ENO_ENTHR
ID ENO_ENTHR Reviewed; 432 AA.
AC Q8GR70;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
OS Enterococcus hirae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN
RP COMPLEX WITH MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX PubMed=12869539; DOI=10.1093/jb/mvg104;
RA Hosaka T., Meguro T., Yamato I., Shirakihara Y.;
RT "Crystal structure of Enterococcus hirae enolase at 2.8 A resolution.";
RL J. Biochem. 133:817-823(2003).
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:12869539};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:12869539};
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: Homodimer. {ECO:0000269|PubMed:12869539}.
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; AB091345; BAC16223.1; -; Genomic_DNA.
DR PDB; 1IYX; X-ray; 2.80 A; A/B=1-432.
DR PDBsum; 1IYX; -.
DR AlphaFoldDB; Q8GR70; -.
DR SMR; Q8GR70; -.
DR STRING; 1354.A6P53_09325; -.
DR PRIDE; Q8GR70; -.
DR BRENDA; 4.2.1.11; 2097.
DR UniPathway; UPA00109; UER00187.
DR EvolutionaryTrace; Q8GR70; -.
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; -; 1.
DR Gene3D; 3.30.390.10; -; 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; PTHR11902; 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 SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Secreted.
FT CHAIN 1..432
FT /note="Enolase"
FT /id="PRO_0000133886"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 340
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 367..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 175..196
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:1IYX"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1IYX"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 398..414
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:1IYX"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:1IYX"
SQ SEQUENCE 432 AA; 46411 MW; 45F203F55685F1C1 CRC64;
MSIITDVYAR EILDSRGNPT IEVEVYTESG AFGRGMVPSG ASTGEYEAVE LRDGDKARYG
GKGVTKAVDN VNNIIAEAII GYDVRDQMAI DKAMIALDGT PNKGKLGANA ILGVSIAVAR
AAADYLEVPL YHYLGGFNTK VLPTPMMNII NGGSHADNSI DFQEFMIMPV GAPTFKEALR
MGAEVFHALA AILKSRGLAT SVGDEGGFAP NLGSNEEGFE VIIEAIEKAG YVPGKDVVLA
MDAASSEFYD KEKGVYVLAD SGEGEKTTDE MIKFYEELVS KYPIISIEDG LDENDWDGFK
KLTDVLGDKV QLVGDDLFVT NTQKLSEGIE KGIANSILIK VNQIGTLTET FEAIEMAKEA
GYTAVVSHRS GETEDSTISD IAVATNAGQI KTGSLSRTDR IAKYNQLLRI EDQLGEVAEY
KGLKSFYNLK AA
