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Reviewed, UniProtKB/Swiss-Prot P07322 (ENOB_CHICK)

Last modified June 16, 2009. Version 80. 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:
    Beta-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Phosphopyruvate hydratase
Gene names
Name: ENO3
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length434 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.

Pathway

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

Subunit structure

Homodimer. Interacts with PNKD By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   PTMAcetylation
   Technical termDirect protein sequencing
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

Initiator methionine11Removed Ref.2
Chain2 – 434433Beta-enolase
PRO_0000134111

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

Amino acid modifications

Modified residue21N-acetylserine Ref.3

Experimental info

Sequence conflict171E → D AA sequence Ref.2
Sequence conflict491P → L AA sequence Ref.2
Sequence conflict941M → V AA sequence Ref.2
Sequence conflict119 – 1202CK → SH AA sequence Ref.2
Sequence conflict2091G → D AA sequence Ref.2
Sequence conflict2581H → D AA sequence Ref.2
Sequence conflict266 – 2672HT → DP AA sequence Ref.2
Sequence conflict2701Y → L AA sequence Ref.2
Sequence conflict3091F → S AA sequence Ref.2
Sequence conflict3231T → A AA sequence Ref.2
Sequence conflict3311G → A AA sequence Ref.2
Sequence conflict3431K → G AA sequence Ref.2
Sequence conflict394 – 3952KT → EQ AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07322-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 892D1BE4B6342F44

FASTA43447,196
        10         20         30         40         50         60 
MSIQKIHARE ILDSRGEPTV EVDLHTAKGH FRAAVPSGAS TGIHEALEPR DGDKKRFLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTIGPALIEK KISVVEQEKI DKVMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN TELILPVPAF NVINGGSHAG NKLAMQEFMV LPVGAASFHD 

       190        200        210        220        230        240 
AMRVGAEVYH SLKGVIKAKY GKDATNVGGE GGFAPNILDN HEALELLKAA IAQAGYTDKV 

       250        260        270        280        290        300 
VIGMDVAASE FCRDGRYHLD FKSPPHTKRY ITGEQLGEIY RGFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WEAWKRFVFH VDIQVVGDDL TVTNPKRIAH GAEQHACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSHGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AKFAGRKFRN PKAK 

« Hide

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: Muscle.
[2]"The complete amino acid sequence of chicken skeletal-muscle enolase."
Russell G.A., Dunbar B., Fothergill-Gilmore L.A.
Biochem. J. 236:115-126(1986) [PubMed: 3539098] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-434.
[3]"Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase."
Gibson B.W., Daley D.J., Williams D.H.
Anal. Biochem. 169:217-226(1988) [PubMed: 2898218] [Abstract]
Cited for: ACETYLATION AT SER-2.

Cross-references

Sequence databases

D37901 mRNA. Translation: BAA07133.1.
IPIIPI00586105.
PIRA23850.
JC4187.
RefSeqNP_990450.1.
UniGeneGga.4297

3D structure databases

HSSPHSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
SMRP07322. Positions 2-431.
ModBaseSearch...

Proteomic databases

PRIDEP07322.

Genome annotation databases

GeneID396016.
KEGGgga:396016.

Phylogenomic databases

HOVERGENP07322.

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 nameENOB_CHICK
AccessionPrimary (citable) accession number: P07322
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 80 of the entry and version 3 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