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P57492 (ENO_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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:BU417
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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 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

Subunit structure

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation By similarity.

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
Reference 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 – 434434Enolase HAMAP-Rule MF_00318
PRO_0000133855

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2091Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2461Magnesium By similarity
Metal binding2911Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1591Substrate By similarity
Binding site1681Substrate By similarity
Binding site2911Substrate By similarity
Binding site3181Substrate By similarity
Binding site3431Substrate (covalent); in inhibited form By similarity
Binding site3941Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P57492 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: D3F5FD25D8F52D40

FASTA43447,428
        10         20         30         40         50         60 
MSKITKIIAR EIIDSRGNPT VESEVHLEGG FVGLASSPSG ASTGSLEALE LRDENKDRFM 

        70         80         90        100        110        120 
GKGVEKAVSL INEKISIALK NKNARNQSDI DHIMIDLDGT INKSKLGANA ILSVSLAVAK 

       130        140        150        160        170        180 
AAAASKRMPL YAHIAEINET PGVFSMPLPM INIINGGKHA NNNIDIQEFM IQPISAKTVK 

       190        200        210        220        230        240 
ESIRIGCEIF HALGELLKEK GMSTTVGDEG GYAPNLKSNE EALNIIQDAI QKTKYKLGQD 

       250        260        270        280        290        300 
IRLAIDCAAS ELYNKNEKKY NLKGENISFS SKEFTHYLEK LSQKYPIVSI EDGQDESDWE 

       310        320        330        340        350        360 
GFLYQTHVLG NKIQLVGDDL FVTNKNILKK GIKKGIANSI LIKLNQIGTL TETLEAIKTA 

       370        380        390        400        410        420 
KQANYGVIIS HRSGETEDAS IADLSVGTSS GQIKTGSMSR SDRTSKYNQL IRIEENLGTK 

       430 
YAPFHGLREI KSAF 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB13115.1.
RefSeqNP_240229.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57492.
SMRP57492. Positions 2-431.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP57492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13115; BAB13115; BAB13115.
GeneID1109765.
KEGGbuc:BU417.
PATRIC21244374. VBIBucAph127364_0426.

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
KOK01689.
OMAHANWQGA.
OrthoDBEOG65J589.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-417-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_BUCAI
AccessionPrimary (citable) accession number: P57492
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 11, 2014
This is version 94 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names