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P40370 (ENO11_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase 1-1
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1-1
2-phosphoglycerate dehydratase 1-1
Gene names
Name:eno101
Synonyms:eno1
ORF Names:SPBC1815.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 By similarity.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from direct assay. Source: GeneDB_Spombe

phosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Enolase 1-1
PRO_0000134058

Regions

Region372 – 3754Substrate binding By similarity

Sites

Active site2111Proton donor By similarity
Active site3451Proton acceptor By similarity
Metal binding2461Magnesium By similarity
Metal binding2951Magnesium By similarity
Metal binding3201Magnesium By similarity
Binding site1591Substrate By similarity
Binding site1681Substrate By similarity
Binding site2951Substrate By similarity
Binding site3201Substrate By similarity
Binding site3961Substrate By similarity

Amino acid modifications

Modified residue851Phosphothreonine Ref.4
Modified residue2491Phosphoserine Ref.4
Modified residue2501Phosphoserine Ref.4
Modified residue2531Phosphotyrosine Ref.4
Modified residue3511Phosphoserine Ref.4
Modified residue3531Phosphothreonine Ref.4
Modified residue3551Phosphoserine Ref.4
Modified residue4211Phosphoserine Ref.4

Experimental info

Sequence conflict13 – 153DSR → ALG in AAA70080. Ref.1
Sequence conflict1911H → Q in AAA70080. Ref.1
Sequence conflict2481A → T in AAA70080. Ref.1
Sequence conflict3581A → V in AAA70080. Ref.1
Sequence conflict3771E → G in AAA70080. Ref.1
Sequence conflict4221E → R in AAA70080. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40370 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 4CA257CFF4B456E3

FASTA43947,436
        10         20         30         40         50         60 
MAIQKVFARQ IYDSRGNPTV EVDLTTETGI HRAIVPSGAS TGIWEALEMR DGDKTKWGGK 

        70         80         90        100        110        120 
GVLKAVGNVN NIIAPAVVKA NLDVTDQKAA DEFLLKLDGT ENKSKLGANA ILGVSMAICR 

       130        140        150        160        170        180 
AGAAQKKLPL WKYIAENFGT KGPYVLPVPS FNVLNGGSHA GGDLAFQEFM ILPTGAPSFS 

       190        200        210        220        230        240 
EAMRWGAETY HTLKSIAKKR YGSSAGNVGD EGGIAPDLQT PQEALDLIVE AINKAGYEGK 

       250        260        270        280        290        300 
IKIGLDVASS EFYVDGKYDL DIKAAKPKPE NKLTYQQLTD LYVELSKKYP IVSIEDPFDQ 

       310        320        330        340        350        360 
DDWSAWTHMK AETDFQIVGD DLTVTNVKRL RTAIDKKCAN ALLLKVNQIG SVTESLNAVR 

       370        380        390        400        410        420 
MSYEAGWGVM VSHRSGETAD TFISHLTVGI GAGQLKSGAP CRSERLAKYN ELLRIEEELG 

       430 
SEGVYAGAHA GKYIKAAKF

« Hide

References

« Hide 'large scale' references
[1]"A cDNA from Schizosaccharomyces pombe encoding a putative enolase."
Jackson J.C., Lopes J.M.
Gene 154:109-113(1995) [PubMed: 7867936] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of enolase gene of S. pombe."
Park S.-K.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: 972 / ATCC 24843.
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-249; SER-250; TYR-253; SER-351; THR-353; SER-355 AND SER-421, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U13799 mRNA. Translation: AAA70080.1.
L37084 mRNA. Translation: AAA51399.2.
CU329671 Genomic DNA. Translation: CAB43486.1.
PIRJC4036.
T39737.
T45116.
RefSeqNP_595903.1. NM_001021810.1.

3D structure databases

ProteinModelPortalP40370.
SMRP40370. Positions 2-427.
ModBaseSearch...

Protein-protein interaction databases

IntActP40370. 2 interactions.
MINTMINT-4689541.
STRINGP40370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1815.01.1; SPBC1815.01.1:pep; SPBC1815.01.
GeneID2539782.
GenomeReviewsGene locus eno101 in contig CU329671_GR.
KEGGspo:SPBC1815.01.
NMPDRfig|4896.1.peg.1769.

Organism-specific databases

GeneDB_SpombeSPBC1815.01.

Phylogenomic databases

eggNOGfuNOG04478.
GeneTreeEFGT00050000005340.
HOGENOMHBG726599.
OMAKVEIGMD.
OrthoDBEOG48WG9D.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003972-MONOMER.

Gene expression databases

ArrayExpressP40370.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 1 hit.
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 nameENO11_SCHPO
AccessionPrimary (citable) accession number: P40370
Secondary accession number(s): Q12703, Q9Y7J7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 11, 2001
Last modified: December 14, 2011
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents