ID ENO_PARC0 Reviewed; 428 AA. AC A1TLS5; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 04-NOV-2026, entry version 108. 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}; GN OrderedLocusNames=Aave_1322; OS Paracidovorax citrulli (strain AAC00-1) (Acidovorax citrulli). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Comamonadaceae; Paracidovorax. OX NCBI_TaxID=397945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.; RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2- CC PG) into phosphoenolpyruvate (PEP). It is essential for the degradation CC of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00318}; CC Note=Binds a second Mg(2+) ion via substrate during catalysis. CC {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. CC {ECO:0000255|HAMAP-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; CP000512; ABM31913.1; -; Genomic_DNA. DR RefSeq; WP_011794465.1; NC_008752.1. DR SMR; A1TLS5; -. DR STRING; 397945.Aave_1322; -. DR GeneID; 79790985; -. DR KEGG; aav:Aave_1322; -. DR eggNOG; COG0148; Bacteria. DR HOGENOM; CLU_031223_2_1_4; -. DR OMA; AACLRQC; -. DR OrthoDB; 9804716at2; -. DR UniPathway; UPA00109; UER00187. DR CDD; cd03313; enolase; 1. DR FunFam; 3.20.20.120:FF:000001; Enolase; 1. DR FunFam; 3.30.390.10:FF:000001; Enolase; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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; ENOLASE; 1. DR PANTHER; PTHR11902:SF1; ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SFLD; SFLDS00001; Enolase; 1. DR SFLD; SFLDF00002; enolase; 1. DR SFLD; SFLDG00178; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR NCBIfam; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. 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 AlphaFoldDB; A1TLS5; -. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Secreted. FT CHAIN 1..428 FT /note="Enolase" FT /id="PRO_0000280830" FT ACT_SITE 205 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 338 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 163 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 286 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 338 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 367 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 368 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 389 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 428 AA; 45853 MW; AC94EBFC0B4B07C2 CRC64; MSAIVDIVGR EVLDSRGNPT VECDVLLESG VMGRAAVPSG ASTGSREAIE LRDGDKSRYL GKGVLKAVEH INTEISEAVL GLDASEQAFL DKTLIDLDGT DNKSRLGANA MLAVSMAVAR AAAEESGLPL YRYLGGMGGL QLPVPMMNVI NGGAHANNSL DLQEFMIIPV GAPSFREAVR WGAEVFHALK KIINDKGMST AVGDEGGFAP SVENHEAAIQ LILQAIDAAG YTAGEQIALG LDCAASEFYK DGHYVLEGEG GIRLTAQQWT DMLATWVDKY PIISIEDGMA EGDWDGWKHL TERLGKNVQL VGDDLFVTNT RILKEGIDKD IGNSILIKIN QIGTLTETFA AIEMAKRAGY TAVISHRSGE TEDSTIADIA VGTNAGQIKT GSLSRSDRIA KYNQLLRIEE DLGDIAHYPG RAAFYNLR //