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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.UniRule annotation

Catalytic activityi

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation

Pathwayi: chorismate biosynthesis

This protein is involved in step 6 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (CBU_0982)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261Shikimate-3-phosphateUniRule annotation1 Publication
Binding sitei123 – 1231PhosphoenolpyruvateUniRule annotation1 Publication
Active sitei315 – 3151Proton acceptorUniRule annotation1 Publication
Binding sitei342 – 3421Shikimate-3-phosphateUniRule annotation1 Publication
Active sitei343 – 3431Proton donorUniRule annotation
Binding sitei346 – 3461PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei387 – 3871PhosphoenolpyruvateUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciCBUR227377:GJ7S-529-MONOMER.
UniPathwayiUPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthaseUniRule annotation
Short name:
EPSP synthaseUniRule annotation
Short name:
EPSPSUniRule annotation
Gene namesi
Name:aroAUniRule annotation
Ordered Locus Names:CBU_0526
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4384383-phosphoshikimate 1-carboxyvinyltransferasePRO_1000071737Add
BLAST

Proteomic databases

PRIDEiQ83E11.

Interactioni

Subunit structurei

Homodimer or homotetramer.3 Publications

Protein-protein interaction databases

STRINGi227377.CBU_0526.

Structurei

Secondary structure

438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 55Combined sources
Beta strandi12 – 165Combined sources
Helixi21 – 3313Combined sources
Beta strandi34 – 429Combined sources
Helixi47 – 5812Combined sources
Beta strandi62 – 665Combined sources
Helixi67 – 693Combined sources
Beta strandi71 – 755Combined sources
Helixi95 – 10511Combined sources
Beta strandi108 – 1158Combined sources
Helixi120 – 1223Combined sources
Helixi126 – 1349Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi164 – 1663Combined sources
Helixi168 – 17811Combined sources
Beta strandi181 – 1888Combined sources
Helixi196 – 2038Combined sources
Beta strandi215 – 2184Combined sources
Helixi234 – 24613Combined sources
Beta strandi251 – 2588Combined sources
Helixi261 – 2633Combined sources
Helixi265 – 2739Combined sources
Beta strandi276 – 28510Combined sources
Beta strandi288 – 2969Combined sources
Helixi307 – 3093Combined sources
Helixi310 – 3134Combined sources
Helixi314 – 3163Combined sources
Helixi317 – 3259Combined sources
Beta strandi327 – 3337Combined sources
Helixi337 – 3415Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 35611Combined sources
Beta strandi360 – 3645Combined sources
Beta strandi367 – 3715Combined sources
Beta strandi378 – 3814Combined sources
Helixi386 – 39813Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi403 – 4064Combined sources
Helixi409 – 4135Combined sources
Helixi418 – 4258Combined sources
Beta strandi429 – 4335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ROIX-ray2.20A/B1-438[»]
3SLHX-ray1.70A/B/C/D1-438[»]
3TR1X-ray2.00A1-438[»]
4EGRX-ray2.50A/B/C/D/E/F1-438[»]
4GFPX-ray2.70A1-438[»]
4ZNDX-ray2.55A1-438[»]
ProteinModelPortaliQ83E11.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 222Shikimate-3-phosphate bindingUniRule annotation1 Publication
Regioni93 – 964PhosphoenolpyruvateUniRule annotation2 Publications

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
HOGENOMiHOG000247371.
KOiK00800.
OMAiMAFADCG.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000505. EPSPS. 1 hit.
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
PROSITEiPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83E11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYQTIPSQG LSGEICVPGD KSISHRAVLL AAIAEGQTQV DGFLMGADNL
60 70 80 90 100
AMVSALQQMG ASIQVIEDEN ILVVEGVGMT GLQAPPEALD CGNSGTAIRL
110 120 130 140 150
LSGLLAGQPF NTVLTGDSSL QRRPMKRIID PLTLMGAKID STGNVPPLKI
160 170 180 190 200
YGNPRLTGIH YQLPMASAQV KSCLLLAGLY ARGKTCITEP APSRDHTERL
210 220 230 240 250
LKHFHYTLQK DKQSICVSGG GKLKANDISI PGDISSAAFF IVAATITPGS
260 270 280 290 300
AIRLCRVGVN PTRLGVINLL KMMGADIEVT HYTEKNEEPT ADITVRHARL
310 320 330 340 350
KGIDIPPDQV PLTIDEFPVL LIAAAVAQGK TVLRDAAELR VKETDRIAAM
360 370 380 390 400
VDGLQKLGIA AESLPDGVII QGGTLEGGEV NSYDDHRIAM AFAVAGTLAK
410 420 430
GPVRIRNCDN VKTSFPNFVE LANEVGMNVK GVRGRGGF
Length:438
Mass (Da):46,432
Last modified:June 1, 2003 - v1
Checksum:iEF1C0FEEEBCD4D54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90072.1.
RefSeqiNP_819558.1. NC_002971.3.
WP_010957637.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO90072; AAO90072; CBU_0526.
GeneIDi1208411.
KEGGicbu:CBU_0526.
PATRICi17929753. VBICoxBur82552_0521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90072.1.
RefSeqiNP_819558.1. NC_002971.3.
WP_010957637.1. NC_002971.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ROIX-ray2.20A/B1-438[»]
3SLHX-ray1.70A/B/C/D1-438[»]
3TR1X-ray2.00A1-438[»]
4EGRX-ray2.50A/B/C/D/E/F1-438[»]
4GFPX-ray2.70A1-438[»]
4ZNDX-ray2.55A1-438[»]
ProteinModelPortaliQ83E11.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_0526.

Proteomic databases

PRIDEiQ83E11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO90072; AAO90072; CBU_0526.
GeneIDi1208411.
KEGGicbu:CBU_0526.
PATRICi17929753. VBICoxBur82552_0521.

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
HOGENOMiHOG000247371.
KOiK00800.
OMAiMAFADCG.
OrthoDBiEOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00089.
BioCyciCBUR227377:GJ7S-529-MONOMER.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000505. EPSPS. 1 hit.
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
PROSITEiPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RSA 493 / Nine Mile phase I.
  2. "2.20 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Light S.H., Minasov G., Krishna S.N., Halavaty A.S., Shuvalova L., Papazisi L., Anderson W.F.
    Submitted (APR-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), SUBUNIT.
  3. "1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase(AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Light S.H., Minasov G., Filippova E.V., Krishna S.N., Shuvalova L., Papazisi L., Anderson W.F.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANLOG, ACTIVE SITE, SUBUNIT.
  4. "Structure of a 3-phosphoshikimate 1-carboxyvinyltransferase (aroA) from Coxiella burnetii."
    Cheung J., Franklin M., Rudolph M., Cassidy M., Gary E., Burshteyn F., Love J.
    Submitted (SEP-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHATES.
  5. "2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate."
    Krishna S.N., Light S.H., Minasov G., Shuvalova L., Kwon K., Anderson W.F.
    Submitted (MAR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVATE, SUBUNIT.
  6. "2.7 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in second conformational state."
    Light S.H., Minasov G., Krishna S.N., Shuvalova L., Papazisi L., Anderson W.F.
    Submitted (AUG-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).

Entry informationi

Entry nameiAROA_COXBU
AccessioniPrimary (citable) accession number: Q83E11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 1, 2003
Last modified: November 11, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.