ID   ENO_ACIC1               Reviewed;         429 AA.
AC   A0LW71;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=eno; OrderedLocusNames=Acel_1909;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA   Leu D., Pujic P., Richardson P.;
RT   "Complete sequence of Acidothermus cellulolyticus 11B.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-
CC       phosphoglycerate into phosphoenolpyruvate. It is essential for the
CC       degradation of carbohydrates via glycolysis (By similarity).
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   -!- ENZYME REGULATION: The covalent binding to the substrate causes
CC       inactivation of the enzyme, and possibly serves as a signal for
CC       the export of the protein (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface.
CC       Note=Fractions of enolase are present in both the cytoplasm and on
CC       the cell surface. The export of enolase possibly depends on the
CC       covalent binding to the substrate; once secreted, it remains
CC       attached to the bacterial cell surface (By similarity).
CC   -!- SIMILARITY: Belongs to the enolase family.
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DR   EMBL; CP000481; ABK53681.1; -; Genomic_DNA.
DR   RefSeq; YP_873667.1; -.
DR   GeneID; 4485556; -.
DR   GenomeReviews; CP000481_GR; Acel_1909.
DR   KEGG; ace:Acel_1909; -.
DR   OMA; A0LW71; DIAVGTN.
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:HAMAP.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_00318; -; 1.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Phosphoprotein; Secreted.
FT   CHAIN         1    429       Enolase.
FT                                /FTId=PRO_0000280829.
FT   REGION      361    364       Substrate binding (By similarity).
FT   ACT_SITE    204    204       Proton donor (By similarity).
FT   ACT_SITE    334    334       Proton acceptor (By similarity).
FT   METAL       241    241       Magnesium (By similarity).
FT   METAL       282    282       Magnesium (By similarity).
FT   METAL       309    309       Magnesium (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
FT   BINDING     163    163       Substrate (By similarity).
FT   BINDING     282    282       Substrate (By similarity).
FT   BINDING     309    309       Substrate (By similarity).
FT   BINDING     334    334       Substrate (covalent); in inhibited form
FT                                (By similarity).
FT   BINDING     385    385       Substrate (By similarity).
FT   MOD_RES     276    276       Phosphotyrosine (By similarity).
SQ   SEQUENCE   429 AA;  45415 MW;  64B845854D47F90E CRC64;
     MAVIEAIGAR EILDSRGNPT VEVEVLLDDG TVGRAAVPSG ASTGAFEAVE KRDGDDRYGG
     KGVRQAVQAV TDQIAPEIIG FDATEQRVLD ARLIELDGTP NKSRLGANAI LGVSMAVARA
     AADSADLPLF RYLGGPNAHL LPVPMMNILN GGAHADSNVD IQEFLIAPIG AATFAEALRY
     GVETYHALKA VLKGRGLATG LGDEGGFAPN LAHNREALDL ILEAIGKAGF RPGRDIAVAI
     DAAATEFYRD GRYILEGQPR TAAELIRYYE ELVASYPLVS LEDPLAEEDW DGWRELTAAL
     GGTVQLVGDD IFVTNPERIS RGIQTSVANA VLIKLNQIGT VTETLDAVEL AHRAGYRTMI
     SHRSGETEDT TIADVAVATN AGQIKTGAPA RSERVAKYNQ LLRIEEELDD AARYAGVAAF
     PRFAGGSAG
//