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Q2YPV0 (ENO_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene names
Name:eno
Ordered Locus Names:BAB1_1155
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length425 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 By similarity. HAMAP-Rule MF_00318

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 By similarity. Secreted By similarity. Cell surface By similarity. 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-HAMAP

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Enolase HAMAP-Rule MF_00318
PRO_0000267006

Regions

Region363 – 3664Substrate binding By similarity

Sites

Active site2041Proton donor By similarity
Active site3361Proton acceptor By similarity
Metal binding2411Magnesium By similarity
Metal binding2841Magnesium By similarity
Metal binding3111Magnesium By similarity
Binding site1541Substrate By similarity
Binding site1631Substrate By similarity
Binding site2841Substrate By similarity
Binding site3111Substrate By similarity
Binding site3361Substrate (covalent); in inhibited form By similarity
Binding site3871Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YPV0 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: A148573BD4696545

FASTA42545,261
        10         20         30         40         50         60 
MTAIIDIVGR EILDSRGNPT VEVDVVLEDG SFGRAAVPSG ASTGAHEAVE LRDGGSRYLG 

        70         80         90        100        110        120 
KGVEKAVEVV NGKIFDAIAG MDAESQLLID QTLIDLDGSA NKGNLGANAI LGVSLAVAKA 

       130        140        150        160        170        180 
AAQASGLPLY RYVGGTNAHV LPVPMMNIIN GGAHADNPID FQEFMILPVG ATSIREAVRY 

       190        200        210        220        230        240 
GSEVFHTLKK RLKDAGHNTN VGDEGGFAPN LKNAQAALDF IMESIEKAGF KPGEDIALGL 

       250        260        270        280        290        300 
DCAATEFFKD GNYVYEGERK TRDPKAQAKY LAKLASDYPI VTIEDGMAED DWEGWKYLTD 

       310        320        330        340        350        360 
LIGNKCQLVG DDLFVTNSAR LRDGIRLGVA NSILVKVNQI GSLSETLDAV ETAHKAGYTA 

       370        380        390        400        410        420 
VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRTAKY NQLIRIEEEL GKQARYAGRS 


ALKLL 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ11111.1.
RefSeqYP_414546.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YPV0.
SMRQ2YPV0. Positions 2-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_1155.

Proteomic databases

PRIDEQ2YPV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ11111; CAJ11111; BAB1_1155.
GeneID3788689.
KEGGbmf:BAB1_1155.
PATRIC17845267. VBIBruMel86222_1203.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072173.
KOK01689.
OMARSEIKGQ.
OrthoDBEOG65J589.

Enzyme and pathway databases

BioCycBABO359391:GKDV-1177-MONOMER.
BMEL359391:GJOQ-1177-MONOMER.
UniPathwayUPA00109; UER00187.

Family and domain databases

Gene3D3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
SUPFAMSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO_BRUA2
AccessionPrimary (citable) accession number: Q2YPV0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 7, 2006
Last modified: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names