CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035858
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Enolase 
Protein Synonyms/Alias
 2-phospho-D-glycerate hydro-lyase; 2-phosphoglycerate dehydratase 
Gene Name
 eno 
Gene Synonyms/Alias
 EAM_2703 
Created Date
 July 27, 2013 
Organism
 Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3) 
NCBI Taxa ID
 716540 
Lysine Modification
Position
Peptide
Type
References
257SEFYKDGKYVLAGEGacetylation[1]
266VLAGEGNKAFSSEEFacetylation[1]
342IANSILIKFNQIGSLacetylation[1]
357TETLAAIKMAKDAGYacetylation[1]
Reference
 [1] Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.
 Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y.
 J Proteomics. 2013 Feb 21;79:60-71. [PMID: 23234799
Functional Description
 Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). 
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 (By similarity).
 METAL 290 290 Magnesium (By similarity).
 METAL 317 317 Magnesium (By similarity).
 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 284 284 Phosphotyrosine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 431 AA 
Protein Sequence
MSKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGLAAAPSG ASTGSREALE LRDGDKSRFL 60
GKGVTKAVGA VNGPIAEAVT GKDAKDQANI DKIMIDLDGT ENKSKFGANA ILAVSLAAAK 120
AAAAAKGMPL YEHIAELNGT AGKFSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLK 180
EAVRIGSEVF HNLAKVLKSK GMSTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD 240
VTLAMDCAAS EFYKDGKYVL AGEGNKAFSS EEFTHFLEDL TKQYPIVSIE DGLDESDWDG 300
FAYQTKVLGD KIQLVGDDLF VTNTRILKEG IDKGIANSIL IKFNQIGSLT ETLAAIKMAK 360
DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS DRVAKYNQLI RIEEALGNRA 420
PFNGLKEVKG Q 431 
Gene Ontology
 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0004634; F:phosphopyruvate hydratase activity; IEA:HAMAP.
 GO:0006096; P:glycolysis; IEA:HAMAP. 
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.