ENO1_ENTHI
ID ENO1_ENTHI Reviewed; 436 AA.
AC P51555;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Enolase 1;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=ENL-1;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=7723780; DOI=10.1016/0166-6851(94)00201-w;
RA Beanan M.J., Bailey G.B.;
RT "The primary structure of an Entamoeba histolytica enolase.";
RL Mol. Biochem. Parasitol. 69:119-121(1995).
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.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; U09736; AAA80166.1; -; mRNA.
DR PDB; 3QTP; X-ray; 1.90 A; A/B=1-436.
DR PDBsum; 3QTP; -.
DR AlphaFoldDB; P51555; -.
DR SMR; P51555; -.
DR STRING; 5759.rna_EHI_130700-1; -.
DR PRIDE; P51555; -.
DR VEuPathDB; AmoebaDB:EHI5A_036590; -.
DR VEuPathDB; AmoebaDB:EHI7A_041120; -.
DR VEuPathDB; AmoebaDB:EHI8A_039740; -.
DR VEuPathDB; AmoebaDB:EHI_130700; -.
DR VEuPathDB; AmoebaDB:KM1_070570; -.
DR eggNOG; KOG2670; Eukaryota.
DR OMA; EFMIIPV; -.
DR SABIO-RK; P51555; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..436
FT /note="Enolase 1"
FT /id="PRO_0000134080"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374..377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 106..123
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 176..198
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:3QTP"
FT TURN 323..327
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:3QTP"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:3QTP"
FT HELIX 405..421
FT /evidence="ECO:0007829|PDB:3QTP"
SQ SEQUENCE 436 AA; 47327 MW; BFBA693A65B44289 CRC64;
MSIQKVHARE ILDSRGNPTI EVEITTGKGM FRSCVPSGAS TGVHEAVELR DGDKKRYGGK
GVLKAVENVN TIIGPALLGK NVLNQAELDE MMIKLDGTNN KGKLGANAIL GCSMSICRAA
AAEKGLPLYK YLAELTGHKE MTMPVPCFNV INGGAHAGNA LAMQEFMICP TGATNFHEAL
RMAAETYQCL KVVIKAKYGQ DATNVGDEGG FAPNVSGARE ALDLLVEAIA KAGYTGKIEI
AMDCAASEFY NEETKKYDLG KKIPADKKDP SLVKDVDGLI AEYVDYGKHY PIASIEDPFA
EDDWAAWNKF TVEHGNFQIV GDDLLVTNPA RVQMAMDKNA CNSVLIKVNQ IGTLTETFKT
IKMAQEKGWG VMASHRSGET EDTFIADLVV GLNCKQIKTG APCRSERLCK YNQLMRIEEE
LGNIPYAGKN WRNSTA
