P0A6P9 (ENO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase

Gene names

Name:	eno
Ordered Locus Names:	b2779, JW2750

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.11 Ref.12
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Enzyme regulation	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. HAMAP-Rule MF_00318
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318
Subunit structure	Homodimer. Interacts with the C-terminal region of the endoribonuclease RNase E in the RNA degradosome. Ref.15
Subcellular location	Cytoplasm › 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 bacterial cell surface. Ref.13
Post-translational modification	Phosphorylated on serine residue(s). Ref.8
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Cytoskeleton Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from mutant phenotype PubMed 410789. Source: EcoliWiki
Cellular_component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from direct assay Ref.16. Source: EcoliWiki phosphopyruvate hydratase activity Inferred from direct assay PubMed 4942326. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-368855,EBI-368855
rne	P21513	15	EBI-368855,EBI-549958

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6 Ref.7

Chain

2 – 432

431

Enolase HAMAP-Rule MF_00318

PRO_0000133882

Regions

Region

369 – 372

4

Substrate binding By similarity

Sites

Active site

209

1

Proton donor By similarity

Active site

342

1

Proton acceptor By similarity

Metal binding

246

1

Magnesium

Metal binding

290

1

Magnesium

Metal binding

317

1

Magnesium

Binding site

159

1

Substrate By similarity

Binding site

168

1

Substrate By similarity

Binding site

290

1

Substrate By similarity

Binding site

317

1

Substrate By similarity

Binding site

342

1

Substrate (covalent); in inhibited form

Binding site

393

1

Substrate By similarity

Site

34

1

Interaction with RNase E

Site

120

1

Interaction with RNase E

Site

376

1

Interaction with RNase E

Site

408

1

Interaction with RNase E

Amino acid modifications

Modified residue

257

1

N6-acetyllysine Ref.14

Modified residue

284

1

Phosphotyrosine By similarity

Experimental info

Mutagenesis

168

1

E → Q: 5% activity; not secreted. Ref.10

Mutagenesis

209

1

E → Q: 1% activity; not secreted. Ref.10

Mutagenesis

342

1

K → A, Q or R: 1% activity; not secreted. Ref.10

Mutagenesis

342

1

K → E: 94% activity; not secreted. Ref.10

Sequence conflict

102

1

N → K in CAA57795. Ref.1

Sequence conflict

102

1

N → K in AAA24486. Ref.1

Sequence conflict

220

1

A → D in CAA57795. Ref.1

Sequence conflict

339

1

I → Y in CAA57795. Ref.1

Sequence conflict

421 – 432

12

PYNGR…IKGQA → RTTVVKRSKARHKTDFI in CAA57795. Ref.1

Secondary structure

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432

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Beta strand

19 – 27

9

Beta strand

32 – 36

5

Beta strand

45 – 47

3

Helix

59 – 61

3

Helix

65 – 72

8

Helix

74 – 79

6

Helix

87 – 98

12

Beta strand

100 – 103

4

Turn

104 – 106

3

Helix

108 – 125

18

Helix

130 – 137

8

Beta strand

151 – 155

5

Helix

157 – 159

3

Beta strand

160 – 163

4

Beta strand

166 – 172

7

Helix

179 – 199

21

Helix

219 – 232

14

Turn

238 – 240

3

Beta strand

241 – 246

6

Helix

249 – 252

4

Beta strand

257 – 259

3

Helix

261 – 263

3

Beta strand

264 – 268

5

Helix

270 – 283

14

Beta strand

286 – 291

6

Helix

298 – 308

11

Turn

309 – 311

3

Beta strand

312 – 317

6

Turn

318 – 322

5

Helix

324 – 332

9

Beta strand

337 – 341

5

Helix

343 – 345

3

Helix

349 – 361

13

Beta strand

365 – 369

5

Helix

379 – 386

8

Beta strand

390 – 393

4

Helix

400 – 416

17

Helix

417 – 419

3

Helix

424 – 427

4

Sequences

	Sequence		Length	Mass (Da)
	P0A6P9 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0569036E87471B91	FASTA	432	45,655
