ID ENO_STRR6 Reviewed; 434 AA. AC Q8DPS0; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 04-NOV-2026, 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=spr1036; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). RN [2] RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20453092; DOI=10.1128/jb.01564-09; RA Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L., Weiser J., RA Branny P.; RT "Identification of multiple substrates of the StkP Ser/Thr protein kinase RT in Streptococcus pneumoniae."; RL J. Bacteriol. 192:3629-3638(2010). 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 -!- PTM: Phosphorylated on Thr residue(s). This phosphorylation is not CC StkP-dependent. {ECO:0000269|PubMed:20453092}. 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; AE007317; AAK99840.1; -; Genomic_DNA. DR PIR; D98001; D98001. DR RefSeq; WP_000022815.1; NC_003098.1. DR AlphaFoldDB; Q8DPS0; -. DR SMR; Q8DPS0; -. DR STRING; 171101.spr1036; -. DR PaxDb; 171101-spr1036; -. DR KEGG; spr:spr1036; -. DR PATRIC; fig|171101.6.peg.1124; -. DR eggNOG; COG0148; Bacteria. DR HOGENOM; CLU_031223_2_1_9; -. DR OMA; AACLRQC; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:UniProtKB-ARBA. 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; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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 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 1: Evidence at protein level; KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome; KW Secreted; Virulence. FT CHAIN 1..434 FT /note="Enolase" FT /id="PRO_0000133981" FT ACT_SITE 205 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 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 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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 343 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 372 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 373 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" FT BINDING 394 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318" SQ SEQUENCE 434 AA; 47103 MW; 3E85FCA26DC8BC96 CRC64; MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFLG FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV AEYRGLKSFY NLKK //