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 09-JAN-2013, entry version 33. 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=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., RA Rabinowicz P.D., Tsuge S., Furutani A., Ochiai H., Delcher A.L., RA Kelley D., Madupu R., Puiu D., Radune D., Shumway M., Trapnell C., RA Aparna G., Jha G., Pandey A., Patil P.B., Ishihara H., Meyer D.F., RA Szurek B., Verdier V., Koebnik R., Dow J.M., Ryan R.P., Hirata H., RA Tsuyumu S., Won Lee S., Seo Y.-S., Sriariyanum M., Ronald P.C., RA Sonti R.V., Van Sluys M.-A., Leach J.E., 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- 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=Fractions of enolase are present in both the cytoplasm and on CC the cell surface. The export of enolase possibly depends on the CC covalent binding to the substrate; once secreted, it remains CC attached to the cell 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; CP000967; ACD58296.1; -; Genomic_DNA. DR RefSeq; YP_001912828.1; NC_010717.1. DR ProteinModelPortal; B2SUA6; -. DR SMR; B2SUA6; 2-429. DR STRING; B2SUA6; -. DR GeneID; 6305181; -. DR GenomeReviews; CP000967_GR; PXO_00171. DR KEGG; xop:PXO_00171; -. DR PATRIC; 24122692; VBIXanOry73153_1719. DR eggNOG; COG0148; -. DR HOGENOM; HOG000072174; -. DR KO; K01689; -. DR OMA; EYMIMPL; -. DR ProtClustDB; PRK00077; -. DR BioCyc; XORY360094:GI45-1654-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:InterPro. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 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; Phosphoprotein; Secreted. FT CHAIN 1 430 Enolase. FT /FTId=PRO_1000115934. FT REGION 366 369 Substrate binding (By similarity). FT ACT_SITE 207 207 Proton donor (By similarity). FT ACT_SITE 339 339 Proton acceptor (By similarity). FT METAL 244 244 Magnesium (By similarity). FT METAL 287 287 Magnesium (By similarity). FT METAL 314 314 Magnesium (By similarity). FT BINDING 157 157 Substrate (By similarity). FT BINDING 166 166 Substrate (By similarity). FT BINDING 287 287 Substrate (By similarity). FT BINDING 314 314 Substrate (By similarity). FT BINDING 339 339 Substrate (covalent); in inhibited form FT (By similarity). FT BINDING 390 390 Substrate (By similarity). FT MOD_RES 281 281 Phosphotyrosine (By similarity). 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 //