	10 20 30 40 50 60 MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL 70 80 90 100 110 120 GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT ENKSKFGANA ILAVSLANAK 130 140 150 160 170 180 AAAAAKGMPL YEHIAELNGT PGKYSMPVPM MNIINGGEHA DNNVDIQEFM IQPVGAKTVK 190 200 210 220 230 240 EAIRMGSEVF HHLAKVLKAK GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD 250 260 270 280 290 300 ITLAMDCAAS EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG 310 320 330 340 350 360 FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT ETLAAIKMAK 370 380 390 400 410 420 DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS DRVAKYNQLI RIEEALGEKA 430 PYNGRKEIKG QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Klein M., Freudl R. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / JM109 / ATCC 53323.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase." Weng M., Makaroff C.A., Zalkin H. J. Biol. Chem. 261:5568-5574(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
[5]	"A DEAD-box RNA helicase in the Escherichia coli RNA degradosome." Py B., Higgins C.F., Krisch H.M., Carpousis A.J. Nature 381:169-172(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION IN DEGRADOSOME.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Phosphorylation of Escherichia coli enolase." Dannelly H.K., Duclos B., Cozzone A.J., Reeves H.C. Biochimie 71:1095-1100(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY CHARACTERIZATION, PHOSPHORYLATION. Strain: K12 / JA200.
[9]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[10]	"Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?" Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S., Giard J.-C., Hartke A., Auffray Y., Deutscher J. J. Mol. Biol. 337:485-496(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE BINDING AT LYS-342, INACTIVATION, SECRETION OF SUBSTRATE-BOUND ENOLASE, MUTAGENESIS OF GLU-168; GLU-209 AND LYS-342.
[11]	"Global analysis of Escherichia coli RNA degradosome function using DNA microarrays." Bernstein J.A., Lin P.-H., Cohen S.N., Lin-Chao S. Proc. Natl. Acad. Sci. U.S.A. 101:2758-2763(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN MRNA TURNOVER.
[12]	"Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli." Morita T., Kawamoto H., Mizota T., Inada T., Aiba H. Mol. Microbiol. 54:1063-1075(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN THE DECAY OF GLUCOSE TRANSPORTER MRNA. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[13]	"RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton." Taghbalout A., Rothfield L. Proc. Natl. Acad. Sci. U.S.A. 104:1667-1672(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: PB103.
[14]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[15]	"Crystal structure of the Escherichia coli RNA degradosome component enolase." Kuhnel K., Luisi B.F. J. Mol. Biol. 313:583-592(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.
[16]	"Recognition of enolase in the Escherichia coli RNA degradosome." Chandran V., Luisi B.F. J. Mol. Biol. 358:8-15(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

NOEC. G65059.

RefSeq

NP_417259.1. NC_000913.2.
YP_490987.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A6P9.

SMR

P0A6P9. Positions 2-431.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31847N.

IntAct

P0A6P9. 31 interactions.

MINT

MINT-1230935.

STRING

511145.b2779.

PTM databases

PhosSite

P010423.

2D gel databases

SWISS-2DPAGE

P0A6P9.

Proteomic databases

PaxDb

P0A6P9.

PRIDE

P0A6P9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75821; AAC75821; b2779.
BAE76853; BAE76853; BAE76853.

GeneID

12933303.
945032.

KEGG

ecj:Y75_p2716.
eco:b2779.

PATRIC

32120974. VBIEscCol129921_2879.

Organism-specific databases

EchoBASE

EB0254.

EcoGene

EG10258. eno.

Phylogenomic databases

eggNOG

COG0148.

HOGENOM

HOG000072173.

KO

K01689.

OMA

EYMIMPL.

ProtClustDB

PRK00077.

Enzyme and pathway databases

BioCyc

EcoCyc:ENOLASE-MONOMER.
ECOL316407:JW2750-MONOMER.
MetaCyc:ENOLASE-MONOMER.

BRENDA

4.2.1.11. 2026.

SABIO-RK

P0A6P9.

UniPathway

UPA00109; UER00187.

Gene expression databases

Genevestigator

P0A6P9.

Family and domain databases

HAMAP

MF_00318. Enolase.

InterPro

IPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]

PANTHER

PTHR11902. PTHR11902. 1 hit.

Pfam

PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6P9.

Entry information

Entry name

ENO_ECOLI

Accession

Primary (citable) accession number: P0A6P9
Secondary accession number(s): P08324, Q2MA53

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program