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Reviewed, UniProtKB/Swiss-Prot Q8DPS0 (ENO_STRR6)

Last modified February 9, 2010. 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

Names and origin

Protein namesRecommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase
Gene names
Name: eno
Ordered Locus Names: spr1036
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Complete proteome] [HAMAP]
Taxonomic identifier171101 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence By similarity. HAMAP MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity. HAMAP MF_00318

Enzyme regulation

The covalent binding to the substrate of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP MF_00318

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP MF_00318

Subunit structure

Homooctamer By similarity. HAMAP MF_00318

Subcellular location

Cytoplasm. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface, probably in complex with plasminogen By similarity. HAMAP MF_00318

Sequence similarities

Belongs to the enolase family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

phosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: HAMAP

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Enolase HAMAP MF_00318
PRO_0000133981

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2051Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2911Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2911Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue2851Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DPS0-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3E85FCA26DC8BC96

FASTA43447,103
        10         20         30         40         50         60 
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG 

        70         80         90        100        110        120 
GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR 

       130        140        150        160        170        180 
AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR 

       190        200        210        220        230        240 
YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFLG 

       250        260        270        280        290        300 
FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD 

       310        320        330        340        350        360 
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA 

       370        380        390        400        410        420 
KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV 

       430 
AEYRGLKSFY NLKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007317 Genomic DNA. Translation: AAK99840.1.
PIRD98001.
RefSeqNP_358630.1.

3D structure databases

SMRQ8DPS0. Positions 1-432.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8DPS0.

Genome annotation databases

GeneID934109.
GenomeReviewsGene locus spr1036 in contig AE007317_GR.
KEGGspr:spr1036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHBG726599.
OMADIAVGTN.
PhylomeDBQ8DPS0.

Enzyme and pathway databases

BioCycSPNE171101:SPR1036-MONOMER.

Family and domain databases

HAMAPMF_00318. Enolase.
[Tree]
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 nameENO_STRR6
AccessionPrimary (citable) accession number: Q8DPS0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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