ID   ENO1_LACPL              Reviewed;         442 AA.
AC   Q88YH3;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 48.
DE   RecName: Full=Enolase 1;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase 1;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
GN   Name=eno1; Synonyms=enoA, enoA1; OrderedLocusNames=lp_0792;
OS   Lactobacillus plantarum.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA   Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA   Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA   Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA   De Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
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; AL935254; CAD63380.1; -; Genomic_DNA.
DR   RefSeq; NP_784537.1; -.
DR   HSSP; Q9NDH8; 1OEP.
DR   SMR; Q88YH3; 2-434.
DR   GeneID; 1063808; -.
DR   GenomeReviews; AL935263_GR; lp_0792.
DR   KEGG; lpl:lp_0792; -.
DR   NMPDR; fig|220668.1.peg.671; -.
DR   HOGENOM; Q88YH3; -.
DR   BioCyc; LPLA220668:LP_0792-MON; -.
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    442       Enolase 1.
FT                                /FTId=PRO_0000133906.
FT   REGION      369    372       Substrate binding (By similarity).
FT   ACT_SITE    205    205       Proton donor (By similarity).
FT   ACT_SITE    342    342       Proton acceptor (By similarity).
FT   METAL       242    242       Magnesium (By similarity).
FT   METAL       290    290       Magnesium (By similarity).
FT   METAL       317    317       Magnesium (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     164    164       Substrate (By similarity).
FT   BINDING     290    290       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
FT   BINDING     342    342       Substrate (covalent); in inhibited form
FT                                (By similarity).
FT   BINDING     393    393       Substrate (By similarity).
FT   MOD_RES     284    284       Phosphotyrosine (By similarity).
SQ   SEQUENCE   442 AA;  48030 MW;  B4FD3E75AA7359D4 CRC64;
     MSIITDIYAR EVLDSRGNPT VEVELYTESG AFGRGIVPSG ASTGEHEAVE LRDGDKSRFM
     GKGVTKAVDN VNKLIAKEIV GYDVTDQRAI DQAMIKLDGT PNKAKLGANA ILGVSIAAAR
     AAADELEMPL YNYLGGFNAH VLPTPMMNVI NGGAHANNDV DFQEFMIMPV GASSVKEAIR
     MGSETFHNLK AILNERGYST AVGDEGGFAP DLKNNEEPFE ILVEAIERAG YKPGKDIAIA
     FDCAASEFYN EETGKYDLKG EGENGQSFTA EEFVDLLDSI VDKYPIVSIE DPLDENNWED
     WQMATAKLGK KVQIVGDDLF VTNTDYLAKG IKMGVANSIL IKVNQIGTLT ETVEAIEMAK
     EAGYTAIVSH RSGETEDTTI ADLVVAMNAG QIKTGSMSRT ERIAKYNQLM RIEDQLESTS
     EYKGIHGFYN LDEAARNTIT SK
//