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 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:

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	Length
Binding siteⁱ	159	SubstrateUniRule annotation	1
Binding siteⁱ	168	SubstrateUniRule annotation	1
Active siteⁱ	209	Proton donorUniRule annotation	1
Metal bindingⁱ	246	Magnesium	1
Metal bindingⁱ	290	Magnesium	1
Binding siteⁱ	290	SubstrateUniRule annotation	1
Metal bindingⁱ	317	Magnesium	1
Binding siteⁱ	317	SubstrateUniRule annotation	1
Active siteⁱ	342	Proton acceptorUniRule annotation	1
Binding siteⁱ	342	Substrate (covalent); in inhibited form	1
Binding siteⁱ	393	SubstrateUniRule annotation	1

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 15236960
- 16858726
magnesium ion binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 16516921
phosphopyruvate hydratase activity
Source: CAFA
Inferred from direct assayⁱ
- 15236960

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glycolytic process
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 410789

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Glycolysis
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ENOLASE-MONOMER MetaCyc: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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10258 eno

EcoGeneⁱ

EG10258 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
Inferred from physical interactionⁱ
- 17242352
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
extracellular region Source: UniProtKB-SubCell
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726
phosphopyruvate hydratase complex
Source: CAFA
Inferred from direct assayⁱ
- 15236960

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

Post-translational modificationⁱ

Phosphorylated on serine residue(s).1 Publication

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	P0A6P9
PaxDbⁱ	P0A6P9
PRIDEⁱ	P0A6P9

2D gel databases

SWISS-2DPAGEⁱ	P0A6P9

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 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	120	Interaction with RNase E	1
Siteⁱ	376	Interaction with RNase E	1
Siteⁱ	408	Interaction with RNase E	1

Binary interactionsⁱ

With	Entry	#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
Inferred from physical interactionⁱ
- 15236960
- 16858726

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4262297, 354 interactors
ComplexPortalⁱ	CPX-403 Degradosome
Database of interacting proteins More...DIPⁱ	DIP-31847N
IntActⁱ	P0A6P9, 38 interactors
STRINGⁱ	316385.ECDH10B_2946

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 13	Combined sources	11
Beta strandⁱ	19 – 27	Combined sources	9
Beta strandⁱ	32 – 36	Combined sources	5
Beta strandⁱ	45 – 47	Combined sources	3
Helixⁱ	59 – 61	Combined sources	3
Helixⁱ	65 – 72	Combined sources	8
Helixⁱ	74 – 79	Combined sources	6
Helixⁱ	87 – 98	Combined sources	12
Beta strandⁱ	100 – 103	Combined sources	4
Turnⁱ	104 – 106	Combined sources	3
Helixⁱ	108 – 125	Combined sources	18
Helixⁱ	130 – 137	Combined sources	8
Beta strandⁱ	151 – 155	Combined sources	5
Helixⁱ	157 – 159	Combined sources	3
Beta strandⁱ	160 – 163	Combined sources	4
Beta strandⁱ	166 – 172	Combined sources	7
Helixⁱ	179 – 199	Combined sources	21
Beta strandⁱ	210 – 212	Combined sources	3
Helixⁱ	219 – 232	Combined sources	14
Turnⁱ	238 – 240	Combined sources	3
Beta strandⁱ	241 – 246	Combined sources	6
Helixⁱ	249 – 252	Combined sources	4
Beta strandⁱ	257 – 259	Combined sources	3
Helixⁱ	261 – 263	Combined sources	3
Beta strandⁱ	264 – 268	Combined sources	5
Helixⁱ	270 – 283	Combined sources	14
Beta strandⁱ	286 – 291	Combined sources	6
Helixⁱ	298 – 308	Combined sources	11
Turnⁱ	309 – 311	Combined sources	3
Beta strandⁱ	312 – 317	Combined sources	6
Turnⁱ	318 – 322	Combined sources	5
Helixⁱ	324 – 332	Combined sources	9
Beta strandⁱ	337 – 341	Combined sources	5
Helixⁱ	343 – 345	Combined sources	3
Helixⁱ	349 – 361	Combined sources	13
Beta strandⁱ	365 – 369	Combined sources	5
Helixⁱ	379 – 386	Combined sources	8
Beta strandⁱ	390 – 393	Combined sources	4
Helixⁱ	400 – 416	Combined sources	17
Helixⁱ	417 – 419	Combined sources	3
Helixⁱ	424 – 427	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A6P9
SMRⁱ	P0A6P9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P0A6P9

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

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C70 Bacteria COG0148 LUCA
HOGENOMⁱ	HOG000072173
InParanoidⁱ	P0A6P9
KEGG Orthology (KO) More...KOⁱ	K01689
OMAⁱ	EFMIIPV
PhylomeDBⁱ	P0A6P9

Family and domain databases

Conserved Domains Database More...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 IPR034390 Enolase-like_superfamily IPR020810 Enolase_C IPR020809 Enolase_CS IPR020811 Enolase_N
PANTHERⁱ	PTHR11902 PTHR11902, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00113 Enolase_C, 1 hit PF03952 Enolase_N, 1 hit
PIRSFⁱ	PIRSF001400 Enolase, 1 hit
PRINTSⁱ	PR00148 ENOLASE
SFLDⁱ	SFLDG00178 enolase, 1 hit SFLDS00001 Enolase, 1 hit
SMARTⁱ	View protein in SMART SM01192 Enolase_C, 1 hit SM01193 Enolase_N, 1 hit
SUPFAMⁱ	SSF51604 SSF51604, 1 hit
TIGRFAMsⁱ	TIGR01060 eno, 1 hit
PROSITEⁱ	View 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]FASTA Add 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 key	Position(s)	DescriptionActions	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
NCBI Reference Sequences More...RefSeqⁱ	NP_417259.1, NC_000913.3 WP_000036723.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75821; AAC75821; b2779 BAE76853; BAE76853; BAE76853
GeneIDⁱ	945032
KEGGⁱ	ecj:JW2750 eco:b2779
PATRICⁱ	fig\|1411691.4.peg.3956

Protein	Similar proteins		Species	Score	Length	Source
P0A6P9	Enolase		ECO24		432	UniRef100_A7ZQM2
Enolase		ECO27		432
Enolase		ECO45		432
Enolase		ECO55		432
Enolase		ECO57		432
+202

Protein	Similar proteins		Species	Score	Length	Source
P0A6P9	Enolase		PHOLL		433	UniRef90_Q7N835
Enolase		EDWI9		433
Enolase		PROMH		433
Enolase		SODGM		433
Enolase		ECO24		432
+949

Protein	Similar proteins		Species	Score	Length	Source
P0A6P9	Enolase		PHOLL		433	UniRef50_Q7N835
Enolase		SODGM		433
Enolase		PROMH		433
Enolase		EDWI9		433
Enolase		SHISS		432
+1266

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:	September 12, 2018
	This is version 127 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, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A6P9 (ENO_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Enolase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Sites

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

pH dependenceⁱ

Pathwayⁱ: glycolysis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