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Q96X30 (ENO_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Allergen=Asp f 22
Gene names
Name:enoA
ORF Names:AFUA_6G06770
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processGlycolysis
   Cellular componentCytoplasm
   DiseaseAllergen
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 438437Enolase
PRO_0000134041

Regions

Region374 – 3774Substrate binding By similarity

Sites

Active site2111Proton donor By similarity
Active site3471Proton acceptor By similarity
Metal binding2461Magnesium By similarity
Metal binding2971Magnesium By similarity
Metal binding3221Magnesium By similarity
Binding site1591Substrate By similarity
Binding site1681Substrate By similarity
Binding site2971Substrate By similarity
Binding site3221Substrate By similarity
Binding site3981Substrate By similarity

Experimental info

Sequence conflict251V → A in AAK49451. Ref.1
Sequence conflict4251A → T in AAK49451. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96X30 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 821212CBDCBAEA2A

FASTA43847,305
        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 

« Hide

References

« Hide '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, ALLERGEN.
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. expand/collapse author list , 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: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF284645 mRNA. Translation: AAK49451.1.
AAHF01000006 Genomic DNA. Translation: EAL88532.1.
RefSeqXP_750570.1. XM_745477.1.

3D structure databases

ProteinModelPortalQ96X30.
SMRQ96X30. Positions 3-432.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96X30.

Protein family/group databases

Allergome3116. Asp f 22.0101.
72. Asp f 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001960; CADAFUAP00001960; CADAFUAG00001960.
GeneID3508747.
GenomeReviewsGene locus enoA in contig CM000174_GR.
KEGGafm:AFUA_6G06770.

Phylogenomic databases

eggNOGfuNOG04478.
GeneTreeEFGT00050000005340.
HOGENOMHBG726599.
OMAEAWSYFY.
OrthoDBEOG48WG9D.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. Eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO_ASPFU
AccessionPrimary (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: December 14, 2011
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families