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Reviewed, UniProtKB/Swiss-Prot P42895 (ENO2_MAIZE)

Last modified June 16, 2009. Version 59. 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

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Names and origin

Protein namesRecommended name:
    Enolase 2
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 2
    2-phospho-D-glycerate hydro-lyase 2
Gene names
Name: ENO2
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

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Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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
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 – 446446Enolase 2
PRO_0000134074

Regions

Region381 – 3844Substrate binding By similarity

Sites

Active site2161Proton donor By similarity
Active site3541Proton acceptor By similarity
Metal binding2511Magnesium By similarity
Metal binding3021Magnesium By similarity
Metal binding3291Magnesium By similarity
Binding site1641Substrate By similarity
Binding site1731Substrate By similarity
Binding site3021Substrate By similarity
Binding site3291Substrate By similarity
Binding site4051Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
P42895-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DC27708CF92F6850

FASTA44648,163
        10         20         30         40         50         60 
MAATIQSVKA RQIFDSRGNP TVEVDVFCSD GTFARAAVPS GASTGVYEAL ELRDGGSYYL 

        70         80         90        100        110        120 
GKGVSKAVNN VNSVIGPALI GKDPTAQTEI DNFMVQQLDG TKNEWGWCKQ KLGANAILAV 

       130        140        150        160        170        180 
SLAVCKAGAS IKRIPLYQHI ANLAGNKQLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG 

       190        200        210        220        230        240 
AASFKEAMKM GVEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIEKA 

       250        260        270        280        290        300 
GYTGKVVIGM DVAASEFYSD KDQTYDLNFK EENNDGSQKI SGDSLKNVYK SFVSEYPIVS 

       310        320        330        340        350        360 
IEDPFDQDDW VHYAKMTEEI GEQVQIVGDD LLVTNPTRVA KAIKEKSCNA LLLKVNQIGS 

       370        380        390        400        410        420 
VTESIEAVKM SKRAGWGVMT SHRSGETEDT FIADLAVGLS TGQIKTGAPC RSERLAKYNQ 

       430        440 
LLRIEEELGA IAVYAGAKFR APVEPY

« Hide

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References

[1]"Differential regulation of enolase during anaerobiosis in maize."
Lal S.K., Lee C., Sachs M.M.
Plant Physiol. 118:1285-1293(1998) [PubMed: 9847102] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. B73.
Tissue: Root.

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Cross-references

Sequence databases

U17973 mRNA. Translation: AAD04187.1.
PIRT02221.
RefSeqNP_001105371.1.
UniGeneZm.410

3D structure databases

HSSPHSSP built from PDB template 1PDZ based on UniProtKB P56252.
ModBaseSearch...

Genome annotation databases

GeneID542316.

Organism-specific databases

GrameneP42895.
MaizeGDB30060.

Enzyme and pathway databases

BRENDA4.2.1.11. 289.

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 nameENO2_MAIZE
AccessionPrimary (citable) accession number: P42895
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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