ID ENO_HELPY Reviewed; 426 AA. AC P48285; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 158. 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=HP_0154; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178. RC STRAIN=ATCC 53726 / 84-183; RX PubMed=7768597; DOI=10.1128/iai.63.6.2185-2193.1995; RA Thompson S.A., Blaser M.J.; RT "Isolation of the Helicobacter pylori recA gene and involvement of the recA RT region in resistance to low pH."; RL Infect. Immun. 63:2185-2193(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68. RC STRAIN=69A; RX PubMed=7476856; DOI=10.1007/bf02423452; RA Schmitt W., Odenbreit S., Heuermann D., Haas R.; RT "Cloning of the Helicobacter pylori recA gene and functional RT characterization of its product."; RL Mol. Gen. Genet. 248:563-572(1995). 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; AE000511; AAD07219.1; -; Genomic_DNA. DR EMBL; U13756; AAC43380.1; -; Genomic_DNA. DR EMBL; Z35478; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B64539; S58684. DR RefSeq; WP_000955673.1; NC_018939.1. DR AlphaFoldDB; P48285; -. DR SMR; P48285; -. DR DIP; DIP-3344N; -. DR FunCoup; P48285; 341. DR IntAct; P48285; 4. DR MINT; P48285; -. DR STRING; 85962.HP_0154; -. DR PaxDb; 85962-HP_0154; -. DR EnsemblBacteria; AAD07219; AAD07219; HP_0154. DR KEGG; heo:C694_00770; -. DR KEGG; hpy:HP_0154; -. DR PATRIC; fig|85962.47.peg.167; -. DR eggNOG; COG0148; Bacteria. DR InParanoid; P48285; -. DR OrthoDB; 9804716at2; -. DR PhylomeDB; P48285; -. DR BRENDA; 4.2.1.11; 2604. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000429; 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; IBA:GO_Central. 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; IBA:GO_Central. 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 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 PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome; KW Secreted. FT CHAIN 1..426 FT /note="Enolase" FT /id="PRO_0000133897" 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" FT CONFLICT 26 FT /note="V -> I (in Ref. 3; Z35478 and 2; AAC43380)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="I -> T (in Ref. 2; AAC43380)" FT /evidence="ECO:0000305" SQ SEQUENCE 426 AA; 46534 MW; 7B7A0B87A5DFB398 CRC64; MLTIKDIHAL EVMDSRGNPT IQASVVLSDN TKASAIVPSG ASTGKREALE LRDNDKTRFL GKGVLRACEN VNSVIKHHLI GLEAINQAFV DERLRALDGT PNYANLGANA VLGVSMALAR ASAKALNLPL YRYLGGANAL TLPVPMLNII NGGTHANNSI DFQEYMIMPL GFESFKEALR ASAEVYHTLK KLLDGKNQLT SVGDEGGFAP NFSNNVEPLE VISQAIEKAG YKLGEEIALA LDVASSELVD ENFNYHLKGE NKILDSHELV AYYKELVAKY PIVSIEDGLS EDDWEGWAFL SKELGRQIQL VGDDLFVTNA SLLQKGIEKN IANAVLIKPN QIGTISETLE TIRLAKHHAY QCVMSHRSGE SEDSFIADFA VALNTGEIKT GSTARSERIA KYNRLLEIEH ELKGGIYIGK ELFKHG //