CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015039
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
 RPA2874 
Created Date
 July 27, 2013 
Organism
 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 
NCBI Taxa ID
 258594 
Lysine Modification
Position
Peptide
Type
References
424YAGKAALKALR****acetylation[1]
Reference
 [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.
 Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC.
 J Biol Chem. 2012 May 4;287(19):15590-601. [PMID: 22416131
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 364 367 Substrate binding (By similarity).
 ACT_SITE 205 205 Proton donor (By similarity).
 ACT_SITE 337 337 Proton acceptor (By similarity).
 METAL 242 242 Magnesium (By similarity).
 METAL 285 285 Magnesium (By similarity).
 METAL 312 312 Magnesium (By similarity).
 BINDING 155 155 Substrate (By similarity).
 BINDING 164 164 Substrate (By similarity).
 BINDING 285 285 Substrate (By similarity).
 BINDING 312 312 Substrate (By similarity).
 BINDING 337 337 Substrate (covalent); in inhibited form
 BINDING 388 388 Substrate (By similarity).
 MOD_RES 279 279 Phosphotyrosine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 427 AA 
Protein Sequence
MTAIVDIIGR EILDSRGNPT VEVDVVLEDG SVGRAAVPSG ASTGAHEAVE LRDGDKARYL 60
GKGVQKAVEA VNGELFDALG GMDAEQQVQI DQTMIELDGT PNKGRIGANA ILGVSLAAAK 120
AAAASYDMPL YRYVGGTSAR TLPVPMMNIV NGGVHADNPI DFQEFMIMPV GAPTFADALR 180
CGSEIFHTLK GELKKAGHNT NVGDEGGFAP NLPSADAALD FVMAAIGKAG YKAGGDVMLA 240
LDCAATEFFK DGSYVYGGEN KTRSRSEQAK YLADLVARYP IVSIEDGMSE DDMDGWKELT 300
DLIGSKCQLV GDDLFVTNVT RLADGIKNGR ANSILIKVNQ IGTLTETLAA VEMAHKAGYT 360
AVMSHRSGET EDSTIADLAV ATNCGQIKTG SLARADRTAK YNQLLRIEQE LGAHAHYAGK 420
AALKALR 427 
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.