CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006807
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
 BSU33900 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
255FYNKEDGKYHLSGEGacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
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 366 369 Substrate binding (By similarity).
 ACT_SITE 205 205 Proton donor (By similarity).
 ACT_SITE 339 339 Proton acceptor (By similarity).
 METAL 242 242 Magnesium (By similarity).
 METAL 287 287 Magnesium (By similarity).
 METAL 314 314 Magnesium (By similarity).
 BINDING 155 155 Substrate (By similarity).
 BINDING 164 164 Substrate (By similarity).
 BINDING 287 287 Substrate (By similarity).
 BINDING 314 314 Substrate (By similarity).
 BINDING 339 339 Substrate (covalent); in inhibited form.
 BINDING 390 390 Substrate (By similarity).
 MOD_RES 141 141 Phosphothreonine.
 MOD_RES 259 259 Phosphoserine.
 MOD_RES 281 281 Phosphotyrosine.
 MOD_RES 325 325 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Secreted; Sporulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 430 AA 
Protein Sequence
MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE LRDGDKDRYL 60
GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT ENKGKLGANA ILGVSMACAR 120
AAADFLQIPL YQYLGGFNSK TLPVPMMNIV NGGEHADNNV DIQEFMIMPV GAPNFREALR 180
MGAQIFHSLK SVLSAKGLNT AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA 240
MDAASSEFYN KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL 300
LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF DAIEMAKRAG 360
YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV AKYNQLLRIE DQLAETAQYH 420
GINSFYNLNK 430 
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.
 GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. 
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.