UniProtKB - P0A6P9 (ENO_ECOLI)
Enolase
eno
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 PublicationsCatalytic activityi
- EC:4.2.1.11UniRule annotation1 Publication
Cofactori
Activity regulationi
pH dependencei
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 159 | SubstrateUniRule annotation | 1 | |
Binding sitei | 168 | SubstrateUniRule annotation | 1 | |
Active sitei | 209 | Proton donorUniRule annotation1 Publication | 1 | |
Metal bindingi | 246 | Magnesium2 Publications | 1 | |
Metal bindingi | 290 | Magnesium2 Publications | 1 | |
Binding sitei | 290 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 317 | Magnesium2 Publications | 1 | |
Binding sitei | 317 | SubstrateUniRule annotation | 1 | |
Active sitei | 342 | Proton acceptorUniRule annotation1 Publication | 1 | |
Binding sitei | 342 | Substrate; covalent; in inhibited form1 Publication | 1 | |
Binding sitei | 393 | SubstrateUniRule annotation | 1 |
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 function | Lyase |
Biological process | Glycolysis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:ENOLASE-MONOMER |
BRENDAi | 4.2.1.11, 2026 |
SABIO-RKi | P0A6P9 |
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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
Cytoskeleton
Other locations
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.
Cytoskeleton
- cytoskeleton Source: EcoCyc
Cytosol
- bacterial degradosome Source: ComplexPortal
- cytosol Source: EcoCyc
- phosphopyruvate hydratase complex Source: CAFA
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- cell surface Source: UniProtKB-SubCell
- membrane Source: ComplexPortal
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 168 | E → Q: 5% activity; not secreted. 1 Publication | 1 | |
Mutagenesisi | 209 | E → Q: 1% activity; not secreted. 1 Publication | 1 | |
Mutagenesisi | 342 | K → A, Q or R: 1% activity; not secreted. 1 Publication | 1 | |
Mutagenesisi | 342 | K → E: 94% activity; not secreted. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed3 Publications | |||
ChainiPRO_0000133882 | 2 – 432 | EnolaseAdd BLAST | 431 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 257 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 342 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, HydroxylationProteomic databases
jPOSTi | P0A6P9 |
PaxDbi | P0A6P9 |
PRIDEi | P0A6P9 |
2D gel databases
SWISS-2DPAGEi | P0A6P9 |
PTM databases
CarbonylDBi | P0A6P9 |
iPTMneti | P0A6P9 |
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 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 120 | Interaction with RNase E2 Publications | 1 | |
Sitei | 376 | Interaction with RNase E2 Publications | 1 | |
Sitei | 408 | Interaction with RNase E2 Publications | 1 |
Binary interactionsi
P0A6P9
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-368855,EBI-368855 |
rne [P21513] | 17 | EBI-368855,EBI-549958 |
rpe [P0AG07] | 3 | EBI-368855,EBI-546020 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4262297, 354 interactors |
ComplexPortali | CPX-403, RNA degradosome |
DIPi | DIP-31847N |
IntActi | P0A6P9, 38 interactors |
STRINGi | 511145.b2779 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A6P9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6P9 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 5 – 34 | Interaction with RNase EAdd BLAST | 30 | |
Regioni | 369 – 372 | Substrate bindingUniRule annotation | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0148, Bacteria |
HOGENOMi | CLU_031223_2_1_6 |
InParanoidi | P0A6P9 |
PhylomeDBi | P0A6P9 |
Family and domain databases
CDDi | cd03313, enolase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
HAMAPi | MF_00318, Enolase, 1 hit |
InterProi | View protein in InterPro IPR000941, Enolase IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR020810, Enolase_C IPR020809, Enolase_CS IPR020811, Enolase_N |
