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 12-AUG-2020, entry version 93. DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=Bpro_3184; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas; unclassified Polaromonas. OX NCBI_TaxID=296591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500; RX PubMed=18723656; DOI=10.1128/aem.00197-08; RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S., RA Stothard P., Coleman N.V.; RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of RT relevance to biotechnology."; RL Appl. Environ. Microbiol. 74:6405-6416(2008). CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate CC into phosphoenolpyruvate. It is essential for the degradation of CC carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00318}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; CC -!- ACTIVITY REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for the CC export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. The export of CC enolase possibly depends on the covalent binding to the substrate; once CC secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP- CC Rule:MF_00318}. 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; WP_011484093.1; NC_007948.1. DR SMR; Q128E4; -. DR STRING; 296591.Bpro_3184; -. DR PRIDE; Q128E4; -. DR EnsemblBacteria; ABE45098; ABE45098; Bpro_3184. DR KEGG; pol:Bpro_3184; -. DR eggNOG; COG0148; Bacteria. DR HOGENOM; CLU_031223_2_1_4; -. DR KO; K01689; -. DR OMA; GPELVGY; -. DR OrthoDB; 533698at2; -. DR BioCyc; PSP296591:G1G6E-3225-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000001983; Chromosome. 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-UniRule. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd03313; enolase; 1. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. 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 SFLD; SFLDG00178; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome; KW Secreted. FT CHAIN 1..427 FT /note="Enolase" FT /id="PRO_0000267071" FT REGION 364..367 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 205 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 337 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 242 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 285 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 312 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 155 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 164 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 285 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 312 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 337 FT /note="Substrate (covalent); in inhibited form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 388 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" 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 //