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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. 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

  • 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.
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

  • 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

  • cell surface Source: UniProtKB-SubCell
  • cytoskeleton Source: EcoCyc
  • cytosol Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • phosphopyruvate hydratase complex Source: CAFA

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

PaxDbiP0A6P9.
PRIDEiP0A6P9.

2D gel databases

SWISS-2DPAGEiP0A6P9.

PTM databases

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262297. 318 interactors.
DIPiDIP-31847N.
IntActiP0A6P9. 38 interactors.
MINTiMINT-1230935.
STRINGi316385.ECDH10B_2946.

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[»]
5OHGX-ray2.00A/B/H/I1-432[»]
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.
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.
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.
SSF54826. SSF54826. 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

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 22, 2017
This is version 122 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. 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