Q9LEJ0 (ENO1_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase 1
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
Allergen=Hev b 9

Gene names

Name:

ENO1

Organism

Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)

Taxonomic identifier

3981 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Crotonoideae › Micrandreae › Hevea

Protein attributes

Sequence length	445 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.
Allergenic properties	Causes an allergic reaction in human. Involved in latex allergic reactions. Ref.1
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Disease	Allergen
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 445	445	Enolase 1		PRO_0000134069
Regions
	Region	380 – 383	4	Substrate binding By similarity
Sites
	Active site	216	1	Proton donor By similarity
	Active site	353	1	Proton acceptor By similarity
	Metal binding	251	1	Magnesium By similarity
	Metal binding	301	1	Magnesium By similarity
	Metal binding	328	1	Magnesium By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity
	Binding site	328	1	Substrate By similarity
	Binding site	404	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LEJ0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 238883FB249F5544	FASTA	445	47,830
	10 20 30 40 50 60 MAITIVSVRA RQIFDSRGNP TVEADVKLSD GYLARAAVPS GASTGIYEAL ELRDGGSDYL 70 80 90 100 110 120 GKGVSKAVEN VNIIIGPALV GKDPTDQVGI DNFMVQQLDG TVNEWGWCKQ KLGANAILAV 130 140 150 160 170 180 SLAVCKAGAH VKGIPLYEHI ANLAGNKNLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG 190 200 210 220 230 240 ASSFKEAMKM GAEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIAKA 250 260 270 280 290 300 GYTGKVVIGM DVAASEFYGS DQTYDLNFKE ENNNGSQKIS GEALKDLYKS FVAEYPIVSI 310 320 330 340 350 360 EDPFDQDDWA HYAKLTSEIG EKVQIVGDDL LVTNPKRVEK AIKEKACNAL LLKVNQIGSV 370 380 390 400 410 420 TESIEAVKMS KRAGWGVMAS HRSGETEDTF IADLSVGLAT GQIKTGAPCR SERLAKYNQL 430 440 LRIEEELGSE AVYAGANFRK PVEPY

References

[1]

"Hev b 9, an enolase and a new cross-reactive allergen from hevea latex and molds. Purification, characterization, cloning and expression." Wagner S., Breiteneder H., Simon-Nobbe B., Susani M., Krebitz M., Niggemann B., Brehler R., Scheiner O., Hoffmann-Sommergruber K. Eur. J. Biochem. 267:7006-7014(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN. Tissue: Latex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132580 mRNA. Translation: CAC00532.1.
3D structure databases
ProteinModelPortal	Q9LEJ0.
SMR	Q9LEJ0. Positions 4-442.
ModBase	Search...
Protein family/group databases
Allergome	3317. Hev b 9.0101. 404. Hev b 9.
Proteomic databases
PRIDE	Q9LEJ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12858.
BRENDA	4.2.1.11. 2665.
UniPathway	UPA00109; UER00187.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 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

ENO1_HEVBR

Accession

Primary (citable) accession number: Q9LEJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program