ID ENO_BRUA2 Reviewed; 425 AA. AC Q2YPV0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 110. 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=BAB1_1155; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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 -!- 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; AM040264; CAJ11111.1; -; Genomic_DNA. DR RefSeq; WP_002964261.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YPV0; -. DR SMR; Q2YPV0; -. DR STRING; 359391.BAB1_1155; -. DR GeneID; 55590816; -. DR KEGG; bmf:BAB1_1155; -. DR PATRIC; fig|359391.11.peg.54; -. DR HOGENOM; CLU_031223_2_1_5; -. DR PhylomeDB; Q2YPV0; -. DR BRENDA; 4.2.1.11; 994. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000002719; Chromosome I. 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; 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..425 FT /note="Enolase" FT /id="PRO_0000267006" FT ACT_SITE 204 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT ACT_SITE 336 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 284 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 311 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 311 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 336 FT /ligand="substrate" FT /note="covalent; in inhibited form" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 363..366 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 387 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 425 AA; 45261 MW; A148573BD4696545 CRC64; MTAIIDIVGR EILDSRGNPT VEVDVVLEDG SFGRAAVPSG ASTGAHEAVE LRDGGSRYLG KGVEKAVEVV NGKIFDAIAG MDAESQLLID QTLIDLDGSA NKGNLGANAI LGVSLAVAKA AAQASGLPLY RYVGGTNAHV LPVPMMNIIN GGAHADNPID FQEFMILPVG ATSIREAVRY GSEVFHTLKK RLKDAGHNTN VGDEGGFAPN LKNAQAALDF IMESIEKAGF KPGEDIALGL DCAATEFFKD GNYVYEGERK TRDPKAQAKY LAKLASDYPI VTIEDGMAED DWEGWKYLTD LIGNKCQLVG DDLFVTNSAR LRDGIRLGVA NSILVKVNQI GSLSETLDAV ETAHKAGYTA VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRTAKY NQLIRIEEEL GKQARYAGRS ALKLL //