[1]	NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. DOI=10.1074/jbc.274.35.24888; PubMed=10455162 [NCBI, ExPASy, EBI, Israel, Japan] Dzierszinski F., Popescu O., Toursel C., Slomianny C., Yahiaoui B., Tomavo S.; "The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes. Implications for evolutionary origin of apicomplexans."; J. Biol. Chem. 274:24888-24895(1999).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PLK; Kibe M., Tomavo S.; "Toxoplasma gondii enolases ENO1 and ENO2 loci."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION. 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).

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 bradyzoite 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

AF051910; AAD51128.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY155668; AAP24058.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9NDH8; 1OEP. [HSSP ENTRY / PDB]

ModBase

Q9UAE6.

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.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 444`	`444`	`Enolase 1.`	`PRO_0000134093`
`REGION`	`382 385`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`217 217`		`Proton donor (By similarity).`
`ACT_SITE`	`355 355`		`Proton acceptor (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: 48341 Da [This is the MW of the unprocessed precursor]

CRC64: 667B3558B5B3D768 [This is a checksum on the sequence]

        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

Q9UAE6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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