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Protein

Chorismate synthase

Gene

aroC

Organism
Escherichia coli (strain K12)
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. It uses NADPH to reduce FMN.UniRule annotation6 Publications

Catalytic activityi

5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate.UniRule annotation5 Publications

Cofactori

FMNH2UniRule annotation6 PublicationsNote: Reduced FMN (FMNH(2)). It can also use FAD, however FMN is the preferred cofactor.UniRule annotation6 Publications

Enzyme regulationi

Competitively inhibited by 6R-6-fluoro-EPSP.2 Publications

Kineticsi

kcat is 16.5 sec(-1) for phospholyase activity with EPSP as substrate. kcat is 27 sec(-1) for phospholyase activity with EPSP as substrate.2 Publications

  1. KM=1.3 µM for EPSP1 Publication
  1. Vmax=25 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is between 7.5 and 8.1 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, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (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 sitei48 – 481NADPUniRule annotation
Binding sitei54 – 541NADPUniRule annotation
Binding sitei278 – 2781FMN; via amide nitrogenUniRule annotation
Binding sitei319 – 3191FMNUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi125 – 1273FMNUniRule annotation
Nucleotide bindingi238 – 2392FMNUniRule annotation
Nucleotide bindingi293 – 2975FMNUniRule annotation

GO - Molecular functioni

  • chorismate synthase activity Source: EcoCyc
  • FMN binding Source: UniProtKB
  • identical protein binding Source: EcoCyc

GO - Biological processi

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

BioCyciEcoCyc:AROC-MONOMER.
ECOL316407:JW2326-MONOMER.
MetaCyc:AROC-MONOMER.
UniPathwayiUPA00053; UER00090.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorismate synthase1 PublicationUniRule annotation (EC:4.2.3.5UniRule annotation5 Publications)
Short name:
CSUniRule annotation
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate phospholyase1 PublicationUniRule annotation
Short name:
EPSP phospholyase1 Publication
Gene namesi
Name:aroC1 PublicationUniRule annotation
Ordered Locus Names:b2329, JW2326
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10075. aroC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 361360Chorismate synthasePRO_0000140584Add
BLAST

Proteomic databases

EPDiP12008.
PaxDbiP12008.
PRIDEiP12008.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263044. 26 interactions.
IntActiP12008. 5 interactions.
STRINGi511145.b2329.

Structurei

3D structure databases

ProteinModelPortaliP12008.
SMRiP12008. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chorismate synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105D10. Bacteria.
COG0082. LUCA.
HOGENOMiHOG000060335.
InParanoidiP12008.
KOiK01736.
OMAiMLSINAV.
OrthoDBiEOG6WDSHT.
PhylomeDBiP12008.

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. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNTIGQLF RVTTFGESHG LALGCIVDGV PPGIPLTEAD LQHDLDRRRP
60 70 80 90 100
GTSRYTTQRR EPDQVKILSG VFEGVTTGTS IGLLIENTDQ RSQDYSAIKD
110 120 130 140 150
VFRPGHADYT YEQKYGLRDY RGGGRSSARE TAMRVAAGAI AKKYLAEKFG
160 170 180 190 200
IEIRGCLTQM GDIPLDIKDW SQVEQNPFFC PDPDKIDALD ELMRALKKEG
210 220 230 240 250
DSIGAKVTVV ASGVPAGLGE PVFDRLDADI AHALMSINAV KGVEIGDGFD
260 270 280 290 300
VVALRGSQNR DEITKDGFQS NHAGGILGGI SSGQQIIAHM ALKPTSSITV
310 320 330 340 350
PGRTINRFGE EVEMITKGRH DPCVGIRAVP IAEAMLAIVL MDHLLRQRAQ
360
NADVKTDIPR W
Length:361
Mass (Da):39,137
Last modified:January 23, 2007 - v4
Checksum:i47C85F91B87DF093
GO

