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B1YLD8 (ENO_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. 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:Exig_2393
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillales Family XII. Incertae Sedis › Exiguobacterium ›

Protein attributes

Sequence length430 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 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 – 430430Enolase HAMAP-Rule MF_00318
PRO_1000115864

Regions

Region366 – 3694Substrate binding By similarity

Sites

Active site2051Proton donor By similarity
Active site3391Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2871Magnesium By similarity
Metal binding3141Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2871Substrate By similarity
Binding site3141Substrate By similarity
Binding site3391Substrate (covalent); in inhibited form By similarity
Binding site3901Substrate By similarity

Amino acid modifications

Modified residue2811Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YLD8 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: D332A59301988103

FASTA43046,328
        10         20         30         40         50         60 
MSMITEIYAR EILDSRGNPT VEVEVYTEDG GFGRALVPSG ASTGEHEAVE LRDGDKSRYL 

        70         80         90        100        110        120 
GKGVLKAVDN VNEKLAPEII GYDVFDQAGI DKKMIDLDGT KNKGNFGANA ILGISMAAAR 

       130        140        150        160        170        180 
AAADELGLPL YTYLGGFNAK TLPTPMMNII NGGSHADNNV DFQEFMIMPV GAPTFKEALR 

       190        200        210        220        230        240 
MGAEIFHALK SVLSGMGLNT AVGDEGGFAP NLKSNEEAIT VILEAIEKAG YKAGEDVYLA 

       250        260        270        280        290        300 
MDVASSEFYD KAAGKYNLAG EGKVLSTEEL VEFYAQLVDK YPIISIEDGC DENDWDGHKL 

       310        320        330        340        350        360 
LTDRIGHKVQ LVGDDLFVTN TEKLAEGIEK GIANSILIKV NQIGTLTETF DAIEMAKKAG 

       370        380        390        400        410        420 
YTAVVSHRSG ETEDSTIADI AVATNAGQIK TGSLSRTDRI AKYNQLLRIE DMLSDVAVYD 

       430 
GIKSFYNLKK

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001022 Genomic DNA. Translation: ACB61843.1.
RefSeqYP_001814860.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YLD8.
ModBaseSearch...

Protein-protein interaction databases

STRING262543.Exig_2393.

Proteomic databases

PRIDEB1YLD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB61843; ACB61843; Exig_2393.
GeneID6172765.
KEGGesi:Exig_2393.
PATRIC32138418. VBIExiSib53410_2431.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072173.
KOK01689.
OMAEYMIMPL.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycESIB262543:GHBP-2473-MONOMER.
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_EXIS2
AccessionPrimary (citable) accession number: B1YLD8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 34 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

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