Reviewed, UniProtKB/Swiss-Prot Q96X30 (ENO_ASPFU)

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=Asp f 22

Gene names

Name:	enoA
ORF Names:	AFUA_6G06770

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Disease	Allergen
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 438	437	Enolase		PRO_0000134041
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
Experimental info
	Sequence conflict	25	1	V → A in AAK49451. Ref.1
	Sequence conflict	425	1	A → T in AAK49451. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96X30-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 821212CBDCBAEA2A	FASTA	438	47,305
	10 20 30 40 50 60 MPISKIHARS VYDSRGNPTV EVDVVTETGL HRAIVPSGAS TGQHEAHELR DGDKTQWGGK 70 80 90 100 110 120 GVLKAVKNVN ETIGPALIKE NIDVKDQSKV DEFLNKLDGT ANKSNLGANA ILGVSLAVAK 130 140 150 160 170 180 AGAAEKGVPL YAHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPDSAPSFS 190 200 210 220 230 240 EALRQGAEVY QKLKALAKKK YGQSAGNVGD EGGVAPDIQT AEEALDLITE AIEQAGYTGK 250 260 270 280 290 300 IKIAMDVASS EFYKADVKKY DLDFKNPESD PSKWLTYEQL ADLYKSLAAK YPIVSIEDPF 310 320 330 340 350 360 AEDDWEAWSY FYKTSDFQIV GDDLTVTNPG RIKKAIELKS CNALLLKVNQ IGTLTESIQA 370 380 390 400 410 420 AKDSYADNWG VMVSHRSGET EDVTIADIAV GLRSGQIKTG APCRSERLAK LNQILRIEEE 430 LGENAVYAGS KFRTAVNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and immunological characterization of a newly identified enolase allergen from Penicillium citrinum and Aspergillus fumigatus." Lai H.-Y., Tam M.F., Tang R.-B., Chou H., Chang C.-Y., Tsai J.-J., Shen H.-D. Int. Arch. Allergy Immunol. 127:181-190(2002) [PubMed: 11979043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22, ALLERGENICITY. Strain: CCRC 33476.
[2]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF284645 mRNA. Translation: AAK49451.1. AAHF01000006 Genomic DNA. Translation: EAL88532.1.
RefSeq	XP_750570.1.
3D structure databases
SMR	Q96X30. Positions 3-432.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96X30.
Genome annotation databases
GeneID	3508747.
GenomeReviews	Gene locus enoA in contig CM000174_GR.
KEGG	afm:AFUA_6G06770.
Phylogenomic databases
HOGENOM	Q96X30.
OMA	INDTIAP
OrthoDB	EOG91G4M7
Enzyme and pathway databases
BRENDA	4.2.1.11. 18841.
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_ASPFU

Accession

Primary (citable) accession number: Q96X30
Secondary accession number(s): Q4WND2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 50 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)