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Q8R967 (ENO_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene names
Name:eno
Ordered Locus Names:TTE1759
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobacter

Protein attributes

Sequence length429 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 By similarity. HAMAP-Rule MF_00318

Catalytic activity

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

Cofactor

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

Enzyme regulation

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

Pathway

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

Sequence similarities

Belongs to the enolase family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   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 – 429429Enolase HAMAP-Rule MF_00318
PRO_0000133997

Regions

Region365 – 3684Substrate binding By similarity

Sites

Active site2051Proton donor By similarity
Active site3381Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2861Magnesium By similarity
Metal binding3131Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2861Substrate By similarity
Binding site3131Substrate By similarity
Binding site3381Substrate (covalent); in inhibited form By similarity
Binding site3891Substrate By similarity

Amino acid modifications

Modified residue2801Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R967 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: ABCC2445DEBA8D65

FASTA42946,297
        10         20         30         40         50         60 
MSSIIDIYAR EILDSRGNPT IEVEVELDSG AVGRAAVPSG ASTGAFEAIE LRDGDKSRYL 

        70         80         90        100        110        120 
GKGVLKAVQN VNDIIAPELI GMEAQDQVAI DKAMIELDGT PNKSKLGANA ILGVSLAVAK 

       130        140        150        160        170        180 
AAAEELGLPL YQYLGGVNAK TLPVPMMNIL NGGKHADNNV DIQEFMIMPV GAPNFKEALR 

       190        200        210        220        230        240 
MCSEVYHSLK NVLHSKGLST TVGDEGGFAP NLTSNEEAIK VILEAIEKAG YVPGEDIVLA 

       250        260        270        280        290        300 
LDPAATEMYK EDGKYHFEGE GIVRTSEEMI EFWEQLVSKY PIVSIEDGLA EEDWNGWKLL 

       310        320        330        340        350        360 
TERLGKKVQL VGDDLFVTNT ERLSKGINMG VANSILIKLN QIGTLTETLD AIEMAKRAGY 

       370        380        390        400        410        420 
TAIVSHRSGE TEDTTIADLV VATNVGQIKT GAPARTDRVA KYNQLLRIEE ALGSVAQYPG 


KNAFYNIRK 

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References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM24953.1.
RefSeqNP_623349.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8R967.
SMRQ8R967. Positions 2-428.
ModBaseSearch...

Protein-protein interaction databases

STRING273068.TTE1759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM24953; AAM24953; TTE1759.
GeneID996800.
KEGGtte:TTE1759.
PATRIC23898261. VBITheTen82880_1768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072173.
KOK01689.
OMAEYMIMPL.
ProtClustDBPRK00077.

Enzyme and pathway databases

UniPathwayUPA00109; UER00187.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 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 nameENO_THETN
AccessionPrimary (citable) accession number: Q8R967
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families