PANTHERi | PTHR11902, PTHR11902, 1 hit |
Pfami | View protein in Pfam PF00113, Enolase_C, 1 hit PF03952, Enolase_N, 1 hit |
PIRSFi | PIRSF001400, Enolase, 1 hit |
PRINTSi | PR00148, ENOLASE |
SFLDi | SFLDF00002, enolase, 1 hit |
SMARTi | View protein in SMART SM01192, Enolase_C, 1 hit SM01193, Enolase_N, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01060, eno, 1 hit |
PROSITEi | View protein in PROSITE PS00164, ENOLASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 102 | N → K in CAA57795 (Ref. 1) Curated | 1 | |
Sequence conflicti | 102 | N → K in AAA24486 (Ref. 1) Curated | 1 | |
Sequence conflicti | 220 | A → D in CAA57795 (Ref. 1) Curated | 1 | |
Sequence conflicti | 339 | I → Y in CAA57795 (Ref. 1) Curated | 1 | |
Sequence conflicti | 421 – 432 | PYNGR…IKGQA → RTTVVKRSKARHKTDFI in CAA57795 (Ref. 1) CuratedAdd BLAST | 12 |
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 |
PIRi | G65059, NOEC |
RefSeqi | NP_417259.1, NC_000913.3 WP_000036723.1, NZ_STEB01000030.1 |
Genome annotation databases
EnsemblBacteriai | AAC75821; AAC75821; b2779 BAE76853; BAE76853; BAE76853 |
GeneIDi | 67413943 945032 |
KEGGi | ecj:JW2750 eco:b2779 |
PATRICi | fig|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 |
PIRi | G65059, NOEC |
RefSeqi | NP_417259.1, NC_000913.3 WP_000036723.1, NZ_STEB01000030.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1E9I | X-ray | 2.48 | A/B/C/D | 2-432 | [»] | |
2FYM | X-ray | 1.60 | A/C/D/F | 2-432 | [»] | |
3H8A | X-ray | 1.90 | A/B/C/D | 1-432 | [»] | |
5OHG | X-ray | 2.00 | A/B/H/I | 1-432 | [»] | |
6BFY | X-ray | 1.81 | A/B/C/D/E/F | 1-432 | [»] | |
6BFZ | X-ray | 2.21 | A/B/C/D/E/F | 1-432 | [»] | |
6D3Q | X-ray | 2.24 | A/B/C/D/E/F | 1-432 | [»] | |
6NPF | X-ray | 2.57 | A/B/C/D/E/F | 1-432 | [»] | |
SMRi | P0A6P9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262297, 354 interactors |
ComplexPortali | CPX-403, RNA degradosome |
DIPi | DIP-31847N |
IntActi | P0A6P9, 38 interactors |
STRINGi | 511145.b2779 |
PTM databases
CarbonylDBi | P0A6P9 |
iPTMneti | P0A6P9 |
2D gel databases
SWISS-2DPAGEi | P0A6P9 |
Proteomic databases
jPOSTi | P0A6P9 |
PaxDbi | P0A6P9 |
PRIDEi | P0A6P9 |
Genome annotation databases
EnsemblBacteriai | AAC75821; AAC75821; b2779 BAE76853; BAE76853; BAE76853 |
GeneIDi | 67413943 945032 |
KEGGi | ecj:JW2750 eco:b2779 |
PATRICi | fig|1411691.4.peg.3956 |
Organism-specific databases
EchoBASEi | EB0254 |
Phylogenomic databases
eggNOGi | COG0148, Bacteria |
HOGENOMi | CLU_031223_2_1_6 |
InParanoidi | P0A6P9 |
PhylomeDBi | P0A6P9 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00187 |
BioCyci | EcoCyc:ENOLASE-MONOMER |
BRENDAi | 4.2.1.11, 2026 |
SABIO-RKi | P0A6P9 |
Miscellaneous databases
EvolutionaryTracei | P0A6P9 |
PROi | PR:P0A6P9 |
Family and domain databases
CDDi | cd03313, enolase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
HAMAPi | MF_00318, Enolase, 1 hit |
InterProi | View protein in InterPro IPR000941, Enolase IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR020810, Enolase_C IPR020809, Enolase_CS IPR020811, Enolase_N |
PANTHERi | PTHR11902, PTHR11902, 1 hit |
Pfami | View protein in Pfam PF00113, Enolase_C, 1 hit PF03952, Enolase_N, 1 hit |
PIRSFi | PIRSF001400, Enolase, 1 hit |
PRINTSi | PR00148, ENOLASE |
SFLDi | SFLDF00002, enolase, 1 hit |
SMARTi | View protein in SMART SM01192, Enolase_C, 1 hit SM01193, Enolase_N, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01060, eno, 1 hit |
PROSITEi | View protein in PROSITE PS00164, ENOLASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ENO_ECOLI | |
Accessioni | P0A6P9Primary (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: | February 23, 2022 | |
This is version 149 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families