3-phosphoshikimate 1-carboxyvinyltransferase - Escherichia coli (strain K12)

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P0A6D3 (AROA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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 MF_00210
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. HAMAP MF_00210
Subunit structure	Monomer.
Subcellular location	Cytoplasm Probable HAMAP 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: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-phosphoshikimate 1-carboxyvinyltransferase activity Inferred from electronic annotation. Source: EC
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 MF_00210

PRO_0000088253

Sites

Site

408

Modified by bromopyruvate

Site

411

Modified by bromopyruvate

Natural variations

Natural variant

G → A Confers glyphosate inhibition.

Experimental info

Sequence conflict

S → T in CAA25223. Ref.1

Sequence conflict

330

T → R in CAA25223. Ref.1

Secondary structure

427

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6D3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B1F55469EB4D9F97
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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

« Hide

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. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [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: 9278503] [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: 16738553] [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: 1899181] [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: 8452542] [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: 11607190] [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.

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.

2D gel databases

SWISS-2DPAGE

P0A6D3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000220; EBESCP00000000220; EBESCG00000000179.
EBESCT00000015885; EBESCP00000015176; EBESCG00000014945.

GeneID

945528.

GenomeReviews

Gene locus JW0891 in contig AP009048_GR.
Gene locus b0908 in contig U00096_GR.

KEGG

ecj:JW0891.
eco:b0908.

PATRIC

32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASE

EB0071.

EcoGene

EG10073. aroA.

Phylogenomic databases

eggNOG

COG0128.

GeneTree

EBGT00050000011541.

HOGENOM

HBG646626.

OMA

GADIEWG.

PhylomeDB

P0A6D3.

ProtClustDB

PRK02427.

Enzyme and pathway databases

BioCyc

EcoCyc:AROA-MONOMER.
MetaCyc:AROA-MONOMER.

Gene expression databases

Genevestigator

P0A6D3.

Family and domain databases

HAMAP

MF_00210. EPSP_synth.
[Tree]

InterPro

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

Gene3D

G3DSA:3.65.10.10. EPSP_synthase. 2 hits.

K00800.

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...

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:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents