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Reviewed, UniProtKB/Swiss-Prot P26301 (ENO1_MAIZE)

Last modified June 16, 2009. Version 60. 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 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1
Gene names
Name: ENO1
Synonyms: PGH1
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 1
PRO_0000134073

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
P26301-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 6266C48914F35198

FASTA44648,064
        10         20         30         40         50         60 
MAVTITWVKA RQIFDSRGNP TVEVDVGLSD GSYARGAVPS GASTGIYEAL ELRDGGSDYL 

        70         80         90        100        110        120 
GKGVLKAVSN VNNIIGPAIV GKDPTEQVEI DNFMVQQLDG TSNEWGWCKQ KLGANAILAV 

       130        140        150        160        170        180 
SLAVCKAGAM VKKIPLYQHI ANLAGNKTLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG 

       190        200        210        220        230        240 
ASSFKEAMKM GVEVYHNLKS IIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKAAIEKA 

       250        260        270        280        290        300 
GYTGKVVIGM DVAASEFFGE KDKTYDLNFK EENNDGSNKI SGDSLKDLYK SFVSEYPIES 

       310        320        330        340        350        360 
IEDPFDQDDW STYAKLTDEI GQKVQIVGDD LLVTNPTRVA KAINEKTCNA LLLKVNQIGS 

       370        380        390        400        410        420 
VTESIEAVRM SKRAGWGVMA SHRSGETEDT FIADLSVGLS TGQIKTGAPC RSERLAKYNQ 

       430        440 
LLRIEEELGD AAVYAGAKFR APVEPY

« Hide

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References

[1]"Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli."
Lal S.K., Johnson S., Conway T., Kelley P.M.
Plant Mol. Biol. 16:787-795(1991) [PubMed: 1859865] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Berkeley Fast.
Tissue: Root.

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Cross-references

Sequence databases

X55981 mRNA. Translation: CAA39454.1.
PIRS16257.
RefSeqNP_001105896.1.
UniGeneZm.93820

3D structure databases

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

Genome annotation databases

GeneID732811.

Organism-specific databases

GrameneP26301.
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 nameENO1_MAIZE
AccessionPrimary (citable) accession number: P26301
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 60 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