ID   ENO_CUNEL               Reviewed;         436 AA.
AC   O74286;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   Flags: Fragment;
OS   Cunninghamella elegans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Cunninghamella.
OX   NCBI_TaxID=4853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 36112 / DSM 8217 / PA-1;
RX   AGRICOLA=IND22048504;
RA   Wang R.F., Khan A.F., Cao W.W., Cerniglia C.E.;
RT   "Cloning, sequencing, and expression of the gene encoding enolase from a
RT   fungus, Cunninghamella elegans.";
RL   Mycol. Res. 104:175-179(2000).
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC       {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; Y17298; CAA76735.1; -; mRNA.
DR   AlphaFoldDB; O74286; -.
DR   SMR; O74286; -.
DR   PRIDE; O74286; -.
DR   UniPathway; UPA00109; UER00187.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           <1..436
FT                   /note="Enolase"
FT                   /id="PRO_0000134048"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   436 AA;  46878 MW;  32BA0B8E5C801738 CRC64;
     STITKVHARQ IFDSRGNPTV EVEVTTDKGV FRAGVPSGAS TGVHEALELR DGVKSDYLGK
     GVLKAVGNVN TIINEELVKA NLSVVDQKAV DDFLIQLDGT ENKEKLGANA ILGVSLAVAK
     AGAAEKGVPF YVHIADLAGS KKPFVLPVPA FNVINGGSHA GNKLAMQEFM IMPTGAKSFS
     EAMKLGSEVY HTLKKVINEK YGQDATNVGD EGGFAPNIQD NQEGLELLVT AIEKAGYTGK
     IKVAMDCAAS DFYKDGKYDL DFKNPNSDPS TYLTGQDLTD LYNSYAGKYP IVSIEDAFDQ
     DDWENWAHMN ASADYQLVGD DLTVTNPKRI ATAVEKKACN ALLLKVNQIG TLTESIQAAL
     DSQKAGWGVM VSHRSGETED TSIASIVVGL RTGQIKTGAP CRSERLAKYN ELLRIEEELG
     DAAIYAGEHF RKAHDL