Sequence cautioni

The sequence AAA23488.1 differs from that shown. Reason: Frameshift at position 335. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27714 Genomic DNA. Translation: AAA23487.1.
Y00720 Genomic DNA. Translation: CAA68707.1. Frameshift.
M33021 Genomic DNA. Translation: AAA23488.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75389.1.
AP009048 Genomic DNA. Translation: BAA16185.1.
PIRiG65005. SYECKR.
RefSeqiNP_416832.1. NC_000913.3.
WP_001333535.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75389; AAC75389; b2329.
BAA16185; BAA16185; BAA16185.
GeneIDi946814.
KEGGiecj:JW2326.
eco:b2329.
PATRICi32120031. VBIEscCol129921_2425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27714 Genomic DNA. Translation: AAA23487.1.
Y00720 Genomic DNA. Translation: CAA68707.1. Frameshift.
M33021 Genomic DNA. Translation: AAA23488.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75389.1.
AP009048 Genomic DNA. Translation: BAA16185.1.
PIRiG65005. SYECKR.
RefSeqiNP_416832.1. NC_000913.3.
WP_001333535.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP12008.
SMRiP12008. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263044. 26 interactions.
IntActiP12008. 5 interactions.
STRINGi511145.b2329.

Proteomic databases

EPDiP12008.
PaxDbiP12008.
PRIDEiP12008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75389; AAC75389; b2329.
BAA16185; BAA16185; BAA16185.
GeneIDi946814.
KEGGiecj:JW2326.
eco:b2329.
PATRICi32120031. VBIEscCol129921_2425.

Organism-specific databases

EchoBASEiEB0073.
EcoGeneiEG10075. aroC.

Phylogenomic databases

eggNOGiENOG4105D10. Bacteria.
COG0082. LUCA.
HOGENOMiHOG000060335.
InParanoidiP12008.
KOiK01736.
OMAiMLSINAV.
OrthoDBiEOG6WDSHT.
PhylomeDBiP12008.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00090.
BioCyciEcoCyc:AROC-MONOMER.
ECOL316407:JW2326-MONOMER.
MetaCyc:AROC-MONOMER.

Miscellaneous databases

PROiP12008.

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. 1 hit.
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. "Isolation, characterization and nucleotide sequences of the aroC genes encoding chorismate synthase from Salmonella typhi and Escherichia coli."
    Charles I.G., Lamb H.K., Pickard D., Dougan G., Hawkins A.R.
    J. Gen. Microbiol. 136:353-358(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The overexpression, purification and complete amino acid sequence of chorismate synthase from Escherichia coli K12 and its comparison with the enzyme from Neurospora crassa."
    White P.J., Millar G., Coggins J.R.
    Biochem. J. 251:313-322(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, FUNCTION, COFACTOR, SUBUNIT.
    Strain: K12.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "A continuous, anaerobic spectrophotometric assay for chorismate synthase activity that utilizes photoreduced flavin mononucleotide."
    Ramjee M.K., Coggins J.R., Thorneley R.N.
    Anal. Biochem. 220:137-141(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect under single-turnover and steady-state conditions shows that a flavin intermediate forms before the C-(6proR)-H bond is cleaved."
    Bornemann S., Balasubramanian S., Coggins J.R., Abell C., Lowe D.J., Thorneley R.N.
    Biochem. J. 305:707-710(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  8. "The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate."
    Bornemann S., Lowe D.J., Thorneley R.N.
    Biochemistry 35:9907-9916(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  9. "Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase."
    Macheroux P., Bornemann S., Ghisla S., Thorneley R.N.
    J. Biol. Chem. 271:25850-25858(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  10. "Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding."
    Macheroux P., Schoenbrunn E., Svergun D.I., Volkov V.V., Koch M.H., Bornemann S., Thorneley R.N.
    Biochem. J. 335:319-327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, SUBUNIT.
  11. "A secondary beta deuterium kinetic isotope effect in the chorismate synthase reaction."
    Bornemann S., Theoclitou M.E., Brune M., Webb M.R., Thorneley R.N., Abell C.
    Bioorg. Chem. 28:191-204(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, REACTION MECHANISM.
  12. "Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction."
    Osborne A., Thorneley R.N., Abell C., Bornemann S.
    J. Biol. Chem. 275:35825-35830(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, REACTION MECHANISM.

Entry informationi

Entry nameiAROC_ECOLI
AccessioniPrimary (citable) accession number: P12008
Secondary accession number(s): P78193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.