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Reviewed, UniProtKB/Swiss-Prot P00924 (ENO1_YEAST)

Last modified November 25, 2008. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1
Gene names
Name: ENO1
Synonyms: ENOA, HSP48
Ordered Locus Names: YGR254W
ORF Names: G9160
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length437 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 + H(2)O.

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 76700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the enolase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKC1P245831EBI-6468,EBI-9860

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 437436Enolase 1
PRO_0000134062

Regions

Region373 – 3764Substrate binding

Sites

Active site2121Proton donor Probable
Active site3461Proton acceptor
Metal binding2471Magnesium
Metal binding2961Magnesium
Metal binding3211Magnesium
Binding site1601Substrate
Binding site1691Substrate
Binding site2961Substrate
Binding site3211Substrate
Binding site3971Substrate

Amino acid modifications

Modified residue101Phosphoserine
Modified residue141Phosphoserine
Modified residue371Phosphoserine
Modified residue401Phosphoserine
Modified residue411Phosphothreonine
Modified residue961Phosphoserine
Modified residue1041Phosphoserine
Modified residue1191Phosphoserine
Modified residue1431Phosphoserine
Modified residue1881Phosphoserine
Modified residue3241Phosphothreonine
Modified residue4041Phosphoserine

Experimental info

Mutagenesis401S → A: Reduces activity by 99.9%
Mutagenesis1601H → A, F or N: Reduces activity by 99%
Mutagenesis1691E → Q: Reduces Kcat over 100000-fold
Mutagenesis2081N → A: Reduces activity by 44%
Mutagenesis2121E → Q: Reduces Kcat over 100000-fold
Mutagenesis3461K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction
Sequence conflict2421V → I in CAA67616 and CAA97283. Ref.2

Secondary structure

............................................................................. 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00924-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5E874ABDFA495E17

FASTA43746,802
        10         20         30         40         50         60 
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK 

        70         80         90        100        110        120 
GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR 

       130        140        150        160        170        180 
AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF 

       190        200        210        220        230        240 
AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG 

       250        260        270        280        290        300 
KVKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA 

       310        320        330        340        350        360 
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA 

       370        380        390        400        410        420 
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 

       430 
GDNAVFAGEN FHHGDKL 

« Hide

References

« Hide 'large scale' references
[1]"The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes."
Holland M.J., Holland J.P., Thill G.P., Jackson K.A.
J. Biol. Chem. 256:1385-1395(1981) [PubMed: 6256394] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
Yeast 13:369-372(1997) [PubMed: 9133741] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [