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Reviewed, UniProtKB/Swiss-Prot Q8NKC2 (ENO12_SCHPO)

Last modified June 16, 2009. Version 46. 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 1-2
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1-2
    2-phospho-D-glycerate hydro-lyase 1-2
Gene names
Name: eno102
Synonyms: eno1
ORF Names: SPBPB21E7.01c, SPBPB8B6.07c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. UniProtKB P00924

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. UniProtKB P00924

Subcellular location

Cytoplasm By similarity. UniProtKB P00924

Sequence similarities

Belongs to the enolase family. UniProtKB P00924

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
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 – 440440Enolase 1-2
PRO_0000134059

Regions

Region373 – 3764Substrate binding By similarity

Sites

Active site2121Proton donor By similarity
Active site3461Proton acceptor By similarity
Metal binding2471Magnesium By similarity UniProtKB P00924
Metal binding2961Magnesium By similarity UniProtKB P00924
Metal binding3211Magnesium By similarity UniProtKB P00924
Binding site1601Substrate By similarity
Binding site1691Substrate By similarity
Binding site2961Substrate By similarity
Binding site3211Substrate By similarity
Binding site3971Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8NKC2-1 [UniParc].

Last modified April 11, 2003. Version 2.
Checksum: E59B1487C8C6B382

FASTA44047,867
        10         20         30         40         50         60 
MTTIQKIYSR SIYDSRGNPT VEVELTTELG TFRSMVPSGA STGEWEAKEL RDNDKNKWGG 

        70         80         90        100        110        120 
KGVTIAVHNV NNIIGPALVK SDIKITDQRG IDEFMIKLDG TNDKSKLGAN SIVGVSMAVA 

       130        140        150        160        170        180 
RAAAAFLKIP LYEYIGKLAG SKTTECIPVP SFNVLNGGRH AGGDLAFQEF MIMPIKAPTF 

       190        200        210        220        230        240 
SEGLRWGSEV YHTLKALAKK KYGASAGNVG DEGGIAPDLT TAEEALDLVN EAIKEAGYDG 

       250        260        270        280        290        300 
KVKIGFDVAA SELYNGKLYD LDFKSEHPKP ENKLDYKKLY EKYSALIEKY PIVFIEDPFS 

       310        320        330        340        350        360 
EEDWGAFSYM SSKTKVEVIA DDLTVTNVKR LSKAIELKCA NALLVKINQI GSLSETIDAA 

       370        380        390        400        410        420 
NMAKKAGWGL MVSHRSGETD DSFIAHLAVG LEAGQMKSGA PCRSERLAKY NELLRIEDNL 

       430        440 
GDSAIYAGTR AADYIKSNTL

« Hide

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References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

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Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAD27913.2.
RefSeqNP_001018769.2.

3D structure databases

HSSPHSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
ModBaseSearch...

Genome annotation databases

GeneID3361181.
KEGGspo:SPBPB21E7.01c.

Organism-specific databases

GeneDB_SpombeSPBPB21E7.01c.

Enzyme and pathway databases

BRENDA4.2.1.11. 653.

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 nameENO12_SCHPO
AccessionPrimary (citable) accession number: Q8NKC2
Secondary accession number(s): Q8TFF7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: April 11, 2003
Last modified: June 16, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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