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Q0BSX3 (ENO_GRABC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:GbCGDNIH1_1181
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter

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_0000267040

Regions

Region364 – 3674Substrate binding By similarity

Sites

Active site2051Proton donor By similarity
Active site3371Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2851Magnesium By similarity
Metal binding3121Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2851Substrate By similarity
Binding site3121Substrate By similarity
Binding site3371Substrate (covalent); in inhibited form By similarity
Binding site3881Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BSX3 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 61ADDFF558F007E7

FASTA42544,964
        10         20         30         40         50         60 
MAAIADIIAR EILDSRGNPT VEVDVTLESG AQGRAAVPSG ASTGAHEAVE LRDGDKSRYG 

        70         80         90        100        110        120 
GKGVLHAVSF VEGEIFEAIG GMDASEQLRI DETLIAVDGT PNKSRLGANA MLAVSLATAK 

       130        140        150        160        170        180 
AAANHQGVPL YRYLGGVYAR TLPVPMMNIV NGGKHADNPI DIQEFMIQPV AAPTIADAVR 

       190        200        210        220        230        240 
VGAEIFAALK KELSAAGHNT NVGDEGGFAP GLKSAEEALS FITKACEKAG YRPGEDVTFA 

       250        260        270        280        290        300 
LDCAATEFFK DGVYDLEGEG KKFDAAGMVR YLEDLAAKFP IVSIEDGLAE DDWEGWKLLT 

       310        320        330        340        350        360 
DTLGRKVQLV GDDLFVTNPD RLRHGIALGT ANAILVKVNQ IGTLSETLEA VETAHRAGYA 

       370        380        390        400        410        420 
AVMSHRSGET EDSTIADLAV ATNCGQIKTG SLSRSDRTAK YNQLIRIEQD LDTSGRYAGR 


TILRG 

« Hide

References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000394 Genomic DNA. Translation: ABI62079.1.
RefSeqYP_745002.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BSX3.
SMRQ0BSX3. Positions 4-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391165.GbCGDNIH1_1181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI62079; ABI62079; GbCGDNIH1_1181.
GeneID4274672.
KEGGgbe:GbCGDNIH1_1181.
PATRIC22078521. VBIGraBet83793_1230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
KOK01689.
OMARSEIKGQ.
OrthoDBEOG65J589.

Enzyme and pathway databases

BioCycGBET391165:GHON-1215-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_GRABC
AccessionPrimary (citable) accession number: Q0BSX3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 60 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