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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 (VC_1507), Phospho-2-dehydro-3-deoxyheptonate aldolase (VC_0695)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ)
  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)DescriptionActionsGraphical viewLength
Binding sitei27Shikimate-3-phosphateUniRule annotation1 Publication1
Binding sitei124PhosphoenolpyruvateUniRule annotation1 Publication1
Binding sitei198Shikimate-3-phosphateUniRule annotation1 Publication1
Active sitei314Proton acceptorUniRule annotation1 Publication1
Binding sitei337Shikimate-3-phosphateUniRule annotation1 Publication1
Binding sitei341Shikimate-3-phosphateUniRule annotation1 Publication1
Active sitei342Proton donorUniRule annotation1 Publication1
Binding sitei345PhosphoenolpyruvateUniRule annotation1 Publication1
Binding sitei387PhosphoenolpyruvateUniRule annotation1 Publication1
Binding sitei412PhosphoenolpyruvateUniRule annotation1

GO - Molecular functioni

  • 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: TIGR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciVCHO:VC1732-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:VC_1732
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000883141 – 4263-phosphoshikimate 1-carboxyvinyltransferaseAdd BLAST426

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243277.VC1732.

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi14 – 17Combined sources4
Helixi22 – 34Combined sources13
Beta strandi35 – 43Combined sources9
Helixi48 – 59Combined sources12
Beta strandi63 – 66Combined sources4
Beta strandi73 – 76Combined sources4
Beta strandi88 – 91Combined sources4
Helixi96 – 105Combined sources10
Beta strandi108 – 110Combined sources3
Beta strandi112 – 116Combined sources5
Helixi119 – 123Combined sources5
Helixi127 – 135Combined sources9
Beta strandi139 – 145Combined sources7
Beta strandi151 – 154Combined sources4
Beta strandi160 – 165Combined sources6
Helixi172 – 180Combined sources9
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi188 – 194Combined sources7
Helixi199 – 211Combined sources13
Beta strandi217 – 219Combined sources3
Turni220 – 222Combined sources3
Beta strandi223 – 226Combined sources4
Beta strandi236 – 239Combined sources4
Helixi244 – 257Combined sources14
Beta strandi259 – 265Combined sources7
Helixi273 – 276Combined sources4
Helixi277 – 284Combined sources8
Beta strandi287 – 290Combined sources4
Beta strandi292 – 298Combined sources7
Beta strandi306 – 308Combined sources3
Turni313 – 315Combined sources3
Helixi316 – 322Combined sources7
Helixi323 – 325Combined sources3
Beta strandi326 – 328Combined sources3
Beta strandi330 – 334Combined sources5
Helixi336 – 340Combined sources5
Beta strandi341 – 343Combined sources3
Helixi345 – 355Combined sources11
Beta strandi359 – 362Combined sources4
Beta strandi364 – 370Combined sources7
Helixi386 – 393Combined sources8
Helixi394 – 397Combined sources4
Beta strandi398 – 400Combined sources3
Beta strandi402 – 406Combined sources5
Helixi407 – 412Combined sources6
Helixi417 – 424Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NVSX-ray1.02A1-426[»]
3TI2X-ray1.90A/B/C/D16-243[»]
ProteinModelPortaliQ9KRB0.
SMRiQ9KRB0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KRB0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 23Shikimate-3-phosphate bindingUniRule annotation1 Publication2
Regioni94 – 97PhosphoenolpyruvateUniRule annotation1 Publication4
Regioni170 – 172Shikimate-3-phosphate bindingUniRule annotation1 Publication3

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
KOiK00800.
OMAiMAFADCG.

Family and domain databases

CDDicd01556. EPSP_synthase. 1 hit.
Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth. 1 hit.
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.

Q9KRB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLTLQPIE LISGEVNLPG SKSVSNRALL LAALASGTTR LTNLLDSDDI
60 70 80 90 100
RHMLNALTKL GVNYRLSADK TTCEVEGLGQ AFHTTQPLEL FLGNAGTAMR
110 120 130 140 150
PLAAALCLGQ GDYVLTGEPR MKERPIGHLV DALRQAGAQI EYLEQENFPP
160 170 180 190 200
LRIQGTGLQA GTVTIDGSIS SQFLTAFLMS APLAQGKVTI KIVGELVSKP
210 220 230 240 250
YIDITLHIME QFGVQVINHD YQEFVIPAGQ SYVSPGQFLV EGDASSASYF
260 270 280 290 300
LAAAAIKGGE VKVTGIGKNS IQGDIQFADA LEKMGAQIEW GDDYVIARRG
310 320 330 340 350
ELNAVDLDFN HIPDAAMTIA TTALFAKGTT AIRNVYNWRV KETDRLAAMA
360 370 380 390 400
TELRKVGATV EEGEDFIVIT PPTKLIHAAI DTYDDHRMAM CFSLVALSDT
410 420
PVTINDPKCT SKTFPDYFDK FAQLSR
Length:426
Mass (Da):46,102
Last modified:October 1, 2000 - v1
Checksum:i38852D6483BFE1C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94882.1.
PIRiD82163.
RefSeqiNP_231368.1. NC_002505.1.
WP_000445261.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF94882; AAF94882; VC_1732.
GeneIDi2613737.
KEGGivch:VC1732.
PATRICi20082522. VBIVibCho83274_1657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94882.1.
PIRiD82163.
RefSeqiNP_231368.1. NC_002505.1.
WP_000445261.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NVSX-ray1.02A1-426[»]
3TI2X-ray1.90A/B/C/D16-243[»]
ProteinModelPortaliQ9KRB0.
SMRiQ9KRB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1732.

Protocols and materials databases

DNASUi2613737.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF94882; AAF94882; VC_1732.
GeneIDi2613737.
KEGGivch:VC1732.
PATRICi20082522. VBIVibCho83274_1657.

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
KOiK00800.
OMAiMAFADCG.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00089.
BioCyciVCHO:VC1732-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KRB0.

Family and domain databases

CDDicd01556. EPSP_synthase. 1 hit.
Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth. 1 hit.
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...

Entry informationi

Entry nameiAROA_VIBCH
AccessioniPrimary (citable) accession number: Q9KRB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 104 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.