Reviewed, UniProtKB/Swiss-Prot Q8GR70 (ENO_ENTHR)

Names and origin

Protein names

Recommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

Gene names

Name:

eno

Organism

Enterococcus hirae

Taxonomic identifier

1354 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Enzyme regulation	The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm. Secreted. Cell surface. Note= Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface By similarity.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	cell surface Inferred from electronic annotation. Source: HAMAP extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 432

432

Enolase

PRO_0000133886

Regions

Region

367 – 370

4

Substrate binding By similarity

Sites

Active site

205

1

Proton donor By similarity

Active site

340

1

Proton acceptor By similarity

Metal binding

242

1

Magnesium

Metal binding

288

1

Magnesium

Metal binding

315

1

Magnesium

Binding site

155

1

Substrate By similarity

Binding site

164

1

Substrate By similarity

Binding site

288

1

Substrate By similarity

Binding site

315

1

Substrate By similarity

Binding site

340

1

Substrate (covalent); in inhibited form By similarity

Binding site

391

1

Substrate By similarity

Amino acid modifications

Modified residue

282

1

Phosphotyrosine By similarity

Secondary structure

1

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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 – 73

9

Helix

75 – 79

5

Helix

87 – 98

12

Turn

104 – 106

3

Helix

108 – 126

19

Helix

130 – 135

6

Beta strand

147 – 151

5

Helix

153 – 155

3

Beta strand

156 – 159

4

Beta strand

162 – 168

7

Helix

175 – 196

22

Beta strand

204 – 206

3

Beta strand

213 – 215

3

Helix

216 – 229

14

Turn

233 – 236

4

Beta strand

238 – 242

5

Turn

245 – 248

4

Turn

251 – 253

3

Beta strand

255 – 257

3

Turn

259 – 262

4

Helix

268 – 281

14

Beta strand

284 – 289

6

Helix

296 – 306

11

Turn

307 – 309

3

Beta strand

310 – 315

6

Turn

316 – 320

5

Helix

322 – 331

10

Beta strand

337 – 339

3

Helix

341 – 344

4

Helix

347 – 359

13

Beta strand

364 – 367

4

Helix

377 – 384

8

Beta strand

388 – 391

4

Beta strand

395 – 397

3

Helix

398 – 414

17

Helix

415 – 417

3

Helix

422 – 425

4

Sequences

	Sequence		Length	Mass (Da)
	Q8GR70-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 45F203F55685F1C1	FASTA	432	46,411
	10 20 30 40 50 60 MSIITDVYAR EILDSRGNPT IEVEVYTESG AFGRGMVPSG ASTGEYEAVE LRDGDKARYG 70 80 90 100 110 120 GKGVTKAVDN VNNIIAEAII GYDVRDQMAI DKAMIALDGT PNKGKLGANA ILGVSIAVAR 130 140 150 160 170 180 AAADYLEVPL YHYLGGFNTK VLPTPMMNII NGGSHADNSI DFQEFMIMPV GAPTFKEALR 190 200 210 220 230 240 MGAEVFHALA AILKSRGLAT SVGDEGGFAP NLGSNEEGFE VIIEAIEKAG YVPGKDVVLA 250 260 270 280 290 300 MDAASSEFYD KEKGVYVLAD SGEGEKTTDE MIKFYEELVS KYPIISIEDG LDENDWDGFK 310 320 330 340 350 360 KLTDVLGDKV QLVGDDLFVT NTQKLSEGIE KGIANSILIK VNQIGTLTET FEAIEMAKEA 370 380 390 400 410 420 GYTAVVSHRS GETEDSTISD IAVATNAGQI KTGSLSRTDR IAKYNQLLRI EDQLGEVAEY 430 KGLKSFYNLK AA

References

[1]

"Crystal structure of Enterococcus hirae enolase at 2.8 A resolution." Hosaka T., Meguro T., Yamato I., Shirakihara Y. J. Biochem. 133:817-823(2003) [PubMed: 12869539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB091345 Genomic DNA. Translation: BAC16223.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IYX	X-ray	2.80	A/B	1-432	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_00318.
[Tree]

InterPro

IPR000941. Enolase.
[Graphical view]

PANTHER

PTHR11902. Enolase. 1 hit.

Pfam

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

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

ProDom

PD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

BLOCKS

Search...

ProtoNet

Search...

Entry information

Entry name

ENO_ENTHR

Accession

Primary (citable) accession number: Q8GR70

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	March 1, 2003
Last modified:	November 4, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)