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Q87WD5 (ENO2_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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 2

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2
2-phosphoglycerate dehydratase 2
Gene names
Name:eno2
Synonyms:eno-2
Ordered Locus Names:PSPTO_4616
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length427 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 MF_00318

Catalytic activity

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

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP 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 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: UniProtKB-KW

   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: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Enolase 2 HAMAP MF_00318
PRO_0000133952

Regions

Region366 – 3694Substrate binding By similarity

Sites

Active site2071Proton donor By similarity
Active site3391Proton acceptor By similarity
Metal binding2441Magnesium By similarity
Metal binding2871Magnesium By similarity
Metal binding3141Magnesium By similarity
Binding site1561Substrate By similarity
Binding site1661Substrate 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
Q87WD5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 49D061CB165A93F2

FASTA42746,023
        10         20         30         40         50         60 
MKTQIQAIHA REILDSRGNP TVEVDVTLEC GAMGRASVPS GASTGAHEAV ELRDKDTQRY 

        70         80         90        100        110        120 
SGKGVLKAVS NVNTEILESV RGMNAIDQEQ IDHLMIKLDG TSDKSRLGGN AILGVSLAVA 

       130        140        150        160        170        180 
RAAASALNLP LFQYLGGEQA ARMPVPMFNI LNGGVHANWQ GPDFQEFMIA PTGAGSFKEA 

       190        200        210        220        230        240 
LRWGSEVYHE LKAVLKDAGY STAVGDEGGF APALKKNSDA IELIIKAIER AGYTPGSQIE 

       250        260        270        280        290        300 
IAIDPASSGF YENGLYHLRS EGRKVDAQEL INLYSSWVDK YPIAVLEDGL AEDDWSGWKL 

       310        320        330        340        350        360 
LNAALGDRIE LVGDDLFVTN VERIQRGITE NVANAVLIKP NQIGTLTETK AAIEMAYGAN 

       370        380        390        400        410        420 
WGAMVSHRSG ETVDSSIADL TVAMGTGHLK TGAPCRGERV EKYNQFLRIE EDLGSRAFYA 


GHDAFVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO58062.1.
RefSeqNP_794367.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ87WD5.
SMRQ87WD5. Positions 3-427.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1186299.
GenomeReviewsGene locus PSPTO_4616 in contig AE016853_GR.
KEGGpst:PSPTO_4616.
NMPDRfig|223283.1.peg.4505.
PATRIC20000744. VBIPseSyr93040_4730.
TIGRPSPTO_4616.

Phylogenomic databases

HOGENOMHBG726599.
OMATNVERIQ.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycPSYR223283:PSPTO_4616-MONOMER.

Family and domain databases

HAMAPMF_00318. Enolase.
[Tree]
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 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 nameENO2_PSESM
AccessionPrimary (citable) accession number: Q87WD5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 69 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