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Protein

Chorismate synthase

Gene

aroC

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 anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.UniRule annotation

Catalytic activityi

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

Cofactori

FMNH2UniRule annotation1 PublicationNote: Reduced FMN (FMNH(2)).UniRule annotation1 Publication

Pathwayi: chorismate biosynthesis

This protein is involved in step 7 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 AroG (aroG)
  2. 3-dehydroquinate synthase (LH57_13905), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ)
  4. no protein annotated in this organism
  5. Shikimate kinase (aroK), Shikimate kinase (LH57_13910)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (LH57_17660)
  7. Chorismate synthase (aroC), Chorismate synthase (LH57_13915)
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 sitei40 – 401NADPUniRule annotation1 Publication
Binding sitei46 – 461NADPUniRule annotation1 Publication
Binding sitei300 – 3001FMN; via amide nitrogenUniRule annotation
Binding sitei341 – 3411FMNUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi135 – 1373FMNUniRule annotation
Nucleotide bindingi256 – 2572FMNUniRule annotation1 Publication
Nucleotide bindingi315 – 3195FMNUniRule annotation1 Publication

GO - Molecular functioni

  • chorismate synthase activity Source: MTBBASE
  • FMN binding Source: MTBBASE
  • NAD binding Source: MTBBASE
  • oxidoreductase activity, acting on NAD(P)H Source: MTBBASE

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  • chorismate biosynthetic process Source: Reactome
  • growth Source: MTBBASE
  • oxidation-reduction process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.
UniPathwayiUPA00053; UER00090.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorismate synthaseUniRule annotation (EC:4.2.3.5UniRule annotation)
Short name:
CS1 PublicationUniRule annotation
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate phospholyaseUniRule annotation
Gene namesi
Name:aroCUniRule annotation
Synonyms:aroF
Ordered Locus Names:Rv2540c
ORF Names:MTCY159.16
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2540c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Chorismate synthasePRO_0000140615Add
BLAST

Proteomic databases

PaxDbiP9WPY1.

Interactioni

Subunit structurei

Homotetramer: dimer of dimers.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2540c.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi12 – 2110Combined sources
Beta strandi24 – 274Combined sources
Helixi30 – 4011Combined sources
Helixi46 – 483Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 648Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 786Combined sources
Helixi82 – 854Combined sources
Turni86 – 894Combined sources
Helixi96 – 1005Combined sources
Helixi103 – 1053Combined sources
Helixi117 – 1248Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 1367Combined sources
Helixi138 – 1403Combined sources
Helixi141 – 15919Combined sources
Beta strandi162 – 1709Combined sources
Helixi183 – 1853Combined sources
Helixi186 – 1916Combined sources
Beta strandi196 – 1983Combined sources
Helixi199 – 21517Combined sources
Beta strandi221 – 2299Combined sources
Beta strandi237 – 2393Combined sources
Helixi240 – 2423Combined sources
Helixi244 – 25310Combined sources
Beta strandi258 – 2636Combined sources
Helixi266 – 2694Combined sources
Helixi274 – 2774Combined sources
Beta strandi289 – 2913Combined sources
Turni294 – 2974Combined sources
Beta strandi308 – 3147Combined sources
Turni321 – 3233Combined sources
Beta strandi325 – 3273Combined sources
Turni329 – 3313Combined sources
Beta strandi334 – 3363Combined sources
Helixi347 – 37024Combined sources
Helixi375 – 39016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZTBX-ray2.65A1-401[»]
2G85X-ray2.22A1-401[»]
2O11X-ray1.65A1-401[»]
2O12X-ray1.72A1-401[»]
2QHFX-ray1.65A1-401[»]
4BAIX-ray2.30A1-401[»]
4BAJX-ray2.30A1-401[»]
ProteinModelPortaliP9WPY1.
SMRiP9WPY1. Positions 1-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chorismate synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D10. Bacteria.
COG0082. LUCA.
KOiK01736.
OMAiMLSINAV.
PhylomeDBiP9WPY1.

