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 19-FEB-2014, entry version 58. DE RecName: Full=Enolase; DE EC=4.2.1.11; DE AltName: Full=2-phospho-D-glycerate hydro-lyase; DE AltName: Full=2-phosphoglycerate dehydratase; 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]. RC STRAIN=JS666 / ATCC BAA-500; RG US DOE Joint Genome Institute; 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 (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 (By similarity). Secreted (By CC similarity). Cell surface (By similarity). Note=Fractions of CC enolase are present in both the cytoplasm and on the cell surface. CC The export of enolase possibly depends on the covalent binding to CC the substrate; once secreted, it remains attached to the cell CC surface (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 RefSeq; YP_549996.1; NC_007948.1. DR ProteinModelPortal; Q128E4; -. DR SMR; Q128E4; 2-427. DR STRING; 296591.Bpro_3184; -. DR PRIDE; Q128E4; -. DR EnsemblBacteria; ABE45098; ABE45098; Bpro_3184. DR GeneID; 4014147; -. DR KEGG; pol:Bpro_3184; -. DR PATRIC; 22959580; VBIPolSp102244_3245. DR eggNOG; COG0148; -. DR HOGENOM; HOG000072174; -. DR KO; K01689; -. DR OMA; NLPLYRY; -. DR OrthoDB; EOG65J589; -. DR ProtClustDB; PRK00077; -. DR BioCyc; PSP296591:GHI4-3905-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR PANTHER; PTHR11902; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. 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; 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); in inhibited form FT (By similarity). FT BINDING 388 388 Substrate (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 //