, P78222

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program