Q9BPL7 (ENO2_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase 2
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2
2-phosphoglycerate dehydratase 2

Gene names

Name:

ENO2

Organism

Toxoplasma gondii

Taxonomic identifier

5811 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Coccidia › Eucoccidiorida › Eimeriorina › Sarcocystidae › Toxoplasma

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence 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 tachyzoite 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 process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Enolase 2		PRO_0000134094
Regions
	Region	382 – 385	4	Substrate binding By similarity
Sites
	Active site	217	1	Proton donor By similarity
	Active site	355	1	Proton acceptor By similarity
	Metal binding	252	1	Magnesium By similarity
	Metal binding	303	1	Magnesium By similarity
	Metal binding	330	1	Magnesium By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	303	1	Substrate By similarity
	Binding site	330	1	Substrate By similarity
	Binding site	406	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9BPL7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 4029B1EA9024D1A1	FASTA	444	48,290
	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

References

[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, DEVELOPMENTAL STAGE. Strain: 76K.
[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. Strain: PLK.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF123457 mRNA. Translation: AAG60329.1. AY155668 Genomic DNA. Translation: AAP24057.1.
3D structure databases
ProteinModelPortal	Q9BPL7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
TIGRFAMs	TIGR01060. Eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO2_TOXGO

Accession

Primary (citable) accession number: Q9BPL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	June 1, 2001
Last modified:	October 19, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)