Reviewed, UniProtKB/Swiss-Prot Q9HDT3 (ENO_ALTAL)

Names and origin

Protein names

Recommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase
    Allergen Alt a 5
    Allergen Alt a 11
    Allergen Alt a XI
    Allergen=Alt a 6

Gene names

Name:	ENO
Synonyms:	ALTA11, ALTA6

Organism

Alternaria alternata (Alternaria rot fungus)

Taxonomic identifier

5599 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporaceae › mitosporic Pleosporaceae › Alternaria › Alternaria alternata group

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Allergenic properties	Causes an allergic reaction in human. Binds to IgE. Ref.1 Ref.2
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-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Enolase		PRO_0000134039
Regions
	Region	374 – 377	4	Substrate binding By similarity
Sites
	Active site	211	1	Proton donor By similarity
	Active site	347	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	297	1	Magnesium By similarity
	Metal binding	322	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	297	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Binding site	398	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDT3-1 [UniParc]. Last modified June 20, 2001. Version 2. Checksum: D60900100A72AF83	FASTA	438	47,205
	10 20 30 40 50 60 MTITKIHARS VYDSRGNPTV EVDIVTETGL HRAIVPSGAS TGSHEACELR DGDKSKWGGK 70 80 90 100 110 120 GVTKAVANVN DTIAPALIKE KLDVKDQSAV DAFLNKLDGT TNKTNLGANA ILGVSMAIAK 130 140 150 160 170 180 AAAAEKGVPL YAHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPCEAPTFS 190 200 210 220 230 240 EAMRQGAEVY QKLKALAKKT YGQSAGNVGD EGGVAPDIQT AEEALDLITK AIEEAGYTGK 250 260 270 280 290 300 IKIAMDVASS EFYKADEKKY DLDFKNPDSD KSKWLTYEQL AEMYKSLAEK YPIVSIEDPF 310 320 330 340 350 360 AEDDWEAWSY FFKTYDGQIV GDDLTVTNPE FIKKAIELKS CNALLLKVNQ IGTITEAIQA 370 380 390 400 410 420 AKDAFGAGWG VMVSHRSGET EDVTIADIVV GLRSGQIKTG APARSERLAK LNQILRIEEE 430 LGDNAVYAGN NFRTAVNL

References

[1]	"IgE-binding epitopes of enolases, a class of highly conserved fungal allergens." Simon-Nobbe B., Probst G., Kajava A.V., Oberkofler H., Susani M., Crameri R., Ferreira F., Ebner C., Breitenbach M. J. Allergy Clin. Immunol. 106:887-895(2000) [PubMed: 11080711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGENICITY. Strain: 08-0203-Berlin.
[2]	"Enolases are highly conserved fungal allergens." Breitenbach M., Simon B., Probst G., Oberkofler H., Ferreira F., Briza P., Achatz G., Unger A., Ebner C., Kraft D., Hirschwehr R. Int. Arch. Allergy Immunol. 113:114-117(1997) [PubMed: 9130497] [Abstract] Cited for: ALLERGENICITY.
[3]	"The allergens of Cladosporium herbarum and Alternaria alternata." Breitenbach M., Simon-Nobbe B. Chem. Immunol. 81:48-72(2002) [PubMed: 12102004] [Abstract] Cited for: REVIEW.
[4]	"The spectrum of fungal allergy." Simon-Nobbe B., Denk U., Poell V., Rid R., Breitenbach M. Int. Arch. Allergy Immunol. 145:58-86(2008) [PubMed: 17709917] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U82437 mRNA. Translation: AAG42022.2.
3D structure databases
SMR	Q9HDT3. Positions 3-432.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.11. 74336.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
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

ENO_ALTAL

Accession

Primary (citable) accession number: Q9HDT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 20, 2001
Last modified:	November 24, 2009
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)