UniProt Accession

 ENO_ECOLI; P0A6P9; P08324; Q2MA53 

Genbank Protein ID

 X82400; U29580; U00096; AP009048; M12843 

Genbank Nucleotide ID

 CAA57795.1; AAA69289.1; AAC75821.1; BAE76853.1; AAA24486.1 

Protein Name

 Enolase 

Protein Synonyms/Alias

 2-phospho-D-glycerate hydro-lyase; 2-phosphoglycerate dehydratase 

Gene Name

 eno 

Gene Synonyms/Alias

 b2779; JW2750 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
3	*****MSKIVKIIGR	acetylation	[1]
6	**MSKIVKIIGREII	acetylation	[1, 2, 3]
56	LELRDGDKSRFLGKG	acetylation	[1]
62	DKSRFLGKGVTKAVA	acetylation	[1, 3]
66	FLGKGVTKAVAAVNG	acetylation	[1, 3]
82	IAQALIGKDAKDQAG	acetylation	[1, 3]
85	ALIGKDAKDQAGIDK	acetylation	[1, 3]
92	KDQAGIDKIMIDLDG	acetylation	[1, 3]
105	DGTENKSKFGANAIL	acetylation	[1]
120	AVSLANAKAAAAAKG	acetylation	[1]
177	MIQPVGAKTVKEAIR	acetylation	[1]
195	EVFHHLAKVLKAKGM	acetylation	[1, 3]
198	HHLAKVLKAKGMNTA	acetylation	[1]
231	AVIAEAVKAAGYELG	acetylation	[1, 3]
239	AAGYELGKDITLAMD	acetylation	[1, 3]
254	CAASEFYKDGKYVLA	acetylation	[1]
257	SEFYKDGKYVLAGEG	acetylation	[1, 4]
266	VLAGEGNKAFTSEEF	acetylation	[1, 3]
306	DGFAYQTKVLGDKIQ	acetylation	[1]
311	QTKVLGDKIQLVGDD	acetylation	[1, 3]
325	DLFVTNTKILKEGIE	acetylation	[1, 3]
328	VTNTKILKEGIEKGI	acetylation	[1, 3]
333	ILKEGIEKGIANSIL	acetylation	[1]
342	IANSILIKFNQIGSL	acetylation	[1, 2]
357	TETLAAIKMAKDAGY	acetylation	[1]
360	LAAIKMAKDAGYTAV	acetylation	[1]
405	SRSDRVAKYNQLIRI	acetylation	[1]
419	IEEALGEKAPYNGRK	acetylation	[1, 3]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [4] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 

Functional Description

 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. 

Sequence Annotation

 REGION 369 372 Substrate binding (By similarity).
 ACT_SITE 209 209 Proton donor (By similarity).
 ACT_SITE 342 342 Proton acceptor (By similarity).
 METAL 246 246 Magnesium.
 METAL 290 290 Magnesium.
 METAL 317 317 Magnesium.
 BINDING 159 159 Substrate (By similarity).
 BINDING 168 168 Substrate (By similarity).
 BINDING 290 290 Substrate (By similarity).
 BINDING 317 317 Substrate (By similarity).
 BINDING 342 342 Substrate (covalent); in inhibited form.
 BINDING 393 393 Substrate (By similarity).
 MOD_RES 257 257 N6-acetyllysine.
 MOD_RES 284 284 Phosphotyrosine (By similarity).  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Secreted. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 432 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
 GO:0004634; F:phosphopyruvate hydratase activity; IDA:EcoliWiki.
 GO:0006096; P:glycolysis; IMP:EcoliWiki. 

Interpro

 IPR000941; Enolase.
 IPR020810; Enolase_C.
 IPR020809; Enolase_CS.
 IPR020811; Enolase_N. 

Pfam

 PF00113; Enolase_C
 PF03952; Enolase_N 

SMART

  

PROSITE

 PS00164; ENOLASE 

PRINTS

 PR00148; ENOLASE.