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Reviewed, UniProtKB/Swiss-Prot P56252 (ENO_HOMGA)

Last modified June 16, 2009. Version 56. 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:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase
OrganismHomarus gammarus (European lobster) (Homarus vulgaris)
Taxonomic identifier6707 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Nephropoidea › Nephropidae › Homarus

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Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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.

Pathway

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

Subunit structure

Homodimer.

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
   PTMAcetylation
   Technical term3D-structure
Direct 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Enolase
PRO_0000134085

Regions

Region371 – 3744Substrate binding

Sites

Active site2091Proton donor By similarity
Active site3441Proton acceptor By similarity
Metal binding2441Magnesium
Metal binding2941Magnesium
Metal binding3191Magnesium
Binding site361Substrate
Binding site1571Substrate
Binding site1661Substrate
Binding site2941Substrate
Binding site3191Substrate
Binding site3441Substrate
Binding site3741Substrate
Binding site3951Substrate

Amino acid modifications

Modified residue11N-acetylserine

Secondary structure

1 ......................................................................... 433
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P56252-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: CC7DA44B67E9DE3D

FASTA43347,042
        10         20         30         40         50         60 
SITKVFARTI FDSRGNPTVE VDLYTSKGLF RAAVPSGAST GVHEALEMRD GDKSKYHGKS 

        70         80         90        100        110        120 
VFNAVKNVND VIVPEIIKSG LKVTQQKECD EFMCKLDGTE NKSSLGANAI LGVSLAICKA 

       130        140        150        160        170        180 
GAAELGIPLY RHIANLANYD EVILPVPAFN VINGGSHAGN KLAMQEFMIL PTGATSFTEA 

       190        200        210        220        230        240 
MRMGTEVYHH LKAVIKARFG LDATAVGDEG GFAPNILNNK DALDLIQEAI KKAGYTGKIE 

       250        260        270        280        290        300 
IGMDVAASEF YKQNNIYDLD FKTANNDGSQ KISGDQLRDM YMEFCKDFPI VSIEDPFDQD 

       310        320        330        340        350        360 
DWETWSKMTS GTTIQIVGDD LTVTNPKRIT TAVEKKACKC LLLKVNQIGS VTESIDAHLL 

       370        380        390        400        410        420 
AKKNGWGTMV SHRSGETEDC FIADLVVGLC TGQIKTGAPC RSERLAKYNQ ILRIEEELGS 

       430 
GAKFAGKNFR APS

« Hide

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References

[1]"X-ray structure and catalytic mechanism of lobster enolase."
Duquerroy S., Camus C., Janin J.
Biochemistry 34:12513-12523(1995) [PubMed: 7547999] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND MAGNESIUM IONS.
Tissue: Muscle.

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Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PDYX-ray2.40A1-433[»]
1PDZX-ray2.20A1-433[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.2.1.11. 292312.

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...

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Entry information

Entry nameENO_HOMGA
AccessionPrimary (citable) accession number: P56252
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 56 of the entry and version 1 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