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Reviewed, UniProtKB/Swiss-Prot O57391 (ENOG_CHICK)

Last modified September 1, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Gamma-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Neural enolase
      Short name=NSE
Gene names
Name: ENO2
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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.

Tissue specificity

Expressed in the brain and, to much less but significant extents, in the pituitary and adrenal glands.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Gamma-enolase
PRO_0000134115

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

Sequences

Sequence LengthMass (Da)Tools
O57391-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 359E32F78BACCE07

FASTA43447,308
        10         20         30         40         50         60 
MAVERIHARE ILDSRGNPTV EVDLYTHKGM FRAAVPSGAS TGIYEALELR DNDKSRFLGK 

        70         80         90        100        110        120 
GVLQAVDHIN STVAPAIVGS GLSVVDQEKI DNLMLEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKDVPL YRHIADLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD 

       190        200        210        220        230        240 
AMRIGAEVYH NLKSVIKEKY GKDATNVGDE GGFAPNILEN SEALELLKEA IDKAGYTDKI 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ISADELGDLY QSFVRAYPVL SIEDPFDQDD 

       310        320        330        340        350        360 
WEAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA 

       370        380        390        400        410        420 
QENGWGVMVS HRSGETEDTF IADLVVALCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE 

       430 
ARFAGHNFRN PSVL 

« Hide

References

[1]"cDNA cloning and characterization of neuron-specific enolase from chicken."
Tanaka M., Taniguchi T., Ohkubo T., Nakashima K.
Biochim. Biophys. Acta 1395:28-33(1998) [PubMed: 9434147] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases

AB004291 mRNA. Translation: BAA24680.1.
IPIIPI00592520.
RefSeqNP_990207.1.
UniGeneGga.4132

3D structure databases

HSSPHSSP built from PDB template 1PDZ based on UniProtKB P56252.
SMRO57391. Positions 2-434.
ModBaseSearch...

Protein-protein interaction databases

STRINGO57391.

Proteomic databases

PRIDEO57391.

Genome annotation databases

EnsemblENSGALT00000023444; ENSGALP00000023398; ENSGALG00000014528; Gallus gallus. [Genome view]
GeneID395689.
KEGGgga:395689.

Organism-specific databases

CTD395689.

Phylogenomic databases

HOGENOMO57391.
HOVERGENO57391.

Enzyme and pathway databases

BRENDA4.2.1.11. 4.

Family and domain databases

InterProIPR000941. Enolase.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
ProDomPD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENOG_CHICK
AccessionPrimary (citable) accession number: O57391
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: September 1, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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