ID ENO_POLSJ Reviewed; 427 AA. AC Q128E4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 24-JUL-2007, entry version 14. DE Enolase (EC 4.2.1.11) (2-phosphoglycerate dehydratase) (2-phospho-D- DE glycerate hydro-lyase). GN Name=eno; OrderedLocusNames=Bpro_3184; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I., Richardson P.; RT "Complete sequence of chromosome of Polaromonas sp. JS666."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible conversion of 2- CC phosphoglycerate into phosphoenolpyruvate. It is essential for the CC degradation of carbohydrates via glycolysis (By similarity). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing CC the dimer (By similarity). CC -!- ENZYME REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for CC the export of the protein (By similarity). CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface. CC Note=Enolase is secreted and attached to the bacterial cell CC surface. The export of enolase possibly depends on the covalent CC binding to the substrate (By similarity). CC -!- SIMILARITY: Belongs to the enolase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000316; ABE45098.1; -; Genomic_DNA. DR GenomeReviews; CP000316_GR; Bpro_3184. DR KEGG; pol:Bpro_3184; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR HAMAP; MF_00318; -; 1. DR InterPro; IPR000941; Enolase. DR PANTHER; PTHR11902; Enolase; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; KW Metal-binding; Phosphorylation; Secreted. FT CHAIN 1 427 Enolase. FT /FTId=PRO_0000267071. FT REGION 364 367 Substrate binding (By similarity). FT ACT_SITE 205 205 Proton donor (By similarity). FT ACT_SITE 337 337 Proton acceptor (By similarity). FT METAL 242 242 Magnesium (By similarity). FT METAL 285 285 Magnesium (By similarity). FT METAL 312 312 Magnesium (By similarity). FT BINDING 155 155 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 285 285 Substrate (By similarity). FT BINDING 312 312 Substrate (By similarity). FT BINDING 337 337 Substrate (covalent) (partial) (By FT similarity). FT BINDING 388 388 Substrate (By similarity). FT MOD_RES 279 279 Phosphotyrosine (By similarity). SQ SEQUENCE 427 AA; 45678 MW; C8BBCB883A426284 CRC64; MSAIVDIVGR EILDSRGNPT VECDVLLESG VMGRAAVPSG ASTGSREAIE LRDGDKSRYL GKGVLKAVEH INTEISEAVL GLDASEQAFL DRTLIDLDGT DNKSRLGANA TLAVSMAVAR AAAEEAGLPL YRYFGGSGAM QMPVPMMNVV NGGAHANNNL DLQELMIIPI GAPSFREAVR YGAEVFHALK KILHDKGMSV AVGDEGGFAP NVPSHEAAIQ MILEAIDKAG YVAGEQIALG LDCAASEFYK DGKYVLAGEG LSLDATEWTN ILATWVDKYP IISIEDGMAE GDWDGWKILT ERLGKQVQLV GDDLFVTNTK ILKEGIDKHI ANSILIKINQ IGTLTETFAA IEMAKRAGYT AVISHRSGET EDSTIADIAV GTNAGQIKTG SLSRSDRMAK YNQLLRIEED LGDIATYPGR AAFYNLR //