ID   ENO_ACICJ               Reviewed;         425 AA.
AC   A5FUW3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=Acry_0167;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
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., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ29395.1; -; Genomic_DNA.
DR   RefSeq; YP_001233314.1; -.
DR   GeneID; 5161216; -.
DR   GenomeReviews; CP000697_GR; Acry_0167.
DR   KEGG; acr:Acry_0167; -.
DR   OMA; A5FUW3; 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; Secreted.
FT   CHAIN         1    425       Enolase.
FT                                /FTId=PRO_1000019180.
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).
SQ   SEQUENCE   425 AA;  44568 MW;  CFF6116943A12737 CRC64;
     MSAIADITAR EILDSRGNPT VEVDVILDSG AMGRAAVPSG ASTGAHEAVE LRDGEPARFG
     GKGVQRAVEA VEGEIFDAIG GMDASEQVAI DETMIDLDGT PNKARLGANA ILGVSLAVAK
     AAADEIGLPL YRYLGGVYAR TLPVPMMNII NGGKHADNPI DIQEFMIQPV GAASIAEAVR
     MGSEVFQALK KILHDAGHNT NVGDEGGFAP GLKSAEEALG FMTRAVEAAG YRAGEDIAFA
     LDCAATEFYK DGRYHLEGEG KVLDAGGMTD YIAALAKSFP IISVEDPLSE DDWEGWAHFT
     STLGGAMQVV GDDLFVTNPT RLRRGIAAKS ANSILIKVNQ IGTLSETLEA VELAQRAGMT
     AVISHRSGET EDATIADIAV ATNAGQIKTG SLARSDRVAK YNQLIRIEAE LDIAGRFAGR
     TILRG
//