ID ENO_XANOP Reviewed; 430 AA. AC B2SUA6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 26-FEB-2020, entry version 74. 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=PXO_00171; OS Xanthomonas oryzae pv. oryzae (strain PXO99A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=360094; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PXO99A; RX PubMed=18452608; DOI=10.1186/1471-2164-9-204; RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D., RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R., RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A., RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R., RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S., RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E., RA White F.F., Bogdanove A.J.; RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas RT oryzae pv. oryzae PXO99A."; RL BMC Genomics 9:204-204(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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. CC {ECO:0000255|HAMAP-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; CP000967; ACD58296.1; -; Genomic_DNA. DR RefSeq; WP_011408895.1; NC_010717.2. DR SMR; B2SUA6; -. DR STRING; 360094.PXO_00171; -. DR EnsemblBacteria; ACD58296; ACD58296; PXO_00171. DR GeneID; 34179118; -. DR KEGG; xop:PXO_00171; -. DR HOGENOM; CLU_031223_2_1_6; -. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; 533698at2; -. DR BioCyc; XORY360094:G1GBE-1645-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000001740; 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 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; Secreted. FT CHAIN 1..430 FT /note="Enolase" FT /id="PRO_1000115934" FT REGION 366..369 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 207 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 244 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 287 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT METAL 314 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 157 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 166 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 287 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 314 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 339 FT /note="Substrate (covalent); in inhibited form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 390 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 430 AA; 46015 MW; DD2FA4CF68FA21A1 CRC64; MTTIAKILAR EILDSRGNPT LEAEVTLDDG SFGRAAVPSG ASTGTKEAVE LRDGDKTRYL GKGVRHAVDN VNGTIAETLK NFDAADQQGL DRRLIDLDGT ENKGRLGANA LLGVSLAAAH AVAASRKQPL WQYLSTITES DVALPVPMMN IINGGAHADN NVDFQEFMVL PVGCSSFSEA LRAGTEIFYS LKSVLKGHGL STAVGDEGGF APDFRSNVEA LDTILEAIGK AGYTAGEDIL LGLDVASSEF YDNGKYNLVG ENKRLTSEQF VDFLADWVAQ YPIISIEDGL AEDDWAGWKL LTDRVGKHVQ LVGDDLFVTN PKIFKQGIDS GTANAILIKV NQIGTLTETL EAIAMAHAAN YASIVSHRSG ETEDTTIADI AVATTATQIK TGSLCRSDRV AKYNQLLRIE QALGSDARYA GRDAFVSIKR //