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Protein

Chorismate synthase

Gene

aroC

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 4 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 (SP_1700), Phospho-2-dehydro-3-deoxyheptonate aldolase (SP_1701)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  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 sitei39NADPUniRule annotation1
Binding sitei45NADPUniRule annotation1
Binding sitei296FMN; via amide nitrogenUniRule annotation1 Publication1
Binding sitei337FMNUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi130 – 132FMNUniRule annotation3
Nucleotide bindingi251 – 252FMNUniRule annotation1 Publication2
Nucleotide bindingi311 – 315FMNUniRule annotation1 Publication5

GO - Molecular functioni

  • chorismate synthase activity Source: UniProtKB-EC
  • FMN binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
LigandFAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

UniPathwayiUPA00053; UER00090.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorismate synthaseUniRule annotation (EC:4.2.3.5UniRule annotation)
Short name:
CSUniRule annotation
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate phospholyaseUniRule annotation
Gene namesi
Name:aroCUniRule annotation
Ordered Locus Names:SP_1374
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001406551 – 388Chorismate synthaseAdd BLAST388

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Chemistry databases

BindingDBiP0A2Y6.

Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi11 – 19Combined sources9
Helixi29 – 40Combined sources12
Helixi48 – 51Combined sources4
Beta strandi57 – 63Combined sources7
Beta strandi72 – 77Combined sources6
Helixi79 – 84Combined sources6
Turni85 – 88Combined sources4
Helixi95 – 97Combined sources3
Turni98 – 101Combined sources4
Helixi112 – 119Combined sources8
Helixi125 – 131Combined sources7
Helixi133 – 135Combined sources3
Helixi136 – 152Combined sources17
Beta strandi156 – 164Combined sources9
Helixi177 – 185Combined sources9
Helixi194 – 196Combined sources3
Helixi197 – 209Combined sources13
Beta strandi216 – 224Combined sources9
Beta strandi232 – 234Combined sources3
Helixi235 – 237Combined sources3
Helixi239 – 248Combined sources10
Beta strandi253 – 258Combined sources6
Helixi261 – 266Combined sources6
Helixi269 – 271Combined sources3
Beta strandi276 – 279Combined sources4
Turni280 – 282Combined sources3
Beta strandi283 – 287Combined sources5
Turni290 – 293Combined sources4
Beta strandi304 – 310Combined sources7
Beta strandi320 – 323Combined sources4
Turni325 – 327Combined sources3
Beta strandi330 – 333Combined sources4
Helixi343 – 365Combined sources23
Helixi371 – 386Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QXOX-ray2.00A/B/C/D1-388[»]
ProteinModelPortaliP0A2Y6.
SMRiP0A2Y6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2Y6.

Family & Domainsi

Sequence similaritiesi

Belongs to the chorismate synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D10. Bacteria.
COG0082. LUCA.
HOGENOMiHOG000060334.
KOiK01736.
OMAiMLSINAV.

Family and domain databases

CDDicd07304. Chorismate_synthase. 1 hit.
Gene3Di3.60.150.10. 1 hit.
HAMAPiMF_00300. Chorismate_synth. 1 hit.
InterProiView protein in InterPro
IPR000453. Chorismate_synth.
IPR020541. Chorismate_synthase_CS.
PANTHERiPTHR21085. PTHR21085. 1 hit.
PfamiView protein in Pfam
PF01264. Chorismate_synt. 1 hit.
PIRSFiPIRSF001456. Chorismate_synth. 1 hit.
SUPFAMiSSF103263. SSF103263. 1 hit.
TIGRFAMsiTIGR00033. aroC. 1 hit.
PROSITEiView protein in PROSITE
PS00787. CHORISMATE_SYNTHASE_1. 1 hit.
PS00788. CHORISMATE_SYNTHASE_2. 1 hit.
PS00789. CHORISMATE_SYNTHASE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A2Y6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYLTAGESH GPRLTAIIEG IPAGLPLTAE DINEDLRRRQ GGYGRGGRMK
60 70 80 90 100
IENDQVVFTS GVRHGKTTGA PITMDVINKD HQKWLDIMSA EDIEDRLKSK
110 120 130 140 150
RKITHPRPGH ADLVGGIKYR FDDLRNSLER SSARETTMRV AVGAVAKRLL
160 170 180 190 200
AELDMEIANH VVVFGGKEID VPENLTVAEI KQRAAQSEVS IVNQEREQEI
210 220 230 240 250
KDYIDQIKRD GDTIGGVVET VVGGVPVGLG SYVQWDRKLD ARLAQAVVSI
260 270 280 290 300
NAFKGVEFGL GFEAGYRKGS QVMDEILWSK EDGYTRRTNN LGGFEGGMTN
310 320 330 340 350
GQPIVVRGVM KPIPTLYKPL MSVDIETHEP YKATVERSDP TALPAAGMVM
360 370 380
EAVVATVLAQ EILEKFSSDN LEELKEAVAK HRDYTKNY
Length:388
Mass (Da):42,872
Last modified:March 15, 2005 - v1
Checksum:i766565BDD9267D83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75472.1.
PIRiG95159.
RefSeqiWP_001269860.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75472; AAK75472; SP_1374.
KEGGispn:SP_1374.

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.

Entry informationi

Entry nameiAROC_STRPN
AccessioniPrimary (citable) accession number: P0A2Y6
Secondary accession number(s): Q97Q57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 5, 2017
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete 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