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   16-JUN-2009, entry version 53.
DE   RecName: Full=Enolase 1;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=ENL-1;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Archamoebae; Entamoebidae; Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=HM-1:IMSS;
RX   MEDLINE=95240662; 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: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the enolase family.
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DR   EMBL; U09736; AAA80166.1; -; mRNA.
DR   HSSP; Q9NDH8; 1OEP.
DR   BRENDA; 4.2.1.11; 323.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   PANTHER; PTHR11902; Enolase; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   ProDom; PD000902; Enolase; 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       Enolase 1.
FT                                /FTId=PRO_0000134080.
FT   REGION      374    377       Substrate binding (By similarity).
FT   ACT_SITE    208    208       Proton donor (By similarity).
FT   ACT_SITE    347    347       Proton acceptor (By similarity).
FT   METAL       243    243       Magnesium (By similarity).
FT   METAL       296    296       Magnesium (By similarity).
FT   METAL       322    322       Magnesium (By similarity).
FT   BINDING     156    156       Substrate (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     322    322       Substrate (By similarity).
FT   BINDING     398    398       Substrate (By similarity).
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
//