CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010050
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
 MPN_606; MP236 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
54SGASTGEKEAIELRDacetylation[1]
70DPKAYFGKGVSQAVQacetylation[1]
140AQKTSLFKYLANQVMacetylation[1]
205ETFHALQKLLKQRGLacetylation[1]
362ATNSILIKLNQIGTLacetylation[1]
425SRSERIAKYNRLLQIacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
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 389 392 Substrate binding (By similarity).
 ACT_SITE 219 219 Proton donor (By similarity).
 ACT_SITE 362 362 Proton acceptor (By similarity).
 METAL 256 256 Magnesium (By similarity).
 METAL 310 310 Magnesium (By similarity).
 METAL 337 337 Magnesium (By similarity).
 BINDING 169 169 Substrate (By similarity).
 BINDING 178 178 Substrate (By similarity).
 BINDING 310 310 Substrate (By similarity).
 BINDING 337 337 Substrate (By similarity).
 BINDING 362 362 Substrate (covalent); in inhibited form
 BINDING 413 413 Substrate (By similarity).
 MOD_RES 304 304 Phosphotyrosine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MSAQTGTDLF KIADLFAYQV FDSRGFPTVA CVVKLASGHT GEAMVPSGAS TGEKEAIELR 60
DGDPKAYFGK GVSQAVQNVN QTIAPKLIGL NATDQAAIDA LMIQLDGTPN KAKLGANAIL 120
AVSLAVAKAA ASAQKTSLFK YLANQVMGLN KTEFILTVPM LNVINGGAHA DNNIDFQEFM 180
IMPLGANSMH QALKMASETF HALQKLLKQR GLNTNKGDEG GFAPNLKLAE EALDLMVEAI 240
KAAGYQPGSD IAIALDVAAS EFYDDTTKRY VFKKGIKAKI LDEKEWSLTT AQMIAYLKKL 300
TEQYPIISIE DGLSEHDWEG METLTKTLGQ HIQIVGDDLY CTNPAIAEKG VAHKATNSIL 360
IKLNQIGTLT ETIKAINIAK DANWSQVISH RSGETEDTTI ADLAVAACTG QIKTGSMSRS 420
ERIAKYNRLL QIELELGNNA KYLGWNTFKN IKPQKA 456 
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.