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Protein

Enolase

Gene

eno

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.UniRule annotation3 Publications

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation2 PublicationsNote: Mg2+ is required for catalysis and for stabilizing the dimer.UniRule annotation2 Publications

Activity regulationi

The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Inhibited by fluoride ion.2 Publications

pH dependencei

Optimum pH is 8.1.1 Publication

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), Probable phosphoglycerate mutase GpmB (gpmB)
  4. Enolase (eno)
  5. Pyruvate kinase I (pykF), Pyruvate kinase II (pykA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei159SubstrateUniRule annotation1
Binding sitei168SubstrateUniRule annotation1
Active sitei209Proton donorUniRule annotation1
Metal bindingi246Magnesium1
Metal bindingi290Magnesium1
Binding sitei290SubstrateUniRule annotation1
Metal bindingi317Magnesium1
Binding sitei317SubstrateUniRule annotation1
Active sitei342Proton acceptorUniRule annotation1
Binding sitei342Substrate (covalent); in inhibited form1
Binding sitei393SubstrateUniRule annotation1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • magnesium ion binding Source: EcoliWiki
  • phosphopyruvate hydratase activity Source: CAFA

GO - Biological processi

  • glycolytic process Source: EcoliWiki

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENOLASE-MONOMER
MetaCyc:ENOLASE-MONOMER
BRENDAi4.2.1.11 2026
SABIO-RKiP0A6P9
UniPathwayi
UPA00109;UER00187

Names & Taxonomyi

Protein namesi
Recommended name:
EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseUniRule annotation
2-phosphoglycerate dehydrataseUniRule annotation
Gene namesi
Name:enoUniRule annotation
Ordered Locus Names:b2779, JW2750
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10258 eno

Subcellular locationi

  • cytoskeleton
  • Secreted
  • Cell surface
  • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the cell surface.

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi168E → Q: 5% activity; not secreted. 1 Publication1
Mutagenesisi209E → Q: 1% activity; not secreted. 1 Publication1
Mutagenesisi342K → A, Q or R: 1% activity; not secreted. 1 Publication1
Mutagenesisi342K → E: 94% activity; not secreted. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001338822 – 432EnolaseAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei257N6-acetyllysine1 Publication1

Post-translational modificationi

Phosphorylated on serine residue(s).1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A6P9
PaxDbiP0A6P9
PRIDEiP0A6P9

2D gel databases

SWISS-2DPAGEiP0A6P9

PTM databases

CarbonylDBiP0A6P9
iPTMnetiP0A6P9

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with the C-terminal region of the endoribonuclease RNase E. Homodimer.UniRule annotation7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Interaction with RNase E1
Sitei376Interaction with RNase E1
Sitei408Interaction with RNase E1

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4262297, 354 interactors
ComplexPortaliCPX-403 Degradosome
DIPiDIP-31847N
IntActiP0A6P9, 38 interactors
STRINGi316385.ECDH10B_2946

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A6P9
SMRiP0A6P9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6P9

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni5 – 34Interaction with RNase EAdd BLAST30
Regioni369 – 372Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
HOGENOMiHOG000072173
InParanoidiP0A6P9
KOiK01689
PhylomeDBiP0A6P9

Family and domain databases

CDDicd03313 enolase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SFLDiSFLDG00178 enolase, 1 hit
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6P9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE
60 70 80 90 100
LRDGDKSRFL GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT
110 120 130 140 150
ENKSKFGANA ILAVSLANAK AAAAAKGMPL YEHIAELNGT PGKYSMPVPM
160 170 180 190 200
MNIINGGEHA DNNVDIQEFM IQPVGAKTVK EAIRMGSEVF HHLAKVLKAK
210 220 230 240 250
GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD ITLAMDCAAS
260 270 280 290 300
EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG
310 320 330 340 350
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT
360 370 380 390 400
ETLAAIKMAK DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS
410 420 430
DRVAKYNQLI RIEEALGEKA PYNGRKEIKG QA
Length:432
Mass (Da):45,655
Last modified:January 23, 2007 - v2
Checksum:i0569036E87471B91
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102N → K in CAA57795 (Ref. 1) Curated1
Sequence conflicti102N → K in AAA24486 (Ref. 1) Curated1
Sequence conflicti220A → D in CAA57795 (Ref. 1) Curated1
Sequence conflicti339I → Y in CAA57795 (Ref. 1) Curated1
Sequence conflicti421 – 432PYNGR…IKGQA → RTTVVKRSKARHKTDFI in CAA57795 (Ref. 1) CuratedAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82400 Genomic DNA Translation: CAA57795.1
U29580 Genomic DNA Translation: AAA69289.1
U00096 Genomic DNA Translation: AAC75821.1
AP009048 Genomic DNA Translation: BAE76853.1
M12843 mRNA Translation: AAA24486.1
PIRiG65059 NOEC
RefSeqiNP_417259.1, NC_000913.3
WP_000036723.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75821; AAC75821; b2779
BAE76853; BAE76853; BAE76853
GeneIDi945032
KEGGiecj:JW2750
eco:b2779
PATRICifig|1411691.4.peg.3956

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82400 Genomic DNA Translation: CAA57795.1
U29580 Genomic DNA Translation: AAA69289.1
U00096 Genomic DNA Translation: AAC75821.1
AP009048 Genomic DNA Translation: BAE76853.1
M12843 mRNA Translation: AAA24486.1
PIRiG65059 NOEC
RefSeqiNP_417259.1, NC_000913.3
WP_000036723.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E9IX-ray2.48A/B/C/D2-432[»]
2FYMX-ray1.60A/C/D/F2-432[»]
3H8AX-ray1.90A/B/C/D1-432[»]
5OHGX-ray2.00A/B/H/I1-432[»]
ProteinModelPortaliP0A6P9
SMRiP0A6P9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262297, 354 interactors
ComplexPortaliCPX-403 Degradosome
DIPiDIP-31847N
IntActiP0A6P9, 38 interactors
STRINGi316385.ECDH10B_2946

PTM databases

CarbonylDBiP0A6P9
iPTMnetiP0A6P9

2D gel databases

SWISS-2DPAGEiP0A6P9

Proteomic databases

EPDiP0A6P9
PaxDbiP0A6P9
PRIDEiP0A6P9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75821; AAC75821; b2779
BAE76853; BAE76853; BAE76853
GeneIDi945032
KEGGiecj:JW2750
eco:b2779
PATRICifig|1411691.4.peg.3956

Organism-specific databases

EchoBASEiEB0254
EcoGeneiEG10258 eno

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
HOGENOMiHOG000072173
InParanoidiP0A6P9
KOiK01689
PhylomeDBiP0A6P9

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00187

BioCyciEcoCyc:ENOLASE-MONOMER
MetaCyc:ENOLASE-MONOMER
BRENDAi4.2.1.11 2026
SABIO-RKiP0A6P9

Miscellaneous databases

EvolutionaryTraceiP0A6P9
PROiPR:P0A6P9

Family and domain databases

CDDicd03313 enolase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SFLDiSFLDG00178 enolase, 1 hit
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiENO_ECOLI
AccessioniPrimary (citable) accession number: P0A6P9
Secondary accession number(s): P08324, Q2MA53
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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Main funding by: National Institutes of Health

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