ID   ENO_MYCUA               Reviewed;         428 AA.
AC   A0PW55;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-NOV-2008, entry version 20.
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=MUL_4631;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
RA   Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
RA   Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL06574.1; -; Genomic_DNA.
DR   RefSeq; YP_908045.1; -.
DR   GeneID; 4550802; -.
DR   GenomeReviews; CP000325_GR; MUL_4631.
DR   KEGG; mul:MUL_4631; -.
DR   BuruList; MUL_4631; -.
DR   GO; GO:0009986; C:cell surface; IEA:HAMAP.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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    428       Enolase.
FT                                /FTId=PRO_0000280866.
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   428 AA;  44736 MW;  58A29D49E5EBF57F CRC64;
     MPIIEQVGAR EILDSRGNPT VEVEVALIDG TFARAAVPSG ASTGEHEAVE LRDGGDRYGG
     KGVKKAVEAV LDEIGPAVIG LNADDQRLVD QALVDLDGTP DKSRLGGNSI LGVSLAVAKA
     ASESAELPLF RYIGGPNAHI LPVPMMNILN GGAHADTGVD IQEFMVAPIG APSFSEALRW
     GAEVYHALKA VLKKAGLSTG LGDEGGFAPD VASTTAALDL ISQAIEAAGF KPGVDVALAL
     DAAANEFHAD GSYTFEGTPR TAAQMTEFYA GLLGSYPVVS IEDPLYENDW DGWAALTAEI
     GDRVQIVGDD VFVTNPERLE EGIDRGVANA LLVKVNQIGT LTETLDAVAL AHHSGYRTMI
     SHRSGETEDT IIADLAVAVG SGQIKTGAPA RSERVAKYNQ LLRIEEALGD AARYAGDLAF
     PRFVADPK
//