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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation1 Publication

Catalytic activityi

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation1 Publication

Pathwayi: chorismate biosynthesis

This protein is involved in step 6 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotationCurated
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (LH57_11870), Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
  2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ), 3-dehydroquinate dehydratase (aroQ)
  4. no protein annotated in this organism
  5. Shikimate kinase (aroK), Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC), 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 sitei28 – 281Shikimate-3-phosphateUniRule annotation1 Publication
Binding sitei124 – 1241PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei196 – 1961Shikimate-3-phosphateUniRule annotation1 Publication
Active sitei311 – 3111Proton acceptorUniRule annotation1 Publication
Binding sitei336 – 3361Shikimate-3-phosphate1 Publication
Binding sitei340 – 3401Shikimate-3-phosphate1 Publication
Active sitei341 – 3411Proton donorUniRule annotation
Binding sitei344 – 3441PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei385 – 3851PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei410 – 4101PhosphoenolpyruvateUniRule annotation1 Publication

GO - Molecular functioni

  • 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: MTBBASE

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.
UniPathwayiUPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferase1 PublicationUniRule annotation (EC:2.5.1.19UniRule annotation1 Publication)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase1 PublicationUniRule annotation
Short name:
EPSP synthase1 PublicationUniRule annotation
Short name:
EPSPS1 PublicationUniRule annotation
Gene namesi
Name:aroA1 PublicationUniRule annotation
Ordered Locus Names:Rv3227
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3227.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4504503-phosphoshikimate 1-carboxyvinyltransferasePRO_0000088273Add
BLAST

Proteomic databases

PaxDbiP9WPY5.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3227.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 174Combined sources
Helixi23 – 3816Combined sources
Beta strandi44 – 474Combined sources
Helixi53 – 6412Combined sources
Beta strandi68 – 703Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 805Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 10611Combined sources
Beta strandi109 – 1168Combined sources
Helixi119 – 1235Combined sources
Helixi127 – 1359Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi158 – 1625Combined sources
Turni164 – 1674Combined sources
Helixi169 – 1779Combined sources
Helixi178 – 1803Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi185 – 1895Combined sources
Helixi197 – 20913Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi233 – 2353Combined sources
Helixi240 – 25314Combined sources
Beta strandi256 – 2594Combined sources
Helixi270 – 27910Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi303 – 3053Combined sources
Helixi310 – 3123Combined sources
Helixi313 – 3219Combined sources
Beta strandi328 – 3336Combined sources
Helixi335 – 3395Combined sources
Beta strandi340 – 3423Combined sources
Helixi344 – 35411Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi376 – 3783Combined sources
Helixi384 – 39411Combined sources
Beta strandi400 – 4034Combined sources
Helixi405 – 4106Combined sources
Helixi415 – 4239Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJBX-ray1.80A1-450[»]
2O0BX-ray1.15A1-450[»]
2O0DX-ray1.60A1-450[»]
2O0EX-ray1.81A1-450[»]
2O0XX-ray1.96A1-450[»]
2O0ZX-ray2.00A1-450[»]
2O15X-ray1.95A1-450[»]
ProteinModelPortaliP9WPY5.
SMRiP9WPY5. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 242Shikimate-3-phosphate bindingUniRule annotation1 Publication
Regioni94 – 974Phosphoenolpyruvate bindingUniRule annotation1 Publication
Regioni167 – 1693Shikimate-3-phosphate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
KOiK00800.
OMAiCPDLAQT.
PhylomeDBiP9WPY5.

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.

P9WPY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTWPAPTAP TPVRATVTVP GSKSQTNRAL VLAALAAAQG RGASTISGAL
60 70 80 90 100
RSRDTELMLD ALQTLGLRVD GVGSELTVSG RIEPGPGARV DCGLAGTVLR
110 120 130 140 150
FVPPLAALGS VPVTFDGDQQ ARGRPIAPLL DALRELGVAV DGTGLPFRVR
160 170 180 190 200
GNGSLAGGTV AIDASASSQF VSGLLLSAAS FTDGLTVQHT GSSLPSAPHI
210 220 230 240 250
AMTAAMLRQA GVDIDDSTPN RWQVRPGPVA ARRWDIEPDL TNAVAFLSAA
260 270 280 290 300
VVSGGTVRIT GWPRVSVQPA DHILAILRQL NAVVIHADSS LEVRGPTGYD
310 320 330 340 350
GFDVDLRAVG ELTPSVAALA ALASPGSVSR LSGIAHLRGH ETDRLAALST
360 370 380 390 400
EINRLGGTCR ETPDGLVITA TPLRPGIWRA YADHRMAMAG AIIGLRVAGV
410 420 430 440 450
EVDDIAATTK TLPEFPRLWA EMVGPGQGWG YPQPRSGQRA RRATGQGSGG
Length:450
Mass (Da):46,426
Last modified:April 16, 2014 - v1
Checksum:i27BB86F9412A07D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52269 Genomic DNA. Translation: CAA36510.1.
M62708 Genomic DNA. Translation: AAA25356.1.
AL123456 Genomic DNA. Translation: CCP46046.1.
PIRiE70590.
RefSeqiNP_217744.1. NC_000962.3.
WP_003416914.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP46046; CCP46046; Rv3227.
GeneIDi888753.
KEGGimtu:Rv3227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52269 Genomic DNA. Translation: CAA36510.1.
M62708 Genomic DNA. Translation: AAA25356.1.
AL123456 Genomic DNA. Translation: CCP46046.1.
PIRiE70590.
RefSeqiNP_217744.1. NC_000962.3.
WP_003416914.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJBX-ray1.80A1-450[»]
2O0BX-ray1.15A1-450[»]
2O0DX-ray1.60A1-450[»]
2O0EX-ray1.81A1-450[»]
2O0XX-ray1.96A1-450[»]
2O0ZX-ray2.00A1-450[»]
2O15X-ray1.95A1-450[»]
ProteinModelPortaliP9WPY5.
SMRiP9WPY5. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3227.

Proteomic databases

PaxDbiP9WPY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46046; CCP46046; Rv3227.
GeneIDi888753.
KEGGimtu:Rv3227.

Organism-specific databases

TubercuListiRv3227.

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
KOiK00800.
OMAiCPDLAQT.
PhylomeDBiP9WPY5.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00089.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

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. "Cloning and characterization of the aroA gene from Mycobacterium tuberculosis."
    Garbe T., Jones C., Charles I.G., Dougan G., Young D.
    J. Bacteriol. 172:6774-6782(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis."
    Oliveira J.S., Pinto C.A., Basso L.A., Santos D.S.
    Protein Expr. Purif. 22:430-435(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  5. "Mycobacterium tuberculosis EPSP synthase in unliganded state."
    Bourenkov G.P., Kachalova G.S., Strizhov N., Bruning M., Vagin A., Bartunik H.D.
    Submitted (FEB-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  6. "Complex of 3-phosphoshikimate 1-carboxyvinyltransferase with S3P."
    Kachalova G.S., Burenkov G.P., Strizhov N.I., Brunning M.G., Bartunik H.D.
    Submitted (NOV-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE, ACTIVE SITE.

Entry informationi

Entry nameiAROA_MYCTU
AccessioniPrimary (citable) accession number: P9WPY5
Secondary accession number(s): L0TDI9, P22487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 17, 2016
This is version 18 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: 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.