NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND DEVELOPMENTAL STAGE.
STRAIN=76K;
DOI=10.1006/jmbi.2001.4730; PubMed=11399076 [NCBI, ExPASy, EBI, Israel, Japan]
Dzierszinski F., Mortuaire M., Dendouga N., Popescu O., Tomavo S.;
"Differential expression of two plant-like enolases with distinct enzymatic and antigenic properties during stage conversion of the protozoan parasite Toxoplasma gondii.";
J. Mol. Biol. 309:1017-1027(2001).

[2]

NUCLEOTIDE SEQUENCE.
STRAIN=PLK;
Kibe M., Tomavo S.;
"Toxoplasma gondii enolases ENO1 and ENO2 loci.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.

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: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
DEVELOPMENTAL STAGE: Expressed preferentially in the tachyzoite stage.
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).
SIMILARITY: Belongs to the enolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF123457; AAG60329.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY155668; AAP24057.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P56252; 1PDZ. [HSSP ENTRY / PDB]

ModBase

Q9BPL7.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000941; Enolase.
Graphical view of domain structure.

PANTHER

PTHR11902; Enolase; 1.

Pfam

PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001400; Enolase; 1.

PRINTS

PR00148; ENOLASE.

ProDom

PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 444`	`444`	`Enolase 2.`	`PRO_0000134094`
`REGION`	`382 385`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`217 217`		`Proton donor (By similarity).`
`ACT_SITE`	`355 355`		`Proton acceptor (By similarity).`
`METAL`	`252 252`		`Magnesium (By similarity).`
`METAL`	`303 303`		`Magnesium (By similarity).`
`METAL`	`330 330`		`Magnesium (By similarity).`
`BINDING`	`165 165`		`Substrate (By similarity).`
`BINDING`	`174 174`		`Substrate (By similarity).`
`BINDING`	`303 303`		`Substrate (By similarity).`
`BINDING`	`330 330`		`Substrate (By similarity).`
`BINDING`	`406 406`		`Substrate (By similarity).`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 48290 Da [This is the MW of the unprocessed precursor]

CRC64: 4029B1EA9024D1A1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVAIKDITAR QILDSRGNPT VEVDLLTDGG CFRAAVPSGA STGIYEALEL RDKDQTKFMG 

        70         80         90        100        110        120 
KGVMKAVENI HKIIKPALIG KDPCDQKGID KLMVEELDGT KNEWGWCKSK LGANAILAVS 

       130        140        150        160        170        180 
MACCRAGAAA KGMPLYKYIA TLAGNPTDKM VMPVPFFNVI NGGSHAGNKV AMQEFMIAPV 

       190        200        210        220        230        240 
GASTIQEAIQ IGAEVYQHLK VVIKKKYGLD ATNVGDEGGF APNISGATEA LDLLMEAIKV 

       250        260        270        280        290        300 
SGHEGKVKIA ADVAASEFFL QDDKVYDLDF KTPNNDKSQR KTGEELRNLY KDLCQKYPFV 

       310        320        330        340        350        360 
SIEDPFDQDD FHSYAQLTNE VGEKVQIVGD DLLVTNPTRI EKAVQEKACN GLLLKVNQIG 

       370        380        390        400        410        420 
TVSESIEACQ LAQKNKWGVM VSHRSGETED SFIADLVVGL RTGQIKTGAP CRSERLCKYN 

       430        440 
QLMRIEESLG SDCQYAGAGF RHPN

Q9BPL7 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools