ID   ENO_ALHEH               Reviewed;         429 AA.
AC   Q0A7K4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Mlg_1839;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI57183.1; -; Genomic_DNA.
DR   RefSeq; YP_742673.1; -.
DR   GeneID; 4269207; -.
DR   GenomeReviews; CP000453_GR; Mlg_1839.
DR   KEGG; aeh:Mlg_1839; -.
DR   NMPDR; fig|187272.6.peg.1750; -.
DR   HOGENOM; Q0A7K4; -.
DR   OMA; Q0A7K4; 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_0000266993.
FT   REGION      364    367       Substrate binding (By similarity).
FT   ACT_SITE    205    205       Proton donor (By similarity).
FT   ACT_SITE    337    337       Proton acceptor (By similarity).
FT   METAL       242    242       Magnesium (By similarity).
FT   METAL       285    285       Magnesium (By similarity).
FT   METAL       312    312       Magnesium (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     164    164       Substrate (By similarity).
FT   BINDING     285    285       Substrate (By similarity).
FT   BINDING     312    312       Substrate (By similarity).
FT   BINDING     337    337       Substrate (covalent); in inhibited form
FT                                (By similarity).
FT   BINDING     388    388       Substrate (By similarity).
FT   MOD_RES     279    279       Phosphotyrosine (By similarity).
SQ   SEQUENCE   429 AA;  46083 MW;  65E5BA96EBF84536 CRC64;
     MGTIKQIKAR EILDSRGNPT VEADVILDSG VMGRAAVPSG ASTGTREAVE LRDGDAGRYL
     GKGVRKAVEN VNTVIADALC GMDASGQRAL DDRMRELDGT DNKGKLGANA LLAVSLAAAR
     ATAAERGQSL FRYLNPEGPW SLPVPMMNIL NGGEHADNSV DIQEFMVMPT GFDRFSEALR
     CGTEIFHALK KVLQDRGLNT GVGDEGGFAP DLPSNEAALE VILEAIDRAG YKAGENVWLA
     LDAASSEFYQ DGVYRLASEG REFSAEAFAD YLADLCARYP ILSIEDGMDE SDWVGWKALT
     DKLGDRVQLV GDDLFVTNTR ILKRGIDEGV GNSILIKFNQ IGTLSETLDA IAMAHEAGFT
     SVVSHRSGET EDTTIADLAV ATTATQIKTG SLSRSDRVAK YNQLLRIEEE LGEQADYPGL
     AAFPQLRRG
//