Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase

Gene

eno

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  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

  • magnesium ion binding Source: EcoliWiki
  • phosphopyruvate hydratase activity Source: EcoCyc

GO - Biological processi

  • glycolytic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENOLASE-MONOMER.
ECOL316407:JW2750-MONOMER.
MetaCyc:ENOLASE-MONOMER.
BRENDAi4.2.1.11. 2026.
SABIO-RKP0A6P9.
UniPathwayiUPA00109; 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

  • Cytoplasmcytoskeleton
  • 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

  • cell surface Source: UniProtKB-SubCell
  • cytoskeleton Source: EcoCyc
  • cytosol Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • phosphopyruvate hydratase complex Source: InterPro
Complete GO annotation...

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-2DPAGEP0A6P9.

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

WithEntry#Exp.IntActNotes
itself2EBI-368855,EBI-368855
rneP2151315EBI-368855,EBI-549958

Protein-protein interaction databases

BioGridi4262297. 313 interactors.
DIPiDIP-31847N.
IntActiP0A6P9. 31 interactors.
MINTiMINT-1230935.
STRINGi511145.b2779.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 13Combined sources11
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Beta strandi45 – 47Combined sources3
Helixi59 – 61Combined sources3
Helixi65 – 72Combined sources8
Helixi74 – 79Combined sources6
Helixi87 – 98Combined sources12
Beta strandi100 – 103Combined sources4
Turni104 – 106Combined sources3
Helixi108 – 125Combined sources18
Helixi130 – 137Combined sources8
Beta strandi151 – 155Combined sources5
Helixi157 – 159Combined sources3
Beta strandi160 – 163Combined sources4
Beta strandi166 – 172Combined sources7
Helixi179 – 199Combined sources21
Helixi219 – 232Combined sources14
Turni238 – 240Combined sources3
Beta strandi241 – 246Combined sources6
Helixi249 – 252Combined sources4
Beta strandi257 – 259Combined sources3
Helixi261 – 263Combined sources3
Beta strandi264 – 268Combined sources5
Helixi270 – 283Combined sources14
Beta strandi286 – 291Combined sources6
Helixi298 – 308Combined sources11
Turni309 – 311Combined sources3
Beta strandi312 – 317Combined sources6
Turni318 – 322Combined sources5
Helixi324 – 332Combined sources9
Beta strandi337 – 341Combined sources5
Helixi343 – 345Combined sources3
Helixi349 – 361Combined sources13
Beta strandi365 – 369Combined sources5
Helixi379 – 386Combined sources8
Beta strandi390 – 393Combined sources4
Helixi400 – 416Combined sources17
Helixi417 – 419Combined sources3
Helixi424 – 427Combined sources4

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[»]
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.
OMAiEFMIIPV.
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.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

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.
PATRICi32120974. VBIEscCol129921_2879.

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[»]
ProteinModelPortaliP0A6P9.
SMRiP0A6P9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262297. 313 interactors.
DIPiDIP-31847N.
IntActiP0A6P9. 31 interactors.
MINTiMINT-1230935.
STRINGi511145.b2779.

2D gel databases

SWISS-2DPAGEP0A6P9.

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.
PATRICi32120974. VBIEscCol129921_2879.

Organism-specific databases

EchoBASEiEB0254.
EcoGeneiEG10258. eno.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072173.
InParanoidiP0A6P9.
KOiK01689.
OMAiEFMIIPV.
PhylomeDBiP0A6P9.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciEcoCyc:ENOLASE-MONOMER.
ECOL316407:JW2750-MONOMER.
MetaCyc:ENOLASE-MONOMER.
BRENDAi4.2.1.11. 2026.
SABIO-RKP0A6P9.

Miscellaneous databases

EvolutionaryTraceiP0A6P9.
PROiP0A6P9.

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.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENO_ECOLI
AccessioniPrimary (citable) accession number: P0A6P9
Secondary accession number(s): P08324, Q2MA53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.