Family and domain databases

Gene3Di3.60.150.10. 1 hit.
HAMAPiMF_00300. Chorismate_synth.
InterProiIPR000453. Chorismate_synth.
IPR020541. Chorismate_synthase_CS.
[Graphical view]
PANTHERiPTHR21085. PTHR21085. 2 hits.
PfamiPF01264. Chorismate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001456. Chorismate_synth. 1 hit.
SUPFAMiSSF103263. SSF103263. 1 hit.
TIGRFAMsiTIGR00033. aroC. 1 hit.
PROSITEiPS00787. CHORISMATE_SYNTHASE_1. 1 hit.
PS00788. CHORISMATE_SYNTHASE_2. 1 hit.
PS00789. CHORISMATE_SYNTHASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WPY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRWITAGES HGRALVAVVE GMVAGVHVTS ADIADQLARR RLGYGRGARM
60 70 80 90 100
TFERDAVTVL SGIRHGSTLG GPIAIEIGNT EWPKWETVMA ADPVDPAELA
110 120 130 140 150
DVARNAPLTR PRPGHADYAG MLKYGFDDAR PVLERASARE TAARVAAGTV
160 170 180 190 200
ARAFLRQALG VEVLSHVISI GASAPYEGPP PRAEDLPAID ASPVRAYDKA
210 220 230 240 250
AEADMIAQIE AAKKDGDTLG GVVEAVALGL PVGLGSFTSG DHRLDSQLAA
260 270 280 290 300
AVMGIQAIKG VEIGDGFQTA RRRGSRAHDE MYPGPDGVVR STNRAGGLEG
310 320 330 340 350
GMTNGQPLRV RAAMKPISTV PRALATVDLA TGDEAVAIHQ RSDVCAVPAA
360 370 380 390 400
GVVVETMVAL VLARAALEKF GGDSLAETQR NIAAYQRSVA DREAPAARVS

G
Length:401
Mass (Da):41,792
Last modified:April 16, 2014 - v1
Checksum:i6A3C14761261ADEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45335.1.
PIRiH70658.
RefSeqiNP_217056.1. NC_000962.3.
WP_003413027.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45335; CCP45335; Rv2540c.
GeneIDi887379.
KEGGimtu:Rv2540c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45335.1.
PIRiH70658.
RefSeqiNP_217056.1. NC_000962.3.
WP_003413027.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZTBX-ray2.65A1-401[»]
2G85X-ray2.22A1-401[»]
2O11X-ray1.65A1-401[»]
2O12X-ray1.72A1-401[»]
2QHFX-ray1.65A1-401[»]
4BAIX-ray2.30A1-401[»]
4BAJX-ray2.30A1-401[»]
ProteinModelPortaliP9WPY1.
SMRiP9WPY1. Positions 1-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2540c.

Proteomic databases

PaxDbiP9WPY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45335; CCP45335; Rv2540c.
GeneIDi887379.
KEGGimtu:Rv2540c.

Organism-specific databases

TubercuListiRv2540c.

Phylogenomic databases

eggNOGiENOG4105D10. Bacteria.
COG0082. LUCA.
KOiK01736.
OMAiMLSINAV.
PhylomeDBiP9WPY1.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00090.
ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

Family and domain databases

Gene3Di3.60.150.10. 1 hit.
HAMAPiMF_00300. Chorismate_synth.
InterProiIPR000453. Chorismate_synth.
IPR020541. Chorismate_synthase_CS.
[Graphical view]
PANTHERiPTHR21085. PTHR21085. 2 hits.
PfamiPF01264. Chorismate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001456. Chorismate_synth. 1 hit.
SUPFAMiSSF103263. SSF103263. 1 hit.
TIGRFAMsiTIGR00033. aroC. 1 hit.
PROSITEiPS00787. CHORISMATE_SYNTHASE_1. 1 hit.
PS00788. CHORISMATE_SYNTHASE_2. 1 hit.
PS00789. CHORISMATE_SYNTHASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), SUBUNIT.
  5. "Crystal structure of chorismate synthase from mycobacterium tuberculosis at 2.22 angstrons of resolution."
    Dias M.V.B., Dos Santos B.B., Ely F., Basso L.A., Santos D.S., de Azevedo W.F. Jr.
    Submitted (MAR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS).
  6. "Mycobacterium tuberculosis chorismate synthase in complex with NCA and FMN."
    Bruning M., Bourenkov G.P., Strizhov N.I., Bartunik H.D.
    Submitted (JUL-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NADP ANALOG; FMN, COFACTOR.
  7. "In-house UV radiation-damage-induced phasing of selenomethionine-labeled protein structures."
    Pereira P.J., Royant A., Panjikar S., de Sanctis D.
    J. Struct. Biol. 181:89-94(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Entry informationi

Entry nameiAROC_MYCTU
AccessioniPrimary (citable) accession number: P9WPY1
Secondary accession number(s): L0T9X6, P63611, P95013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 11, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.

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.