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Reviewed, UniProtKB/Swiss-Prot Q9UAE6 (ENO1_TOXGO)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1
Gene names
Name: ENO1
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Developmental stage

Expressed preferentially in the bradyzoite stage. Ref.1

Miscellaneous

While ENO1 and ENO2 display similar K(m) values, the pure tachyzoite-specific enzyme (ENO2) has a threefold specific activity at V(max) compared with that of the bradyzoite-specific enolase (ENO1).

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionLyase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Enolase 1
PRO_0000134093

Regions

Region382 – 3854Substrate binding By similarity

Sites

Active site2171Proton donor By similarity
Active site3551Proton acceptor By similarity
Binding site1651Substrate By similarity
Binding site1741Substrate By similarity
Binding site3031Substrate By similarity
Binding site3301Substrate By similarity
Binding site4061Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UAE6-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 667B3558B5B3D768

FASTA44448,341
        10         20         30         40         50         60 
MVVIKDIVAR EILDSRGNPT IEVDVSTEGG VFRAAVPSGA STGIYEALEL RDKDPKRYLG 

        70         80         90        100        110        120 
KGVLNAVEIV RQEIKPALLG KDPCDQKGID MLMVEQLDGT KNEWGYSKSK LGANAILGVS 

       130        140        150        160        170        180 
IACCRAGAAS KGLPLYKYIA TLAGKTIDKM VMPVPFFNVI NGGEHAGNGL ALQEFLIAPV 

       190        200        210        220        230        240 
GAPNIREAIR YGSETYHHLK NVIKNKYGLD ATNVGDEGGF APNVATAEEA LNLLVEAIKA 

       250        260        270        280        290        300 
AGYEGKIKIA FDAAASEFYK QDEKKYDLDY KCKTKNASKH LTGEKLKEVY EGWLKKYPII 

       310        320        330        340        350        360 
SVEDPFDQDD FASFSAFTKD VGEKTQVIGD DILVTNILRI EKALKDKACN CLLLKVNQIG 

       370        380        390        400        410        420 
SVTEAIEACL LAQKSGWGVQ VSHRSGETED SFIADLVVGL RCGQIKSGSP CRSERLCKYN 

       430        440 
QLMRIEESLG ADCVYAGESF RHPK 

« Hide

References

[1]"The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes. Implications for evolutionary origin of apicomplexans."
Dzierszinski F., Popescu O., Toursel C., Slomianny C., Yahiaoui B., Tomavo S.
J. Biol. Chem. 274:24888-24895(1999) [PubMed: 10455162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[2]"Toxoplasma gondii enolases ENO1 and ENO2 loci."
Kibe M., Tomavo S.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PLK.
[3]"Differential expression of two plant-like enolases with distinct enzymatic and antigenic properties during stage conversion of the protozoan parasite Toxoplasma gondii."
Dzierszinski F., Mortuaire M., Dendouga N., Popescu O., Tomavo S.
J. Mol. Biol. 309:1017-1027(2001) [PubMed: 11399076] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

AF051910 mRNA. Translation: AAD51128.1.
AY155668 Genomic DNA. Translation: AAP24058.1.

3D structure databases

HSSPHSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.2.1.11. 262552.

Family and domain databases

InterProIPR000941. Enolase.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
ProDomPD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO1_TOXGO
AccessionPrimary (citable) accession number: Q9UAE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents