ID ENO_BUCAI Reviewed; 434 AA. AC P57492; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 141. 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=BU417; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; Evidence={ECO:0000255|HAMAP- CC 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; BA000003; BAB13115.1; -; Genomic_DNA. DR RefSeq; NP_240229.1; NC_002528.1. DR RefSeq; WP_010896105.1; NC_002528.1. DR AlphaFoldDB; P57492; -. DR SMR; P57492; -. DR STRING; 563178.BUAP5A_410; -. DR EnsemblBacteria; BAB13115; BAB13115; BAB13115. DR KEGG; buc:BU417; -. DR PATRIC; fig|107806.10.peg.426; -. DR eggNOG; COG0148; Bacteria. DR HOGENOM; CLU_031223_2_1_6; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000001806; 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; 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 NCBIfam; TIGR01060; eno; 1. 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 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 PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome; KW Secreted. FT CHAIN 1..434 FT /note="Enolase" FT /id="PRO_0000133855" FT ACT_SITE 209 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 343 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 318 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 343 FT /ligand="substrate" FT /note="covalent; in inhibited form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 370..373 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 394 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 434 AA; 47428 MW; D3F5FD25D8F52D40 CRC64; MSKITKIIAR EIIDSRGNPT VESEVHLEGG FVGLASSPSG ASTGSLEALE LRDENKDRFM GKGVEKAVSL INEKISIALK NKNARNQSDI DHIMIDLDGT INKSKLGANA ILSVSLAVAK AAAASKRMPL YAHIAEINET PGVFSMPLPM INIINGGKHA NNNIDIQEFM IQPISAKTVK ESIRIGCEIF HALGELLKEK GMSTTVGDEG GYAPNLKSNE EALNIIQDAI QKTKYKLGQD IRLAIDCAAS ELYNKNEKKY NLKGENISFS SKEFTHYLEK LSQKYPIVSI EDGQDESDWE GFLYQTHVLG NKIQLVGDDL FVTNKNILKK GIKKGIANSI LIKLNQIGTL TETLEAIKTA KQANYGVIIS HRSGETEDAS IADLSVGTSS GQIKTGSMSR SDRTSKYNQL IRIEENLGTK YAPFHGLREI KSAF //