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Reviewed, UniProtKB/Swiss-Prot P51913 (ENOA_CHICK)

Last modified November 24, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Phosphopyruvate hydratase
Gene names
Name: ENO1
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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.

Sequence similarities

Belongs to the enolase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
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: UniProtKB-KW

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Alpha-enolase
PRO_0000134101

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2451Magnesium By similarity
Metal binding2931Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Secondary structure

1 ........................................................................... 434
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P51913-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 81428BB175FD7400

FASTA43447,305
        10         20         30         40         50         60 
MSILKIHARE IFDSRGNPTV EVDLYTNKGL FRAAVPSGAS TGIYEALELR DNDKTRYLGK 

        70         80         90        100        110        120 
GVSKAVEHVN KTIAPALISK NVNVVEQEKI DKLMLEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGADTFKE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IGKAGYSDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ISPDQLADLY LGFVKNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WAAWKKFTAS VGIQVVGDDL TVTNPKRIAK AVEEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 

       430 
ARFAGRNFRN PRIN

« Hide

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References

[1]"Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis."
Tanaka M., Maeda K., Nakashima K.
J. Biochem. 117:554-559(1995) [PubMed: 7629021] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: White leghorn.
Tissue: Kidney.

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Cross-references

Sequence databases

D37900 mRNA. Translation: BAA07132.1.
IPIIPI00575584.
PIRJC4186.
RefSeqNP_990451.1.
UniGeneGga.1383

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GUAmodel-A1-434[»]
SMRP51913. Positions 2-433.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51913.

Proteomic databases

PRIDEP51913.

Genome annotation databases

EnsemblENSGALT00000003745; ENSGALP00000003737; ENSGALG00000002377; Gallus gallus. [Genome view]
GeneID396017.
KEGGgga:396017.

Organism-specific databases

CTD396017.

Phylogenomic databases

HOVERGENP51913.

Enzyme and pathway databases

BRENDA4.2.1.11. 4.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
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...

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Entry information

Entry nameENOA_CHICK
AccessionPrimary (citable) accession number: P51913
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 24, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents