Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271Shikimate-3-phosphateUniRule annotation1 Publication
Binding sitei124 – 1241PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei198 – 1981Shikimate-3-phosphateUniRule annotation1 Publication
Active sitei314 – 3141Proton acceptorUniRule annotation1 Publication
Binding sitei337 – 3371Shikimate-3-phosphateUniRule annotation1 Publication
Binding sitei341 – 3411Shikimate-3-phosphateUniRule annotation1 Publication
Active sitei342 – 3421Proton donorUniRule annotation1 Publication
Binding sitei345 – 3451PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei387 – 3871PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei412 – 4121PhosphoenolpyruvateUniRule annotation

GO - Molecular functioni

  • 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: TIGR

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  • chorismate biosynthetic process Source: TIGR
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4264263-phosphoshikimate 1-carboxyvinyltransferasePRO_0000088314Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243277.VC1732.

Structurei

Secondary structure

1
426
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi14 – 174Combined sources
Helixi22 – 3413Combined sources
Beta strandi35 – 439Combined sources
Helixi48 – 5912Combined sources
Beta strandi63 – 664Combined sources
Beta strandi73 – 764Combined sources
Beta strandi88 – 914Combined sources
Helixi96 – 10510Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi112 – 1165Combined sources
Helixi119 – 1235Combined sources
Helixi127 – 1359Combined sources
Beta strandi139 – 1457Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi160 – 1656Combined sources
Helixi172 – 1809Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 1947Combined sources
Helixi199 – 21113Combined sources
Beta strandi217 – 2193Combined sources
Turni220 – 2223Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi236 – 2394Combined sources
Helixi244 – 25714Combined sources
Beta strandi259 – 2657Combined sources
Helixi273 – 2764Combined sources
Helixi277 – 2848Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi292 – 2987Combined sources
Beta strandi306 – 3083Combined sources
Turni313 – 3153Combined sources
Helixi316 – 3227Combined sources
Helixi323 – 3253Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi330 – 3345Combined sources
Helixi336 – 3405Combined sources
Beta strandi341 – 3433Combined sources
Helixi345 – 35511Combined sources
Beta strandi359 – 3624Combined sources
Beta strandi364 – 3707Combined sources
Helixi386 – 3938Combined sources
Helixi394 – 3974Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi402 – 4065Combined sources
Helixi407 – 4126Combined sources
Helixi417 – 4248Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NVSX-ray1.02A1-426[»]
3TI2X-ray1.90A/B/C/D16-243[»]
ProteinModelPortaliQ9KRB0.
SMRiQ9KRB0. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KRB0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232Shikimate-3-phosphate bindingUniRule annotation1 Publication
Regioni94 – 974PhosphoenolpyruvateUniRule annotation1 Publication
Regioni170 – 1723Shikimate-3-phosphate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3NVSX-ray1.02A1-426[»]
3TI2X-ray1.90A/B/C/D16-243[»]
ProteinModelPortaliQ9KRB0.
SMRiQ9KRB0. Positions 1-426.
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

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: September 7, 2016
This is version 101 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.