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Reviewed, UniProtKB/Swiss-Prot Q9W7L2 (ENOA_SCEUN)

Last modified February 9, 2010. Version 54. 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:
    Alpha-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Phosphopyruvate hydratase
OrganismSceloporus undulatus (Eastern fence lizard) (Skink)
Taxonomic identifier8520 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataIguaniaIguanidaePhrynosomatinaeSceloporus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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

Initiator methionine11Removed By similarity
Chain2 – 434433Alpha-enolase
PRO_0000134104

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
Q9W7L2-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6E377E0F0A767E11

FASTA43447,493
        10         20         30         40         50         60 
MSILKLHARE IFDSRGNPTV EVDLYTNKGL FRAAVPSGAS TGIYEALELR DNDKTRFLGK 

        70         80         90        100        110        120 
GVSKAVEHVN KTIAPALVNK KVNVVEQEKI DKLMLEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN EDVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAENFKE 

       190        200        210        220        230        240 
AMRIGAEVYQ NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKSA ISKAGYTDKI 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ITPDQLSDLY KGFIKNYPVV SIEDPFDQHD 

       310        320        330        340        350        360 
WAAWKKFTAS AGIQVVGDDL TVTNPRRITK AVEEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QTNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK 

       430 
GRFAGRNFRN PRVN 

« Hide

References

[1]"Molecular evidence for a clade of turtles."
Mannen H., Li S.S.-L.
Mol. Phylogenet. Evol. 13:144-148(1999) [PubMed: 10508547] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF072587 mRNA. Translation: AAD41644.1.

3D structure databases

SMRQ9W7L2. Positions 2-431.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9W7L2.

Enzyme and pathway databases

BRENDA4.2.1.11. 278199.

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...

Entry information

Entry nameENOA_SCEUN
AccessionPrimary (citable) accession number: Q9W7L2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 54 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